Histone-arginine methyltransferase CARM1 (Carm1) is a 608-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9WVG6.
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The mean pLDDT of this model is 78.3 (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 | 57% |
| 70 to 90 | Confident: backbone generally right | 16% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability (PubMed:10381882, PubMed:11341840, PubMed:11997499, PubMed:14966289, PubMed:17218272, PubMed:19897492, PubMed:21138967). Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activation of transcription via chromatin remodeling (PubMed:10381882, PubMed:11341840, PubMed:11747826, PubMed:11751582, PubMed:11997499,…
Homodimer (PubMed:17882261, PubMed:19897492). Interacts with NR1H4 (By similarity). Interacts with SNRPC (By similarity). Interacts with the C-terminus of NCOA2/GRIP1, NCO3/ACTR and NCOA1/SRC1 (PubMed:10381882). Part of a complex consisting of CARM1, EP300/P300 and NCOA2/GRIP1 (PubMed:11997499). Interacts with FLII, TP53, myogenic factor MEF2, EP300/P300, TRIM24, CREBBP and CTNNB1…
Nucleus, Cytoplasm, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5IH3 | X-ray | 1.77 Å | A/B/C/D=130-487 |
| 5LV3 | X-ray | 1.8 Å | A/B/C/D=130-487 |
| 7QPH | X-ray | 1.9 Å | A/B/C/D=130-487 |
| 5K8X | X-ray | 1.99 Å | A/B/C/D=130-487 |
| 5ISB | X-ray | 2.0 Å | A/B/C/D=130-487 |
| 5LGR | X-ray | 2.0 Å | A/B/C/D=130-487 |
| 7QRD | X-ray | 2.0 Å | A/B/C/D=130-507 |
| 5IS6 | X-ray | 2.01 Å | A/B/C/D=130-487 |
| 5LGP | X-ray | 2.04 Å | A/B/C/D=130-487 |
| 7PUQ | X-ray | 2.09 Å | A/B/C/D=130-486 |
| 5ISE | X-ray | 2.1 Å | A/B/C/D=130-487 |
| 5K8W | X-ray | 2.1 Å | A/B/C/D=130-487 |
| 5LGS | X-ray | 2.1 Å | A/B/C/D=130-487 |
| 7PPQ | X-ray | 2.1 Å | A/B/C/D=130-487 |
| 5LGQ | X-ray | 2.11 Å | A/B/C/D=130-487 |
| 5ISH | X-ray | 2.15 Å | A/B/C/D=130-487 |
| 7PU8 | X-ray | 2.19 Å | A/B/C/D=130-487 |
| 7PUC | X-ray | 2.19 Å | A/B/C/D=130-487 |
| 7OKP | X-ray | 2.2 Å | A/B/C/D=130-497 |
| 9I9U | X-ray | 2.2 Å | A/B/C/D=130-497 |
Showing 20 of 43 experimental structures (best resolution first).
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