CARM1_HUMAN
ID CARM1_HUMAN Reviewed; 608 AA.
AC Q86X55; A6NN38;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Histone-arginine methyltransferase CARM1;
DE EC=2.1.1.319 {ECO:0000269|PubMed:19405910};
DE AltName: Full=Coactivator-associated arginine methyltransferase 1;
DE AltName: Full=Protein arginine N-methyltransferase 4;
GN Name=CARM1; Synonyms=PRMT4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 194-608 (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-608 (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP METHYLATION OF ELAVL1.
RX PubMed=12237300; DOI=10.1074/jbc.m206187200;
RA Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A., Aswad D.W.,
RA Stallcup M.R., Laird-Offringa I.A.;
RT "Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing
RT protein, by CARM1. Coactivator-associated arginine methyltransferase.";
RL J. Biol. Chem. 277:44623-44630(2002).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15221992; DOI=10.1002/cncr.20327;
RA Hong H., Kao C., Jeng M.-H., Eble J.N., Koch M.O., Gardner T.A., Zhang S.,
RA Li L., Pan C.-X., Hu Z., MacLennan G.T., Cheng L.;
RT "Aberrant expression of CARM1, a transcriptional coactivator of androgen
RT receptor, in the development of prostate carcinoma and androgen-independent
RT status.";
RL Cancer 101:83-89(2004).
RN [7]
RP INTERACTION WITH NR1H4.
RX PubMed=15471871; DOI=10.1074/jbc.m410021200;
RA Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J.;
RT "Ligand-dependent activation of the farnesoid X-receptor directs arginine
RT methylation of histone H3 by CARM1.";
RL J. Biol. Chem. 279:54348-54357(2004).
RN [8]
RP METHYLATION OF EP300.
RX PubMed=15731352; DOI=10.1073/pnas.0407159102;
RA Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R.;
RT "Regulation of coactivator complex assembly and function by protein
RT arginine methylation and demethylimination.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005).
RN [9]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
RX PubMed=17005681; DOI=10.1128/jvi.00186-06;
RA Jeong S.J., Lu H., Cho W.K., Park H.U., Pise-Masison C., Brady J.N.;
RT "Coactivator-associated arginine methyltransferase 1 enhances
RT transcriptional activity of the human T-cell lymphotropic virus type 1 long
RT terminal repeat through direct interaction with Tax.";
RL J. Virol. 80:10036-10044(2006).
RN [10]
RP METHYLATION OF HISTONE H3, INTERACTION WITH RELA, AND FUNCTION.
RX PubMed=16497732; DOI=10.1210/me.2005-0365;
RA Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
RT "Coactivator-associated arginine methyltransferase-1 enhances nuclear
RT factor-kappaB-mediated gene transcription through methylation of histone H3
RT at arginine 17.";
RL Mol. Endocrinol. 20:1562-1573(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19405910; DOI=10.1042/bj20090268;
RA Lakowski T.M., Frankel A.;
RT "Kinetic analysis of human protein arginine N-methyltransferase 2:
RT formation of monomethyl- and asymmetric dimethyl-arginine residues on
RT histone H4.";
RL Biochem. J. 421:253-261(2009).
RN [13]
RP PHOSPHORYLATION AT SER-216, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=19843527; DOI=10.1074/jbc.m109.065524;
RA Feng Q., He B., Jung S.Y., Song Y., Qin J., Tsai S.Y., Tsai M.J.,
RA O'Malley B.W.;
RT "Biochemical control of CARM1 enzymatic activity by phosphorylation.";
RL J. Biol. Chem. 284:36167-36174(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 135-482 IN COMPLEX WITH SAM ANALOG
RP AND INHIBITORS, AND SAM BINDING SITES.
RX PubMed=21410432; DOI=10.1042/bj20102161;
RA Sack J.S., Thieffine S., Bandiera T., Fasolini M., Duke G.J., Jayaraman L.,
RA Kish K.F., Klei H.E., Purandare A.V., Rosettani P., Troiani S., Xie D.,
RA Bertrand J.A.;
RT "Structural basis for CARM1 inhibition by indole and pyrazole inhibitors.";
RL Biochem. J. 436:331-339(2011).
