RUNX1T1 (ETO / MTG8) domain architecture
also called RUNX1T1 · ETO / MTG8
RUNX1T1 is the 3' partner of RUNX1::RUNX1T1, the t(8;21) fusion of core-binding-factor AML. This entry lists where each of its functional parts sits along the protein, measured as residue numbers, so the fusion diagrams can draw which parts survive the break and which are thrown away.
The same thing, for a scientist
Reference domain architecture for RUNX1T1 (UniProt Q06455, 604 aa). The founding ETO-family corepressor and the closest paralogue of CBFA2T3, with the same architecture: TAFH at 120-215, NHR2 oligomerisation region at 337-383, NHR3 at 443-492, MYND zinc finger at 515-551. Created so the 3D fusion viewer can resolve fusion-runx1-runx1t1, which previously had no coordinates for this partner and silently dropped the lane. Domain fate in the fusion is asserted by the fusion entry, not here.
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.
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.
Why this entry exists
The join checker reported fusion-runx1-runx1t1: no protein entry for RUNX1T1. Without coordinates the comparative 3D viewer cannot draw the lane at all, and it was omitting it without warning rather than flagging it. This is a reference-coordinate entry: it asserts the architecture and nothing about the fusion.
Folded domains versus functional regions. UniProt mixes two very different annotation kinds. Domain, Zinc finger and DNA binding are fold calls with real boundaries. Region is a functional assertion that often spans disorder and can overlap other regions or run for hundreds of residues. Both are recorded with boundary_precision marking which is which, because drawing a soft functional region as a crisp box is exactly the kind of false precision this graph exists to avoid.
Architecture
| Part | Residues | Kind | Precision |
|---|---|---|---|
| TAFH | 120-215 | Domain | firm |
| MYND-type | 515-551 | Zinc finger | firm |
| Important for oligomerization | 337-383 | Region | soft |
| Nervy homology region 2 (NHR2) | 337-383 | Region | soft |
| Nervy homology region 3 (NHR3) | 443-492 | Region | soft |
9 PDB entries reference this protein.
| uniprot | Q06455 |
|---|---|
| gene symbol | RUNX1T1 |
| length AA | 604 |
| protein name | Protein CBFA2T1 |
| alphafold ID | AF-Q06455-F1 |
| n PDB total | 9 |
| uniprot verified | true |
| accession resolution | exact gene-name search, reviewed human only, gene symbol confirmed in the response |
| created for | fusion-runx1-runx1t1 |
domains — the numbers behind the chart
[
{
"name": "TAFH",
"start": 120,
"end": 215,
"feature_type": "Domain",
"note": "UniProt folded-domain call.",
"boundary_precision": "firm",
"aliases": [
"NHR1",
"TAFH/NHR1",
"NHR1 (TAF110-like)",
"Nervy homology region 1"
],
"alias_basis": "InterPro IPR003894 is named \"TAFH/NHR1\", establishing that the ETO-family TAFH domain and NHR1 are the same domain under two naming conventions."
},
{
"name": "MYND-type",
"start": 515,
"end": 551,
"feature_type": "Zinc finger",
"note": "UniProt folded-domain call.",
"boundary_precision": "firm"
},
{
"name": "Important for oligomerization",
"start": 337,
"end": 383,
"feature_type": "Region",
"note": "UniProt functional region, not a fold boundary. Soft edges; render as low confidence.",
"boundary_precision": "soft"
},
{
"name": "Nervy homology region 2 (NHR2)",
"start": 337,
"end": 383,
"feature_type": "Region",
"note": "UniProt functional region, not a fold boundary. Soft edges; render as low confidence.",
"boundary_precision": "soft"
},
{
"name": "Nervy homology region 3 (NHR3)",
"start": 443,
"end": 492,
"feature_type": "Region",
"note": "UniProt functional region, not a fold boundary. Soft edges; render as low confidence.",
"boundary_precision": "soft"
}
]PDB IDS
[ "1WQ6", "2DJ8", "2H7B", "2KNH", "2KYG", "2OD1", "2ODD", "2PP4", "4JOL" ]
- Nothing here licenses targeting any part of RUNX1T1. These are coordinates, not a druggability claim; a domain with crisp boundaries is not thereby a ligandable pocket.
- Drawing UniProt `Region` features as boxes in the viewer risks implying structural knowledge that does not exist. They are marked soft and should be rendered differently from fold calls.
- Where does the fusion-runx1-runx1t1 breakpoint fall relative to these boundaries, and is the junction codon actually mapped or only inferred from cDNA?
- Which of these parts are retained in the fusion, and is retention ever being confused with requirement for transformation?
- Do InterPro and the deposited crystal constructs agree with these UniProt boundaries? Where they do not, the disagreement should be recorded rather than silently resolved in UniProt's favour.
- E1strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.dataset
Human RUNX1T1 (Protein CBFA2T1) is 604 residues (UniProt Q06455) with the domain and region boundaries tabulated in this entry, and is referenced by 9 PDB entries.
UniProtKB Q06455 (RUNX1T1_HUMAN): sequence length, domain, zinc-finger, DNA-binding, repeat, motif and region features, and PDB cross-references · UniProt Consortium · UniProtKB 2026What this evidence cannot show
Accession resolved by exact gene-name search restricted to reviewed human entries and confirmed against the gene symbol returned, because a previous lookup in this project silently resolved to the wrong gene. Coordinates are for the canonical isoform only; several of these proteins have isoforms that shift numbering. UniProt `Region` features are curator functional calls, not folds.
Evidence that argues against this (1)
- Domain boundaries are not a settled fact and differ between sources. InterPro, Pfam, SMART and individual crystal-structure constructs routinely disagree with UniProt by tens of residues, and published figures often use construct boundaries rather than database ones. Any downstream claim that a breakpoint falls just inside or just outside a domain is therefore only as firm as the boundary definition it assumes, which for every `Region` feature here is soft. InterPro Consortium 2026
reference domain coordinates for the RUNX1T1 side of this fusion
- ← analogous toCBFA2T3 (ETO2 / MTG16) domain architecture
ETO-family paralogues with the same TAFH / NHR2 / NHR3 / MYND architecture; both contribute the identical corepressor module to a different leukemia fusion
the NHR2 domain that the compound binds