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DP01065 - Probable ATP-dependent RNA helicase DDX4

Organism Homo sapiens
Gene DDX4 (VASA)
Sequence length 724
Disorder content 32.6%
Isoform entries DP01066 (Q9NQI0-2)
Cross references UniProtKB:Q9NQI0, MobiDB:Q9NQI0
Dataset(s) Condensates-related proteins
Last update 2022-02-14
Entry history
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70140210280350420490560630700DisProt consensusStructural stateMolecular function
Example filters structural state transition interaction partner disorder function magnetic resonance
Selected regions 2 / 2
DP01065r004 Structural state
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Term disorder, IDPO:00076
Fragment 1 - 236
Evidence nuclear magnetic resonance spectroscopy evidence used in manual assertion, ECO:0006165
Reference Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles. Nott TJ, Petsalaki E, Farber P, Jervis D, Fussner E, Plochowietz A, Craggs TD, Bazett-Jones DP, Pawson T, Forman-Kay JD, Baldwin AJ. Mol Cell, 2015, pmid:25747659
Statements Results "The narrow range of amide proton chemical shifts observed in a 1H/15N HSQC spectra of the two proteins (Figure S5A) confirmed that they are intrinsically disordered." Introduction "Here, we demonstrate that human Ddx4 and its isolated disordered N terminus spontaneously self-associate both in cells and in vitro into structures that are indistinguishable from the cellular Ddx4-organelles."
Curator Edoardo Salladini
validated by Victoria Nugnes
DP01065r005 Molecular function
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Term molecular condensate scaffold activity, GO:0140693
Fragment 1 - 236
Evidence spectrometry evidence used in manual assertion, ECO:0007731
Reference Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles. Nott TJ, Petsalaki E, Farber P, Jervis D, Fussner E, Plochowietz A, Craggs TD, Bazett-Jones DP, Pawson T, Forman-Kay JD, Baldwin AJ. Mol Cell, 2015, pmid:25747659
Statements Introduction "Here, we demonstrate that human Ddx4 and its isolated disordered N terminus spontaneously self-associate both in cells and in vitro into structures that are indistinguishable from the cellular Ddx4-organelles." Results "The organelles are clearly partitioned from surrounding nuclear structures including chromatin domains and other native nuclear bodies (Figures 1C and S2B), a finding consistent with the liquid droplet-like nature suggested by FRAP measurements (Figure 2A)." Results "These data reveal that the disordered termini of Ddx4 mediate self-organization into macroscopic fluxional spherical structures in live cells that can be classified as organelles, which can respond rapidly to changes in the cellular environment."
Curator Edoardo Salladini
validated by Victoria Nugnes
BioComputing UP, 2021 - University of Padua, Italy
License and disclaimer
This database is part of a project that has received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 778247.
University of Padua
Department of Biomedical Sciences
ELIXIR Europe
IDPfun
Non-globular proteins - COST Action BM1405