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UniProtKB/Swiss-Prot entry Q86X55


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CARM1_HUMAN
Primary accession number Q86X55
Secondary accession numbers None
Integrated into Swiss-Prot on January 4, 2005
Sequence was last modified on January 4, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 47)
Name and origin of the protein
Protein name Histone-arginine methyltransferase CARM1
Synonyms EC 2.1.1.125
EC 2.1.1.-
Protein arginine N-methyltransferase 4
Coactivator-associated arginine methyltransferase 1
Gene name
Name: CARM1
Synonyms: PRMT4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-203 (ISOFORMS 1/2).
TISSUE=Retinoblastoma;
The MGC Project Team;
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-585 (ISOFORM 2).
TISSUE=Amygdala;
The German cDNA consortium;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 194-585 (ISOFORM 1).
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
METHYLATION OF ELAVL1.
DOI=10.1074/jbc.M206187200; PubMed=12237300 [NCBI, ExPASy, EBI, Israel, Japan]
Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W., Stallcup M.R., Laird-Offringa I.A.;
"Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase.";
J. Biol. Chem. 277:44623-44630(2002).
[5]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
DOI=10.1002/cncr.20327; PubMed=15221992 [NCBI, ExPASy, EBI, Israel, Japan]
Hong H., Kao C., Jeng M.-H., Eble J.N., Koch M.O., Gardner T.A., Zhang S., Li L., Pan C.-X., Hu Z., MacLennan G.T., Cheng L.;
"Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status.";
Cancer 101:83-89(2004).
[6]
INTERACTION WITH NR1H4.
DOI=10.1074/jbc.M410021200; PubMed=15471871 [NCBI, ExPASy, EBI, Israel, Japan]
Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J.;
"Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1.";
J. Biol. Chem. 279:54348-54357(2004).
[7]
METHYLATION OF EP300.
DOI=10.1073/pnas.0407159102; PubMed=15731352 [NCBI, ExPASy, EBI, Israel, Japan]
Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R.;
"Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination.";
Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005).
[8]
METHYLATION OF HISTONE H3, INTERACTION WITH RELA, AND FUNCTION.
DOI=10.1210/me.2005-0365; PubMed=16497732 [NCBI, ExPASy, EBI, Israel, Japan]
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. 20:1562-1573(2006).
[9]
INTERACTION WITH HTLV-1 TAX-1.
DOI=10.1128/JVI.00186-06; PubMed=17005681 [NCBI, ExPASy, EBI, Israel, Japan]
Jeong S.J., Lu H., Cho W.K., Park H.U., Pise-Masison C., Brady J.N.;
"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. 80:10036-10044(2006).
Comments
  • FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, 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' and 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. 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.
  • CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine.
  • SUBUNIT: Homodimer (Probable). Interacts with the C-terminus of NCOA2/GRIP1, NCO3/ACTR and NCOA1/SRC1. Part of a complex consisting of CARM1, EP300/P300 and NCOA2/GRIP1. Interacts with FLII, TP53, myogenic factor MEF2, EP300/P300, CREBBP and CTNNB1. Interacts with SNRPC (By similarity). Interacts with NR1H4. Interacts with RELA. Interacts with HTLV-1 Tax-1.
  • SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ86X55-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ86X55-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_012506, VSP_012507.
  • TISSUE SPECIFICITY: Overexpressed in prostate adenocarcinomas and high-grade prostatic intraepithelial neoplasia.
  • MISCELLANEOUS: Methylation of H3-R17 by CARM1 is stimulated by preacetylation of H3-K18/H3-K23 by EP300 and blocked by citrullination of H3-R17 by PADI4 (By similarity).
  • SIMILARITY: Belongs to the protein arginine N-methyltransferase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BU176535; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
AL833242; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
BC046240; AAH46240.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Hs.371416
3D structure databases
HSSP Q63009; 1OR8. [HSSP ENTRY / PDB]
ModBase Q86X55.
PTM databases
PhosphoSite Q86X55; -.
Organism-specific databases
H-InvDB HIX0014757; -.
HGNC HGNC:23393; CARM1.
GenAtlas CARM1.
MIM 603934; gene. [NCBI / EBI]
PharmGKB PA134959553; -.
GeneCards Q86X55.
Gene expression databases
CleanEx HS_CARM1; -.
GermOnline ENSG00000142453; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0008276; Molecular function: protein methyltransferase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0003713; Molecular function: transcription coactivator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0016571; Biological process: histone methylation (inferred from sequence or structural similarity from UniProtKB).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR013216; Methyltransf_11.
Graphical view of domain structure.
Pfam PF08241; Methyltransf_11; 1.
Pfam graphical view of domain structure.
BLOCKS Q86X55.
Genome annotation databases
Ensembl ENSG00000142453; Homo sapiens. [Contig view]
Phylogenomic databases
HOVERGEN Q86X55; -.
Other
SOURCE CARM1; Homo sapiens.
ProtoNet Q86X55.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Chromatin regulator; Cytoplasm; Host-virus interaction; Methyltransferase; Nucleus; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   585  585     Histone-arginine methyltransferase CARM1. PRO_0000212338
REGION   499   585  87     Transactivation domain (By similarity). 
BINDING   159   159        S-adenosyl-L-methionine (By similarity). 
BINDING   168   168        S-adenosyl-L-methionine (By similarity). 
BINDING   192   192        S-adenosyl-L-methionine; via carbonyl oxygen (By similarity). 
BINDING   214   214        S-adenosyl-L-methionine (By similarity). 
BINDING   243   243        S-adenosyl-L-methionine (By similarity). 
VAR_SEQ   369   412        RIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTA PTEPL -> SACLASPAATALCLPGKSHSNSTCCIQGWSTAWLSGLTL LSSAP (in isoform 2). VSP_012506
VAR_SEQ   413   585        Missing (in isoform 2). VSP_012507
CONFLICT   186   186        K -> Q (in Ref. 2; BU176535). 
Sequence information
Length: 585 AA [This is the length of the unprocessed precursor] Molecular weight: 63460 Da [This is the MW of the unprocessed precursor] CRC64: 15C6720FBEB864FE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAAAAAVGP GAGGAGSAVP GGAGPCATVS VFPGARLLTI GDANGEIQRH AEQQALRLEV 

