Set1/Ash2 histone methyltransferase complex subunit ASH2 (ASH2L) is a 628-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UBL3.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 75.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 50% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 27% |
What pLDDT means and how to read it
Transcriptional regulator (PubMed:12670868). Component or associated component of some histone methyltransferase complexes which regulates transcription through recruitment of those complexes to gene promoters (PubMed:19131338). Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated (PubMed:19556245). As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3 (PubMed:19556245). May play a role in hematopoiesis (PubMed:12670868). In association with RBBP5 and WDR5, stimulates the histone methyltransferase…
Interacts with HCFC1 (PubMed:12670868). Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7 (PubMed:15199122, PubMed:15960975, PubMed:17500065). Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5F6L | X-ray | 1.9 Å | B=380-496, B=516-598 |
| 3TOJ | X-ray | 2.07 Å | A/B=370-496, A/B=516-617 |
| 3RSN | X-ray | 2.1 Å | A=96-271 |
| 4X8N | X-ray | 2.1 Å | A=380-495, A=539-598 |
| 7W67 | X-ray | 2.19 Å | A=380-496, A=516-598 |
| 4X8P | X-ray | 2.2 Å | A=380-495, A=539-598 |
| 7W6A | X-ray | 2.21 Å | A=380-496, A=516-598 |
| 4RIQ | X-ray | 2.23 Å | C/F/I/L/O/R/U/X=603-618 |
| 6E2H | X-ray | 2.24 Å | D=380-622 |
| 7W6L | X-ray | 2.26 Å | A/B=380-496, A/B=516-598 |
| 5F6K | X-ray | 2.41 Å | A/B=380-496, A/B=516-598 |
| 3S32 | X-ray | 2.45 Å | A=95-280 |
| 7W6I | X-ray | 2.56 Å | A=380-496, A=516-598 |
| 7W6J | X-ray | 2.68 Å | A=380-496, A=516-598 |
| 7BRE | X-ray | 2.8 Å | A/D=380-496, A/D=516-598 |
| 6KIU | EM | 3.2 Å | T=95-628 |
| 6KIV | EM | 4.0 Å | T=95-628 |
| 6KIW | EM | 4.0 Å | T=95-628 |
| 6KIX | EM | 4.1 Å | T=95-628 |
| 7UD5 | EM | 4.25 Å | M=95-628 |
Showing 20 of 27 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.