Reviewed,
UniProtKB/Swiss-Prot Q86X55 (CARM1_HUMAN)
Last modified
November 25, 2008.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histone-arginine methyltransferase CARM1 EC=2.1.1.125 EC=2.1.1.- Alternative name(s): Protein arginine N-methyltransferase 4 Coactivator-associated arginine methyltransferase 1 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 585 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (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 structure | 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 | |
| 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. |
| Sequence similarities | Belongs to the protein arginine N-methyltransferase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Host-virus interaction Transcription Transcription regulation |
| Cellular component | Cytoplasm Nucleus |
| Coding sequence diversity | Alternative splicing |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Chromatin regulator Methyltransferase Transferase |
Gene Ontology (GO) | |
| Biological process | histone methylation Inferred from sequence or structural similarity. Source: UniProtKB interspecies interaction between organismsInferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependentInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | cytoplasm Ref.5 Inferred from direct assay. Source: UniProtKB nucleus Ref.5Inferred from direct assay. Source: UniProtKB |
| Molecular function | histone-arginine N-methyltransferase activity Inferred from electronic annotation. Source: EC transcription coactivator activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q86X55-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q86X55-2) The sequence of this isoform differs from the canonical sequence as follows: 369-412: RIEIPFKFHM...WLSTAPTEPL → SACLASPAAT...SGLTLLSSAP 413-585: Missing. | ||||||
| Notes: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 585 | 585 | Histone-arginine methyltransferase CARM1 | PRO_0000212338 | |||||
Regions | |||||||||
| Region | 499 – 585 | 87 | Transactivation domain By similarity | ||||||
Sites | |||||||||
| Binding site | 159 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 168 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 192 | 1 | S-adenosyl-L-methionine; via carbonyl oxygen By similarity | ||||||
| Binding site | 214 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 243 | 1 | S-adenosyl-L-methionine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 369 – 412 | 44 | RIEIP…PTEPL → SACLASPAATALCLPGKSHS NSTCCIQGWSTAWLSGLTLL SSAP in isoform 2. | VSP_012506 | |||||
| Alternative sequence | 413 – 585 | 173 | Missing in isoform 2. | VSP_012507 | |||||
Experimental info | |||||||||
| Sequence conflict | 186 | 1 | K → Q in BU176535. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | The MGC Project Team Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-203 (ISOFORMS 1/2). Tissue: Retinoblastoma. |
| [2] | The German cDNA consortium Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-585 (ISOFORM 2). Tissue: Amygdala. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 194-585 (ISOFORM 1). Tissue: Skin. |
| [4] | "Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase." Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W., Stallcup M.R., Laird-Offringa I.A. J. Biol. Chem. 277:44623-44630(2002) [PubMed: 12237300] [Abstract] Cited for: METHYLATION OF ELAVL1. |
| [5] | "Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status." 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. Cancer 101:83-89(2004) [PubMed: 15221992] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION. |
| [6] | "Ligand-dependent activation of the farnesoid X-receptor directs arginine methylation of histone H3 by CARM1." Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J. J. Biol. Chem. 279:54348-54357(2004) [PubMed: 15471871] [Abstract] Cited for: INTERACTION WITH NR1H4. |
| [7] | "Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination." Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R. Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005) [PubMed: 15731352] [Abstract] Cited for: METHYLATION OF EP300. |
| [8] | "Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17." Miao F., Li S., Chavez V., Lanting L., Natarajan R. Mol. Endocrinol. 20:1562-1573(2006) [PubMed: 16497732] [Abstract] Cited for: METHYLATION OF HISTONE H3, INTERACTION WITH RELA, FUNCTION. |
| [9] | "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." Jeong S.J., Lu H., Cho W.K., Park H.U., Pise-Masison C., Brady J.N. J. Virol. 80:10036-10044(2006) [PubMed: 17005681] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX-1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| BU176535 mRNA. No translation available. AL833242 mRNA. No translation available. BC046240 mRNA. Translation: AAH46240.1. | |
| UniGene | Hs.371416 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OR8 based on UniProtKB Q63009. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q86X55. |
Genome annotation databases | |
| Ensembl | ENSG00000142453. Homo sapiens. [Contig view] |
Organism-specific databases | |
| H-InvDB | HIX0014757. |
| HGNC | HGNC:23393. CARM1. |
| MIM | 603934. gene. |
| PharmGKB | PA134959553. |
| GenAtlas | Search... |
| GeneCards | Search... |
Phylogenomic databases | |
| HOVERGEN | Q86X55. |
Gene expression databases | |
| CleanEx | HS_CARM1. |
| GermOnline | ENSG00000142453. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR013216. Methyltransf_11. [Graphical view] |
| Pfam | PF08241. Methyltransf_11. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | CARM1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q86X55 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 19 Human chromosome 19: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


