CARM1
entrez
10498
canonical
uniprot
Q86X55
canonical
ensembl
ENSG00000142453
resolver
ensp
ENSP00000325690
resolver
ensp
ENSP00000340934
resolver
genesymbol
CARM1
resolver
genesymbol_syn
PRMT4
resolver
hgnc
HGNC:23393
resolver
uniprot
A6NN38
resolver
uniprot_entry
CARM1_HUMAN
resolver
uniprot_sec
A6NN38
resolver
activity_regulation
ACTIVITY REGULATION: 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. {ECO:0000250|UniProtKB:Q9WVG6}.
uniprot
proteins
amino_acid_sequence
MAAAAAAVGPGAGGAGSAVPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDSAGIALYSHEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSFYNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPSPPPGSHYTSPSENMWNTGSTYNLSSGMAVAGMPTAYDLSSVIASGSSVGHNNLIPLANTGIVNHTHSRMGSIMSTGIVQGSSGAQGSGGGSTSAHYAVNSQFTMGGPAISMASPMSIPTNTMHYGS
uniprot
proteins
ec_number
2.1.1.319
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250|UniProtKB:Q9WVG6, ECO:0000269|PubMed:12237300, ECO:0000269|PubMed:15731352, ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:19405910, ECO:0000269|PubMed:33412112}.
uniprot
proteins
mass_dalton
65854
uniprot
proteins
mutagenesis
MUTAGEN 168; /note="R->A: Loss of protein methyltransferase activity without affecting ability to regulate replication fork progression."; /evidence="ECO:0000269|PubMed:19405910"; MUTAGEN 227; /note="K->A: Loss of FBXO9-mediated ubiquitination and subsequent proteasomal degradation."; /evidence="ECO:0000269|PubMed:34480022
uniprot
proteins
post_translational_modification
PTM: Auto-methylated on Arg-550. Methylation enhances transcription coactivator activity. Methylation is required for its role in the regulation of pre-mRNA alternative splicing (By similarity). {ECO:0000250|UniProtKB:Q9WVG6}.; PTM: Phosphorylation at Ser-216 is strongly increased during mitosis, and decreases rapidly to a very low, basal level after entry into the G1 phase of the cell cycle (PubMed:19843527). Phosphorylation at Ser-216 may promote location in the cytosol. Phosphorylation at Ser-216 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity (By similarity). {ECO:0000250|UniProtKB:Q9WVG6, ECO:0000269|PubMed:19843527}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9 at Lys-227; leading to proteasomal degradation. {ECO:0000269|PubMed:34480022}.
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
Protein arginine N-methyltransferase family
uniprot
proteins
pubmed
12237300
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15221992
uniprot
proteins
pubmed
15471871
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15731352
uniprot
proteins
pubmed
16497732
uniprot
proteins
pubmed
17005681
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19405910
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19843527
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21410432
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
33412112
uniprot
proteins
pubmed
34480022
uniprot
proteins
sequence_length
608
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19843527}. Cytoplasm {ECO:0000269|PubMed:19843527}. Chromosome {ECO:0000269|PubMed:33412112}. Note=Mainly nuclear during the G1, S and G2 phases of the cell cycle (PubMed:19843527). Cytoplasmic during mitosis, after breakup of the nuclear membrane (PubMed:19843527). Localizes to replication forks (PubMed:33412112). {ECO:0000269|PubMed:19843527, ECO:0000269|PubMed:33412112}.
uniprot
proteins