        70         80         90        100        110        120 
RAGPDSAGIA LYSHEDVCVF KCSVSRETEC SRVGKQSFII TLGCNSVLIQ FATPNDFCSF 

       130        140        150        160        170        180 
YNILKTCRGH TLERSVFSER TEESSAVQYF QFYGYLSQQQ NMMQDYVRTG TYQRAILQNH 

       190        200        210        220        230        240 
TDFKDKIVLD VGCGSGILSF FAAQAGARKI YAVEASTMAQ HAEVLVKSNN LTDRIVVIPG 

       250        260        270        280        290        300 
KVEEVSLPEQ VDIIISEPMG YMLFNERMLE SYLHAKKYLK PSGNMFPTIG DVHLAPFTDE 

       310        320        330        340        350        360 
QLYMEQFTKA NFWYQPSFHG VDLSALRGAA VDEYFRQPVV DTFDIRILMA KSVKYTVNFL 

       370        380        390        400        410        420 
EAKEGDLHRI EIPFKFHMLH SGLVHGLAFW FDVAFIGSIM TVWLSTAPTE PLTHWYQVRC 

       430        440        450        460        470        480 
LFQSPLFAKA GDTLSGTCLL IANKRQSYDI SIVAQVDQTG SKSSNLLDLK NPFFRYTGTT 

       490        500        510        520        530        540 
PSPPPGSHYT SPSENMWNTG STYNLSSGMA VAGMPTAYDL SSVIASGSSV GHNNLIPLGS 

       550        560        570        580 
SGAQGSGGGS TSAHYAVNSQ FTMGGPAISM ASPMSIPTNT MHYGS 

Q86X55 in FASTA format

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