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Showing Protein Histone-arginine methyltransferase CARM1 (HMDBP09009)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 3 metabolites
Identification
HMDB Protein ID HMDBP09009
Secondary Accession Numbers
  • 14750
Name Histone-arginine methyltransferase CARM1
Synonyms
  1. Coactivator-associated arginine methyltransferase 1
  2. Protein arginine N-methyltransferase 4
Gene Name CARM1
Protein Type Unknown
Biological Properties
General Function Involved in pathogenesis
Specific 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. 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.
Pathways Not Available
Reactions
S-Adenosylmethionine + arginine-[histone] → S-Adenosylhomocysteine + N(omega)-methyl-arginine-[histone] details
GO Classification
Biological Process
small molecule metabolic process
positive regulation of cell proliferation
virus-host interaction
endochondral bone morphogenesis
histone H3-R2 methylation
intracellular steroid hormone receptor signaling pathway
negative regulation of protein binding
pathogenesis
positive regulation of fat cell differentiation
regulation of growth plate cartilage chondrocyte proliferation
regulation of intracellular estrogen receptor signaling pathway
cellular lipid metabolic process
regulation of transcription, DNA-dependent
transcription, DNA-dependent
response to cAMP
Cellular Component
cytosol
nucleoplasm
Component
cell part
intracellular part
cytoplasm
Function
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
Molecular Function
protein-arginine omega-N asymmetric methyltransferase activity
beta-catenin binding
histone acetyl-lysine binding
histone methyltransferase activity (H3-R17 specific)
ligand-dependent nuclear receptor transcription coactivator activity
transcription regulatory region DNA binding
Process
pathogenesis
multi-organism process
Cellular Location
  1. Nucleus
  2. Cytoplasm
Gene Properties
Chromosome Location 19
Locus 19p13.2
SNPs CARM1
Gene Sequence 
>1827 bp
ATGGCAGCGGCGGCGGCGGCGGTGGGGCCGGGCGCGGGCGGCGCGGGGTCGGCGGTCCCG
GGCGGCGCGGGGCCCTGCGCTACCGTGTCGGTGTTCCCCGGCGCCCGCCTCCTCACCATC
GGCGACGCGAACGGCGAGATCCAGCGGCACGCGGAGCAGCAGGCGCTGCGCCTCGAGGTG
CGCGCCGGCCCGGACTCGGCGGGCATCGCCCTCTACAGCCATGAAGATGTGTGTGTCTTT
AAGTGCTCAGTGTCCCGAGAGACAGAGTGCAGCCGTGTGGGCAAGCAGTCCTTCATCATC
ACCCTGGGCTGCAACAGCGTCCTCATCCAGTTCGCCACACCCAACGATTTCTGTTCCTTC
TACAACATCCTGAAAACCTGCCGGGGCCACACCCTGGAGCGGTCTGTGTTCAGCGAGCGG
ACGGAGGAGTCTTCTGCCGTGCAGTACTTCCAGTTTTATGGCTACCTGTCCCAGCAGCAG
AACATGATGCAGGACTACGTGCGGACAGGCACCTACCAGCGCGCCATCCTGCAAAACCAC
ACCGACTTCAAGGACAAGATCGTTCTTGATGTTGGCTGTGGCTCTGGGATCCTGTCGTTT
TTTGCCGCCCAAGCTGGAGCACGGAAAATCTACGCGGTGGAGGCCAGCACCATGGCCCAG
CACGCTGAGGTCTTGGTGAAGAGTAACAACCTGACGGACCGCATCGTGGTCATCCCGGGC
AAGGTGGAGGAGGTGTCACTCCCCGAGCAGGTGGACATCATCATCTCGGAGCCCATGGGC
TACATGCTCTTCAACGAGCGCATGCTGGAGAGCTACCTCCACGCCAAGAAGTACCTGAAG
CCCAGCGGAAACATGTTTCCTACCATTGGTGACGTCCACCTTGCACCCTTCACGGATGAA
CAGCTCTACATGGAGCAGTTCACCAAGGCCAACTTCTGGTACCAGCCATCTTTCCATGGA
GTGGACCTGTCGGCCCTCCGAGGTGCCGCGGTGGATGAGTATTTCCGGCAGCCTGTGGTG
GACACATTTGACATCCGGATCCTGATGGCCAAGTCTGTCAAGTACACGGTGAACTTCTTA
GAAGCCAAAGAAGGAGATTTGCACAGGATAGAAATCCCATTCAAATTCCACATGCTGCAT
TCAGGGCTGGTCCACGGCCTGGCTTTCTGGTTTGACGTTGCTTTCATCGGCTCCATAATG
