CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016291
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
227QHAEVLVKSNNLTDRubiquitination[1]
470SSNLLDLKNPFFRYTubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
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 activate 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 499 608 Transactivation domain (By similarity).
 BINDING 159 159 S-adenosyl-L-methionine.
 BINDING 168 168 S-adenosyl-L-methionine.
 BINDING 192 192 S-adenosyl-L-methionine; via carbonyl
 BINDING 214 214 S-adenosyl-L-methionine.
 BINDING 243 243 S-adenosyl-L-methionine.
 BINDING 271 271 S-adenosyl-L-methionine.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 216 216 Phosphoserine.
 MOD_RES 550 550 Dimethylated arginine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; Host-virus interaction; Methylation; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 608 AA 
Protein Sequence
MAAAAAAVGP GAGGAGSAVP GGAGPCATVS VFPGARLLTI GDANGEIQRH AEQQALRLEV 60
RAGPDSAGIA LYSHEDVCVF KCSVSRETEC SRVGKQSFII TLGCNSVLIQ FATPNDFCSF 120
YNILKTCRGH TLERSVFSER TEESSAVQYF QFYGYLSQQQ NMMQDYVRTG TYQRAILQNH 180
TDFKDKIVLD VGCGSGILSF FAAQAGARKI YAVEASTMAQ HAEVLVKSNN LTDRIVVIPG 240
KVEEVSLPEQ VDIIISEPMG YMLFNERMLE SYLHAKKYLK PSGNMFPTIG DVHLAPFTDE 300
QLYMEQFTKA NFWYQPSFHG VDLSALRGAA VDEYFRQPVV DTFDIRILMA KSVKYTVNFL 360
EAKEGDLHRI EIPFKFHMLH SGLVHGLAFW FDVAFIGSIM TVWLSTAPTE PLTHWYQVRC 420
LFQSPLFAKA GDTLSGTCLL IANKRQSYDI SIVAQVDQTG SKSSNLLDLK NPFFRYTGTT 480
PSPPPGSHYT SPSENMWNTG STYNLSSGMA VAGMPTAYDL SSVIASGSSV GHNNLIPLGS 540
SGAQGSGGGS TSAHYAVNSQ FTMGGPAISM ASPMSIPTNT MHYGS 585 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0008013; F:beta-catenin binding; TAS:AgBase.
 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:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0060350; P:endochondral bone morphogenesis; IEA:Compara.
 GO:0034970; P:histone H3-R2 methylation; IMP:UniProtKB.
 GO:0030520; P:intracellular estrogen receptor signaling pathway; IEA:Compara.
 GO:0032091; P:negative regulation of protein binding; IEA:Compara.
 GO:0009405; P:pathogenesis; IEA:InterPro.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 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; ISS:UniProtKB.
 GO:0051591; P:response to cAMP; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR025799; Arg_MeTrfase.
 IPR025797; Arg_MeTrfase_CARM1.
 IPR020989; Histone-Arg_MeTrfase_N. 
Pfam
 PF11531; CARM1
 PF05185; PRMT5 
SMART
  
PROSITE
  
PRINTS