Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
CARM1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CARM1 a protein arginine methyltransferase that methylates histones and other proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginine residues. A key epigenetic regulator of hematopoiesis affecting multiple lineages. Recruited to promoters upon gene activation together with histone acetyltransferases from P300 and p160 families, methylates histone H3 at R17 (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2 activation, acts synergically with P300 and either one of the p160 histone acetyltransferases SRC1, NCoA2 and SRC-3 or CTNNB1 to activate transcription. During myogenic transcriptional activation, acts together with SRC-3 as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53 transcriptional activation. Methylates P300, both at R 2142, which may loosen its interaction with NCoA2, and at R580 and R604 in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Methylates RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA- stabilizing properties and the half-life of their target mRNAs. Interacts with the C-terminus of NCoA2, SRC-3 and SRC1. Part of a complex consisting of CARM1, P300 and NCoA2. Interacts with FLII, TP53, myogenic factor MEF2, P300, TRIM24, CREBBP and CTNNB1. Identified in a complex containing CARM1, TRIM24 and NCoA2. Interacts with SRC3. Interacts with SNRPC. Interacts with NR1H4. Interacts with RELA. Interacts with HTLV-1 Tax-1. Overexpressed in prostate adenocarcinomas and high-grade prostatic intraepithelial neoplasia. Methylation of H3R17 (H3R17me) by CARM1 is stimulated by preacetylation of H3 K18 (H3K18ac) H3 K23 (H3K23ac) by EP300 and blocked by citrullination of H3 R17 (H3R17ci) by PADI4. Belongs to the protein arginine N-methyltransferase family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Methyltransferase, protein arginine; EC 2.1.1.125; Methyltransferase; EC 2.1.1.-; Nuclear receptor co-regulator
Cellular Component: nucleoplasm; cytoplasm; nucleus; cytosol
Molecular Function: protein-arginine omega-N asymmetric methyltransferase activity; histone methyltransferase activity; protein-arginine N-methyltransferase activity; protein binding; protein homodimerization activity; ligand-dependent nuclear receptor transcription coactivator activity; transcription coactivator activity; beta-catenin binding; histone-arginine N-methyltransferase activity; protein methyltransferase activity
Biological Process: histone methylation; regulation of estrogen receptor signaling pathway; response to cAMP; estrogen receptor signaling pathway; viral reproduction; transcription, DNA-dependent; regulation of transcription, DNA-dependent; positive regulation of cell proliferation; positive regulation of fat cell differentiation; pathogenesis; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; cellular lipid metabolic process; negative regulation of protein binding
Reference #:  Q86X55 (UniProtKB)
Alt. Names/Synonyms: CARM1; Coactivator-associated arginine methyltransferase 1; Histone-arginine methyltransferase CARM1; PRMT4; Protein arginine N-methyltransferase 4
Gene Symbols: CARM1
Molecular weight: 65,854 Da
Basal Isoelectric point: 6.25  Predict pI for various phosphorylation states
CST Pathways:  Histone Methylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CARM1

Protein Structure Not Found.


STRING  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  NURSA


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 R49-m2 DANGEIQrHAEQQAL
0 1 T171-p QDYVRTGtyQRAILQ
0 1 Y172-p DYVRTGtyQRAILQN
1 1 S216-p KIYAVEAsTMAQHAE
0 1 K227-ub QHAEVLVksNNLTDR
1 0 S228-p HAEVLVksNNLTDRI
0 1 K276-ac LESYLHAkKYLKPSG
0 1 K276-m1 LESYLHAkKYLKPSG
0 1 T413 TAPTEPLTHWYQVRC
1 0 S447-p LIANKRQsYDISIVA
0 4 K462-ub QVDQTGSkSSNLLDL
0 6 K470-ub SSNLLDLkNPFFRYT
  mouse

 
R50 DANGEIQRHAEQQAL
T172 QDYVRTGTYQRAILQ
Y173 DYVRTGTYQRAILQN
S217-p KIYAVEAsTMAQHAE
K228 QHAEVLVKsNNLTDR
S229-p HAEVLVKsNNLTDRI
K277 LESYLHAKKYLKPSG
K277 LESYLHAKKYLKPSG
T414-p TAPTEPLtHWYQVRC
S448 LIANKRQSYDISIVA
K463-ub QVDQTGSkSSNLLDL
K471-ub SSNLLDLkNPFFRYT
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.