Carm1
entrez
59035
canonical
uniprot
Q9WVG6
canonical
ensembl
ENSMUSG00000032185
resolver
ensp
ENSMUSP00000034703
resolver
ensp
ENSMUSP00000111053
resolver
genesymbol
Carm1
resolver
genesymbol_syn
Prmt4
resolver
uniprot
Q3TYB9
resolver
uniprot
Q8K1Y5
resolver
uniprot
Q91W24
resolver
uniprot
Q99KX8
resolver
uniprot_entry
CARM1_MOUSE
resolver
uniprot_sec
Q3TYB9
resolver
uniprot_sec
Q8K1Y5
resolver
uniprot_sec
Q91W24
resolver
uniprot_sec
Q99KX8
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:0000269|PubMed:17882261}.
uniprot
proteins
amino_acid_sequence
MAAAAATAVGPGAGSAGVAGPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDAAGIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLIQFATPHDFCSFYNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPSPPPGSHYTSPSENMWNTGSTYNLSSGVAVAGMPTAYDLSSVIAGGSSVGHNNLIPLANTGIVNHTHSRMGSIMSTGIVQGSSGAQGGGGSSSAHYAVNNQFTMGGPAISMASPMSIPTNTMHYGS
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: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, PubMed:12498683, PubMed:15339660, PubMed:15616592). 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 (PubMed:11997499, PubMed:16322096, PubMed:17882261, PubMed:19843527). During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C (PubMed:11713257). During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B (PubMed:11983685). Acts as a coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue (PubMed:18188184). Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors (PubMed:21138967). Also seems to be involved in p53/TP53 transcriptional activation (PubMed:15186775). 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:11701890). 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 (PubMed:11850402, PubMed:12237300, PubMed:12756295). Acts as a transcriptional coactivator of ACACA/acetyl-CoA carboxylase by enriching H3R17 methylation at its promoter, thereby positively regulating fatty acid synthesis (PubMed:30366907). 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 (By similarity). {ECO:0000250|UniProtKB:Q86X55, ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:11341840, ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11751582, ECO:0000269|PubMed:11850402, ECO:0000269|PubMed:11983685, ECO:0000269|PubMed:11997499, ECO:0000269|PubMed:12237300, ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:12756295, ECO:0000269|PubMed:14966289, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15339660, ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:17218272, ECO:0000269|PubMed:17882261, ECO:0000269|PubMed:18188184, ECO:0000269|PubMed:19843527, ECO:0000269|PubMed:19897492, ECO:0000269|PubMed:21138967, ECO:0000269|PubMed:30366907}.
uniprot
proteins
mass_dalton
65854
uniprot
proteins
mutagenesis
MUTAGEN 154; /note="Y->A,F,R: Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity."; /evidence="ECO:0000269|PubMed:19843527"; MUTAGEN 169; /note="R->A: Loss of protein methyltransferase activity."; /evidence="ECO:0000269|PubMed:19897492"; MUTAGEN 173; /note="Y->A: Reduces protein methyltransferase activity."; /evidence="ECO:0000269|PubMed:19897492"; MUTAGEN 189..191; /note="VLD->AAA: Abolishes histone methyltransferase activity and coactivator activity."; /evidence="ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:11701890"; MUTAGEN 217; /note="S->A: Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity. Localized in the nucleus."; /evidence="ECO:0000269|PubMed:19843527"; MUTAGEN 217; /note="S->C,T: Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity."; /evidence="ECO:0000269|PubMed:19843527"; MUTAGEN 217; /note="S->E: Loss of S-adenosyl-L-methionine binding. Loss of protein methyltransferase activity. Localized in the cytosol."; /evidence="ECO:0000269|PubMed:19843527"; MUTAGEN 229; /note="S->E: Abolishes dimerization."; /evidence="ECO:0000269|PubMed:19843527"; MUTAGEN 267; /note="E->Q: Abolishes histone methyltransferase activity and reduces coactivator activity."; /evidence="ECO:0000269|PubMed:11983685, ECO:0000269|PubMed:11997499"; MUTAGEN 551; /note="R->K: Abolishes dimethylation. Impairs transcription coactivator activity and regulation of alternative splicing. No effect on methyltransferase activity."; /evidence="ECO:0000269|PubMed:21138967
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-217 is strongly increased during mitosis, and decreases rapidly to a very low, basal level after entry into the G1 phase of the cell cycle (By similarity). Phosphorylation at Ser-217 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity. Phosphorylation at Ser-217 may promote cytosolic location (PubMed:19843527). {ECO:0000250|UniProtKB:Q86X55, ECO:0000269|PubMed:19843527}.; PTM: Auto-methylated on Arg-551. Methylation enhances transcription coactivator activity. Methylation is required for its role in the regulation of pre-mRNA alternative splicing. {ECO:0000269|PubMed:21138967}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9 at Lys-228; leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q86X55}.
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
Protein arginine N-methyltransferase family
uniprot
proteins
pubmed
10381882
uniprot
proteins
pubmed
11341840
uniprot
proteins
pubmed
11701890
uniprot
proteins
pubmed
11713257
uniprot
proteins
pubmed
11747826
uniprot
proteins
pubmed
11751582
uniprot
proteins
pubmed
11850402
uniprot
proteins
pubmed
11983685
uniprot
proteins
pubmed
11997499
uniprot
proteins
pubmed
12237300
uniprot
proteins
pubmed
12351636
uniprot
proteins
pubmed
12498683
uniprot
proteins
pubmed
12756295
uniprot
proteins
pubmed
14966289
uniprot
proteins
pubmed
15186775
uniprot
proteins
pubmed
15339660
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616592
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16322096
uniprot
proteins
pubmed
16508003
uniprot
proteins
pubmed
17218272
uniprot
proteins
pubmed
17882261
uniprot
proteins
pubmed
18188184
uniprot
proteins
pubmed
19843527
uniprot
proteins
pubmed
19897492
uniprot
proteins
pubmed
21138967
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
30366907
uniprot
proteins
sequence_length
608
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:19843527, ECO:0000269|PubMed:30366907}. Cytoplasm {ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:19843527, ECO:0000269|PubMed:30366907}. Chromosome {ECO:0000250|UniProtKB:Q86X55}. Note=Mainly nuclear during the G1, S and G2 phases of the cell cycle. Cytoplasmic during mitosis, after breakup of the nuclear membrane. Localizes to replication forks. {ECO:0000250|UniProtKB:Q86X55}.
uniprot
proteins