{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q86X55","secondaryAccessions":["A6NN38"],"uniProtkbId":"CARM1_HUMAN","entryAudit":{"firstPublicDate":"2005-01-04","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2010-10-05","entryVersion":195,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Histone-arginine methyltransferase CARM1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19405910"}],"value":"2.1.1.319"}]},"alternativeNames":[{"fullName":{"value":"Coactivator-associated arginine methyltransferase 1"}},{"fullName":{"value":"Protein arginine N-methyltransferase 4"}}]},"genes":[{"geneName":{"value":"CARM1"},"synonyms":[{"value":"PRMT4"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9WVG6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12237300"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15731352"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16497732"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19405910"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33412112"}],"value":"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 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription (By similarity). During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C (By similarity). During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B (By similarity). Acts as a coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue (By similarity). Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors (By similarity). Also seems to be involved in p53/TP53 transcriptional activation (By similarity). Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation (PubMed:15731352). Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs (By similarity). Acts as a transcriptional coactivator of ACACA/acetyl-CoA carboxylase by enriching H3R17 methylation at its promoter, thereby positively regulating fatty acid synthesis (By similarity). Independently of its methyltransferase activity, involved in replication fork progression: promotes PARP1 recruitment to replication forks, leading to poly-ADP-ribosylation of chromatin at replication forks and reduced fork speed (PubMed:33412112)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-[protein] + 2 S-adenosyl-L-methionine = N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48096"},{"database":"Rhea","id":"RHEA-COMP:10532"},{"database":"Rhea","id":"RHEA-COMP:11991"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29965"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:61897"}],"ecNumber":"2.1.1.319","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19405910"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9WVG6"}],"value":"Methylation of H3R17 (H3R17me) by CARM1 is stimulated by preacetylation of H3 'Lys-18' (H3K18ac) H3 'Lys-23' (H3K23ac) by EP300 and blocked by citrullination of H3 'Arg-17' (H3R17ci) by PADI4"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q4AE70"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9WVG6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15471871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16497732"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33412112"}],"value":"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 RELA (PubMed:16497732). Identified in a complex containing CARM1, TRIM24 and NCOA2/GRIP1 (By similarity). Interacts with NCOA3/SRC3 (By similarity). Interacts with SKP2 (By similarity). Interacts (via PH domain-like fold) with C9orf72 (By similarity). Interacts with PARP1; promoting PARP1 recruitment to replication forks (PubMed:33412112)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17005681"}],"value":"(Microbial infection) Interacts with HTLV-1 protein Tax"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"P04075","geneName":"ALDOA","intActId":"EBI-709613"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"P17676","geneName":"CEBPB","intActId":"EBI-969696"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"Q96EY1","geneName":"DNAJA3","intActId":"EBI-356767"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"P01112","geneName":"HRAS","intActId":"EBI-350145"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"Q6NYC1","geneName":"JMJD6","intActId":"EBI-8464037"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"Q9Y6Q9","geneName":"NCOA3","intActId":"EBI-81196"},"numberOfExperiments":13,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"O43809","geneName":"NUDT21","intActId":"EBI-355720"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"Q96PU8","geneName":"QKI","intActId":"EBI-945792"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"Q92922","geneName":"SMARCC1","intActId":"EBI-355653"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"P55854","geneName":"SUMO3","intActId":"EBI-474067"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"Q8IUC6","geneName":"TICAM1","intActId":"EBI-525995"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"Q05826","geneName":"CEBPB","intActId":"EBI-7774198"},"numberOfExperiments":3,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"Q86X55","intActId":"EBI-2339854"},"interactantTwo":{"uniProtKBAccession":"A0A1U8QN96","geneName":"YPMT1.27c","intActId":"EBI-20592362"},"numberOfExperiments":2,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19843527"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33412112"}],"value":"Mainly nuclear during the G1, S and G2 phases of the cell cycle (PubMed:19843527). 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Phosphorylation at Ser-216 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34480022"}],"value":"Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9 at Lys-227; leading to proteasomal degradation"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01015"}],"value":"Belongs to the class I-like SAM-binding methyltransferase superfamily. 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