Oncofusion

start / graph / protein-ddx10-domains

Proteinestablished confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.Qn-nup98-family

DDX10 domain architecture (UniProt Q13206)

also called DDX10 · Probable ATP-dependent RNA helicase DDX10

DDX10 is the partner protein in the NUP98::DDX10 fusion. This entry records where each of its parts sits along the protein, in residue numbers, so the fusion diagram can draw what the break keeps and what it throws away.

The same thing, for a scientist

Reference domain architecture for DDX10 (UniProt Q13206, 875 aa), a DEAD-box RNA helicase and ribosome-assembly factor. The helicase ATP-binding and helicase C-terminal domains span 100-274 and 287-448, with the Q motif at 69-97 and the DEAD-box motif at 222-225. Created so the 3D fusion viewer can resolve `fusion-nup98-ddx10`, whose lane previously had no coordinates for the 3' partner and was silently dropped. Note that the transforming element of the fusion is reported to be a 24-residue NOL10-binding stretch rather than the helicase activity, so these domain coordinates describe the protein, not the mechanism.

What it looks like
Probable ATP-dependent RNA helicase DDX10875 aa
Helicase ATP-bindingHelicase ATP-binding · residues 100–274 · UniProt feature call, fetched this session.Helicase C-terminalHelicase C-terminal · residues 287–448 · UniProt feature call, fetched this session.Q moQ motif · residues 69–97 · UniProt feature call, fetched this session.DEAD box motif · residues 222–225 · UniProt feature call, fetched this session.0200400600800
loading AF-Q13206-F1…
AlphaFold AF-Q13206-F1 ↗
colourshape

This is a prediction, not a measurement. No one has seen this protein in this shape. The colours say how much the software trusts itself, and that is worth reading before anything else — the orange stretches are places the model is effectively saying this part has no fixed shape.

very high (90+)confident (70–90)low (50–70)very low (<50)
I have never read one of these pictures before

A protein is one long chain of amino acids that folds up. The ribbon traces that chain from one end to the other; it is not a wire, it is a simplification of where the backbone runs. Drag to rotate, scroll to zoom.

Domains are the stretches of chain that do a particular job, and they are what the coloured blocks above the picture mark out. Click one and the view flies to it. In this project the important question about any domain is usually whether the fusion still has it — the labels say lost where it does not.

Anything in yellow sticks is a bound small molecule, which is usually the drug.

Go deeper
How this accession was resolved

UniProt's gene_exact: search matches synonyms, so a search hit is not proof of identity. This entry was built by fetching https://rest.uniprot.org/uniprotkb/Q13206.json directly and reading back the primary gene name from genes[0].geneName.value (DDX10) and the length from sequence.length (875 aa), then copying every feature boundary out of the same fetched record 1.

UniProt lists no gene-name synonyms for DDX10, so alias searching cannot under-count it on the current symbol; older literature under legacy names would still be missed.

Facts and figures
uniprotQ13206
gene symbolDDX10
length AA875
protein nameProbable ATP-dependent RNA helicase DDX10
alphafold IDAF-Q13206-F1
resolution noteFetched from the UniProt REST API this session; primary gene name asserted from genes[0].geneName.value, not from a gene_exact search, which matches synonyms.
domains
Q motif69.0Q motif: 69Helicase ATP-binding100.0Helicase ATP-binding: 100DEAD box motif222.0DEAD box motif: 222Helicase C-terminal287.0Helicase C-terminal: 287
uniprot gene name synonyms
[]
domains — the numbers behind the chart
[
  {
    "name": "Helicase ATP-binding",
    "start": 100,
    "end": 274,
    "feature_type": "Domain",
    "note": "UniProt feature call, fetched this session.",
    "boundary_precision": "firm"
  },
  {
    "name": "Helicase C-terminal",
    "start": 287,
    "end": 448,
    "feature_type": "Domain",
    "note": "UniProt feature call, fetched this session.",
    "boundary_precision": "firm"
  },
  {
    "name": "Q motif",
    "start": 69,
    "end": 97,
    "feature_type": "Motif",
    "note": "UniProt feature call, fetched this session.",
    "boundary_precision": "firm"
  },
  {
    "name": "DEAD box motif",
    "start": 222,
    "end": 225,
    "feature_type": "Motif",
    "note": "UniProt feature call, fetched this session.",
    "boundary_precision": "firm"
  }
]
disordered regions
[
  {
    "start": 1,
    "end": 43
  },
  {
    "start": 562,
    "end": 631
  },
  {
    "start": 703,
    "end": 850
  }
]
How this could bite us back
  • Drawing a domain map implies the domains are what matter; in at least one NUP98 partner the annotated enzymatic domain was a passenger and a short unannotated interaction stretch did the work, so a tidy lane can mislead about mechanism.
Still open
  1. Which residue of DDX10 does the patient fusion breakpoint fall on? The founding reports describe the junction at exon or domain level, not residue level.
  2. Are any of these domains dispensable for transformation in the fusion context? No separation-of-function mutant of this partner has been reported within the fusion.
Every source behind this entry (1)
  1. E1established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.database

    DDX10 is UniProt Q13206, 875 aa (Probable ATP-dependent RNA helicase DDX10), with the domain boundaries listed in data.domains.

    What this evidence cannot show

    Primary gene name and sequence length were read back from the fetched record rather than assumed from a search result. UniProt feature boundaries are curated from primary literature of varying age and are revised; they are reference coordinates for drawing, not experimental measurements of this fusion.

    Evidence that argues against this (2)
    • These are UniProt folded-domain calls for the wild-type protein. Which of them the patient fusion retains depends on the breakpoint, which is not resolved to a residue in the founding report, so the fusion entry asserts retention and this entry does not. Arai Y et al. 1997
    • The published functional work locates the transforming activity in a 24-amino-acid NOL10-binding stretch rather than in the annotated helicase domains, so a viewer lane drawn from these coordinates will emphasise the parts of the protein that matter least. Shima Y et al. 2025
Connected to