Proteinstrongking

GLIS2 (GLI-similar 2) domain architecture

also called GLIS2 · GLI-similar 2

GLIS2 is the 3' partner of CBFA2T3::GLIS2. 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 GLIS2 (UniProt Q9BZE0, 524 aa). A five-C2H2-zinc-finger Kruppel-family transcription factor. UniProt annotates separate activation (71-137) and repression (148-171) regions N-terminal to the finger array. Created so the 3D fusion viewer can resolve fusion-cbfa2t3-glis2, 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.

What it looks like

Zinc finger protein GLIS2524 aa

loading AF-Q9BZE0-F1…

AlphaFold AF-Q9BZE0-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

Why this entry exists

The join checker reported fusion-cbfa2t3-glis2: no protein entry for GLIS2. 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
C2H2-type 1	168-193	Zinc finger	firm
C2H2-type 2; atypical	202-229	Zinc finger	firm
C2H2-type 3	235-257	Zinc finger	firm
C2H2-type 4	263-287	Zinc finger	firm
C2H2-type 5	293-317	Zinc finger	firm
Interaction with CTNND1	35-174	Region	soft
Transcription activation	71-137	Region	soft
Transcription repression	148-171	Region	soft

No PDB entry references this protein. Any structural claim about it rests on prediction alone.

Facts and figures

uniprot	Q9BZE0
gene symbol	GLIS2
length AA	524
protein name	Zinc finger protein GLIS2
alphafold ID	AF-Q9BZE0-F1
n PDB total	0
uniprot verified	true
accession resolution	exact gene-name search, reviewed human only, gene symbol confirmed in the response
created for	fusion-cbfa2t3-glis2

domains

domains — the numbers behind the chart

[
  {
    "name": "C2H2-type 1",
    "start": 168,
    "end": 193,
    "feature_type": "Zinc finger",
    "note": "UniProt folded-domain call.",
    "boundary_precision": "firm"
  },
  {
    "name": "C2H2-type 2; atypical",
    "start": 202,
    "end": 229,
    "feature_type": "Zinc finger",
    "note": "UniProt folded-domain call.",
    "boundary_precision": "firm"
  },
  {
    "name": "C2H2-type 3",
    "start": 235,
    "end": 257,
    "feature_type": "Zinc finger",
    "note": "UniProt folded-domain call.",
    "boundary_precision": "firm"
  },
  {
    "name": "C2H2-type 4",
    "start": 263,
    "end": 287,
    "feature_type": "Zinc finger",
    "note": "UniProt folded-domain call.",
    "boundary_precision": "firm"
  },
  {
    "name": "C2H2-type 5",
    "start": 293,
    "end": 317,
    "feature_type": "Zinc finger",
    "note": "UniProt folded-domain call.",
    "boundary_precision": "firm"
  },
  {
    "name": "Interaction with CTNND1",
    "start": 35,
    "end": 174,
    "feature_type": "Region",
    "note": "UniProt functional region, not a fold boundary. Soft edges; render as low confidence.",
    "boundary_precision": "soft"
  },
  {
    "name": "Transcription activation",
    "start": 71,
    "end": 137,
    "feature_type": "Region",
    "note": "UniProt functional region, not a fold boundary. Soft edges; render as low confidence.",
    "boundary_precision": "soft"
  },
  {
    "name": "Transcription repression",
    "start": 148,
    "end": 171,
    "feature_type": "Region",
    "note": "UniProt functional region, not a fold boundary. Soft edges; render as low confidence.",
    "boundary_precision": "soft"
  }
]

PDB IDS

[]

How this could bite us back

Nothing here licenses targeting any part of GLIS2. 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.

Still open

Where does the fusion-cbfa2t3-glis2 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.

Every source behind this entry (1)

E1strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.dataset
Human GLIS2 (Zinc finger protein GLIS2) is 524 residues (UniProt Q9BZE0) with the domain and region boundaries tabulated in this entry, and is referenced by 0 PDB entries.
UniProtKB Q9BZE0 (GLIS2_HUMAN): sequence length, domain, zinc-finger, DNA-binding, repeat, motif and region features, and PDB cross-references · UniProt Consortium · UniProtKB 2026
What 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

Connected to

analogous to →DUX4 (double homeobox 4) domain architecture
both are DNA-binding transcription factors contributed as the oncogenic moiety of a paediatric fusion
← analogous toHLF (hepatic leukemia factor) domain architecture
both contribute a sequence-specific DNA-binding module to a fusion rather than an enzyme
part of →CBFA2T3::GLIS2, inv(16)(p13.3q24.3)
reference domain coordinates for the GLIS2 side of this fusion