CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013266
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone-arginine methyltransferase CARM1 
Protein Synonyms/Alias
 Coactivator-associated arginine methyltransferase 1; Protein arginine N-methyltransferase 4 
Gene Name
 Carm1 
Gene Synonyms/Alias
 Prmt4 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
471SSNLLDLKNPFFRYTubiquitination[1]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 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. 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 activates transcription via chromatin remodeling. 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. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/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/TP53 transcriptional activation. 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. 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. 
Sequence Annotation
 REGION 500 651 Transactivation domain (By similarity).
 BINDING 160 160 S-adenosyl-L-methionine.
 BINDING 169 169 S-adenosyl-L-methionine.
 BINDING 193 193 S-adenosyl-L-methionine; via carbonyl
 BINDING 215 215 S-adenosyl-L-methionine.
 BINDING 244 244 S-adenosyl-L-methionine.
 BINDING 272 272 S-adenosyl-L-methionine.
 MOD_RES 217 217 Phosphoserine (By similarity).
 MOD_RES 551 551 Dimethylated arginine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; Methylation; Methyltransferase; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 651 AA 
Protein Sequence
MAAAAATAVG PGAGSAGVAG PGGAGPCATV SVFPGARLLT IGDANGEIQR HAEQQALRLE 60
VRAGPDAAGI ALYSHEDVCV FKCSVSRETE CSRVGRQSFI ITLGCNSVLI QFATPHDFCS 120
FYNILKTCRG HTLERSVFSE RTEESSAVQY FQFYGYLSQQ QNMMQDYVRT GTYQRAILQN 180
HTDFKDKIVL DVGCGSGILS FFAAQAGARK IYAVEASTMA QHAEVLVKSN NLTDRIVVIP 240
GKVEEVSLPE QVDIIISEPM GYMLFNERML ESYLHAKKYL KPSGNMFPTI GDVHLAPFTD 300
EQLYMEQFTK ANFWYQPSFH GVDLSALRGA AVDEYFRQPV VDTFDIRILM AKSVKYTVNF 360
LEAKEGDLHR IEIPFKFHML HSGLVHGLAF WFDVAFIGSI MTVWLSTAPT EPLTHWYQVR 420
CLFQSPLFAK AGDTLSGTCL LIANKRQSYD ISIVAQVDQT GSKSSNLLDL KNPFFRYTGT 480
TPSPPPGSHY TSPSENMWNT GSTYNLSSGV AVAGMPTAYD LSSVIAGGSS VGHNNLIPLA 540
NTGIVNHTHS RMGSIMSTGI VQGNRVAGPW AGDLPPGLRT RSSYQWGPGR LRGHAGSSVP 600
MTCPTGSSGA QGGGGSSSAH YAVNNQFTMG GPAISMASPM SIPTNTMHYG S 651 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005634; C:nucleus; IDA:RGD.
 GO:0070577; F:histone acetyl-lysine binding; ISS:UniProtKB.
 GO:0035642; F:histone methyltransferase activity (H3-R17 specific); ISS:UniProtKB.
 GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB.
 GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISS:UniProtKB.
 GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
 GO:0060350; P:endochondral bone morphogenesis; IEA:Compara.
 GO:0034970; P:histone H3-R2 methylation; IEA:Compara.
 GO:0030520; P:intracellular estrogen receptor signaling pathway; IEA:Compara.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0032091; P:negative regulation of protein binding; IEA:Compara.
 GO:0009405; P:pathogenesis; IEA:InterPro.
 GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
 GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
 GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; IEA:Compara.
 GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0051591; P:response to cAMP; IDA:RGD.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR025799; Arg_MeTrfase.
 IPR025797; Arg_MeTrfase_CARM1.
 IPR020989; Histone-Arg_MeTrfase_N. 
Pfam
 PF11531; CARM1
 PF05185; PRMT5 
SMART
  
PROSITE
  
PRINTS