ACCGTGTGGCTGTCCACAGCCCCGACAGAGCCCCTGACCCACTGGTACCAGGTGCGGTGC
CTGTTCCAGTCACCACTGTTCGCCAAGGCAGGGGACACGCTCTCAGGGACATGTCTGCTT
ATTGCCAACAAAAGACAGAGCTACGACATCAGTATTGTGGCCCAGGTGGACCAGACCGGC
TCCAAGTCCAGTAACCTCCTGGATCTGAAAAACCCCTTCTTTAGATACACGGGCACAACG
CCCTCACCCCCACCCGGCTCCCACTACACATCTCCCTCGGAAAACATGTGGAACACGGGC
AGCACCTACAACCTCAGCAGCGGGATGGCCGTGGCAGGGATGCCGACCGCCTATGACTTG
AGCAGTGTTATTGCCAGTGGCTCCAGCGTGGGCCACAACAACCTGATTCCTTTAGCCAAC
ACGGGGATTGTCAATCACACCCACTCCCGGATGGGCTCCATAATGAGCACGGGGATTGTC
CAAGGGTCCTCCGGCGCCCAGGGCAGTGGTGGTGGCAGCACGAGTGCCCACTATGCAGTC
AACAGCCAGTTCACCATGGGCGGCCCCGCCATCTCCATGGCGTCGCCCATGTCCATCCCG
ACCAACACCATGCACTACGGGAGCTAG
Protein Properties
Number of Residues 608
Molecular Weight 65853.185
Theoretical pI 6.733
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Histone-arginine methyltransferase CARM1
MAAAAAAVGPGAGGAGSAVPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEV
RAGPDSAGIALYSHEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSF
YNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNH
TDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPG
KVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDE
QLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFL
EAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRC
LFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTT
PSPPPGSHYTSPSENMWNTGSTYNLSSGMAVAGMPTAYDLSSVIASGSSVGHNNLIPLAN
TGIVNHTHSRMGSIMSTGIVQGSSGAQGSGGGSTSAHYAVNSQFTMGGPAISMASPMSIP
TNTMHYGS
GenBank ID Protein 40288288
UniProtKB/Swiss-Prot ID Q86X55
UniProtKB/Swiss-Prot Entry Name CARM1_HUMAN
PDB IDs
GenBank Gene ID NM_199141.1
GeneCard ID CARM1
GenAtlas ID CARM1
HGNC ID HGNC:23393
References
General References
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  2. Lee YH, Coonrod SA, Kraus WL, Jelinek MA, Stallcup MR: Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination. Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3611-6. Epub 2005 Feb 24. [PubMed:15731352 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  5. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed:15057824 ]
  6. Ananthanarayanan M, Li S, Balasubramaniyan N, Suchy FJ, Walsh MJ: Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1. J Biol Chem. 2004 Dec 24;279(52):54348-57. Epub 2004 Oct 6. [PubMed:15471871 ]
  7. Li H, Park S, Kilburn B, Jelinek MA, Henschen-Edman A, Aswad DW, Stallcup MR, Laird-Offringa IA: Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase. J Biol Chem. 2002 Nov 22;277(47):44623-30. Epub 2002 Sep 16. [PubMed:12237300 ]
  8. Hong H, Kao C, Jeng MH, Eble JN, Koch MO, Gardner TA, Zhang S, Li L, Pan CX, Hu Z, MacLennan GT, Cheng L: Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status. Cancer. 2004 Jul 1;101(1):83-9. [PubMed:15221992 ]
  9. Jeong SJ, Lu H, Cho WK, Park HU, Pise-Masison C, Brady JN: Coactivator-associated arginine methyltransferase 1 enhances transcriptional activity of the human T-cell lymphotropic virus type 1 long terminal repeat through direct interaction with Tax. J Virol. 2006 Oct;80(20):10036-44. [PubMed:17005681 ]
  10. Miao F, Li S, Chavez V, Lanting L, Natarajan R: Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17. Mol Endocrinol. 2006 Jul;20(7):1562-73. Epub 2006 Feb 23. [PubMed:16497732 ]