Histone-arginine methyltransferase CARM1 (CARM1) is a 608-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q86X55.
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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 | 24% |
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:12237300, PubMed:16497732, PubMed:19405910). 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:12237300, PubMed:16497732, PubMed:19405910). During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300…
Homodimer (By similarity). Interacts with NR1H4 (PubMed:15471871). Interacts with SNRPC (By similarity). Interacts with the C-terminus of NCOA2/GRIP1, NCO3/ACTR and NCOA1/SRC1 (By similarity). Part of a complex consisting of CARM1, EP300/P300 and NCOA2/GRIP1 (By similarity). Interacts with FLII, TP53, myogenic factor MEF2, EP300/P300, TRIM24, CREBBP and CTNNB1 (By similarity). Interacts with…
Nucleus, Cytoplasm, Chromosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8G2H | X-ray | 1.49 Å | A=140-480 |
| 6DVR | X-ray | 1.54 Å | A/B=146-489 |
| 8SIG | X-ray | 1.78 Å | A=140-480 |
| 6S7A | X-ray | 1.86 Å | A/B/C/D=135-479 |
| 8UQH | X-ray | 1.87 Å | A/B/C/D=139-479 |
| 5U4X | X-ray | 1.88 Å | A/B/C/D=140-480 |
| 6ARJ | X-ray | 1.92 Å | A/B/C/D=134-479 |
| 5DX1 | X-ray | 1.93 Å | A/B/C/D=134-479 |
| 5DX8 | X-ray | 1.94 Å | A/B/C/D=134-479 |
| 5DXJ | X-ray | 1.95 Å | A/B/C/D=134-479 |
| 4IKP | X-ray | 2.0 Å | A/B/C/D=140-480 |
| 6ARV | X-ray | 2.0 Å | A/B/C/D=134-479 |
| 6D2L | X-ray | 2.0 Å | A/B/C/D/E/F=146-489 |
| 7U9I | X-ray | 2.0 Å | A/B=146-489 |
| 5DX0 | X-ray | 2.05 Å | A/B/C/D=134-479 |
| 6S71 | X-ray | 2.06 Å | A/B/C/D=135-479 |
| 5DXA | X-ray | 2.07 Å | A/B/C/D=134-479 |
| 2Y1W | X-ray | 2.1 Å | A/B/C/D=135-482 |
| 6S74 | X-ray | 2.1 Å | A/B/C/D=135-479 |
| 6S79 | X-ray | 2.1 Å | A/B/C/D=135-479 |
Showing 20 of 31 experimental structures (best resolution first).
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