CC -!- FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino
CC nitrogens of arginyl residues in several proteins involved in DNA
CC packaging, transcription regulation, pre-mRNA splicing, and mRNA
CC stability. Recruited to promoters upon gene activation together with
CC histone acetyltransferases from EP300/P300 and p160 families,
CC methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric
CC dimethylarginine (H3R17me2a), leading to activate transcription via
CC chromatin remodeling. During nuclear hormone receptor activation and
CC TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either
CC one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and
CC NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During
CC myogenic transcriptional activation, acts together with NCOA3/ACTR as a
CC coactivator for MEF2C. During monocyte inflammatory stimulation, acts
CC together with EP300/P300 as a coactivator for NF-kappa-B. Acts as
CC coactivator for PPARG, promotes adipocyte differentiation and the
CC accumulation of brown fat tissue. Plays a role in the regulation of
CC pre-mRNA alternative splicing by methylation of splicing factors. Also
CC seems to be involved in p53/TP53 transcriptional activation. Methylates
CC EP300/P300, both at 'Arg-2142', which may loosen its interaction with
CC NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which
CC impairs its interaction with CREB and inhibits CREB-dependent
CC transcriptional activation. Also methylates arginine residues in RNA-
CC binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-
CC stabilizing properties and the half-life of their target mRNAs. Acts as
CC a transcriptional coactivator of ACACA/acetyl-CoA carboxylase by
CC enriching H3R17 methylation at its promoter, thereby positively
CC regulating fatty acid synthesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9WVG6, ECO:0000269|PubMed:16497732,
CC ECO:0000269|PubMed:19405910}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000269|PubMed:19405910};
CC -!- ACTIVITY REGULATION: Methylation of H3R17 (H3R17me) by CARM1 is
CC stimulated by preacetylation of H3 'Lys-18' (H3K18ac) H3 'Lys-23'
CC (H3K23ac) by EP300 and blocked by citrullination of H3 'Arg-17'
CC (H3R17ci) by PADI4. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with the C-terminus of
CC NCOA2/GRIP1, NCO3/ACTR and NCOA1/SRC1. Part of a complex consisting of
CC CARM1, EP300/P300 and NCOA2/GRIP1. Interacts with FLII, TP53, myogenic
CC factor MEF2, EP300/P300, TRIM24, CREBBP and CTNNB1. Identified in a
CC complex containing CARM1, TRIM24 and NCOA2/GRIP1. Interacts with
CC NCOA3/SRC3. Interacts with SNRPC (By similarity). Interacts with NR1H4.
CC Interacts with RELA. Interacts with SKP2 (By similarity). Interacts
CC (via PH domain-like fold) with C9orf72 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9WVG6, ECO:0000269|PubMed:15471871,
CC ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:21410432, ECO:0000305}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 protein Tax.
CC {ECO:0000269|PubMed:17005681}.
CC -!- INTERACTION:
CC Q86X55; P17676: CEBPB; NbExp=2; IntAct=EBI-2339854, EBI-969696;
CC Q86X55; Q96EY1: DNAJA3; NbExp=2; IntAct=EBI-2339854, EBI-356767;
CC Q86X55; Q6NYC1: JMJD6; NbExp=2; IntAct=EBI-2339854, EBI-8464037;
CC Q86X55; Q9Y6Q9: NCOA3; NbExp=13; IntAct=EBI-2339854, EBI-81196;
CC Q86X55; O43809: NUDT21; NbExp=2; IntAct=EBI-2339854, EBI-355720;
CC Q86X55; Q96PU8: QKI; NbExp=2; IntAct=EBI-2339854, EBI-945792;
CC Q86X55; Q92922: SMARCC1; NbExp=4; IntAct=EBI-2339854, EBI-355653;
CC Q86X55; Q05826: CEBPB; Xeno; NbExp=3; IntAct=EBI-2339854, EBI-7774198;
CC Q86X55; Q7ARE5: YPMT1.27c; Xeno; NbExp=2; IntAct=EBI-2339854, EBI-20592362;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19843527}. Cytoplasm
CC {ECO:0000269|PubMed:19843527}. Note=Mainly nuclear during the G1, S and
CC G2 phases of the cell cycle (PubMed:19843527). Cytoplasmic during
CC mitosis, after breakup of the nuclear membrane (PubMed:19843527).
CC {ECO:0000269|PubMed:19843527}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q86X55-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q86X55-1; Sequence=VSP_039876;
CC Name=2;
CC IsoId=Q86X55-2; Sequence=VSP_012506, VSP_012507;
CC -!- TISSUE SPECIFICITY: Overexpressed in prostate adenocarcinomas and high-
CC grade prostatic intraepithelial neoplasia.
CC {ECO:0000269|PubMed:15221992}.
CC -!- PTM: Auto-methylated on Arg-550. Methylation enhances transcription
CC coactivator activity. Methylation is required for its role in the
CC regulation of pre-mRNA alternative splicing (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-216 interferes with S-adenosyl-L-methionine
CC binding and strongly reduces methyltransferase activity (By
CC similarity). Phosphorylation at Ser-216 is strongly increased during
CC mitosis, and decreases rapidly to a very low, basal level after entry
CC into the G1 phase of the cell cycle. Phosphorylation at Ser-216 may
CC promote location in the cytosol. {ECO:0000250,
CC ECO:0000269|PubMed:19843527}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84156.1; -; Genomic_DNA.
DR EMBL; BC046240; AAH46240.1; -; mRNA.
DR EMBL; BC172490; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL833242; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS12250.1; -. [Q86X55-3]
DR RefSeq; NP_954592.1; NM_199141.1. [Q86X55-3]
DR RefSeq; XP_005259765.1; XM_005259708.4.
DR PDB; 2Y1W; X-ray; 2.10 A; A/B/C/D=135-482.
DR PDB; 2Y1X; X-ray; 2.40 A; A/B/C/D=135-482.
DR PDB; 4IKP; X-ray; 2.00 A; A/B/C/D=140-480.
DR PDB; 5DWQ; X-ray; 2.36 A; A/B/C/D=134-479.
DR PDB; 5DX0; X-ray; 2.05 A; A/B/C/D=134-479.
DR PDB; 5DX1; X-ray; 1.93 A; A/B/C/D=134-479.
DR PDB; 5DX8; X-ray; 1.94 A; A/B/C/D=134-479.
DR PDB; 5DXA; X-ray; 2.07 A; A/B/C/D=134-479.
DR PDB; 5DXJ; X-ray; 1.95 A; A/B/C/D=134-479.
DR PDB; 5U4X; X-ray; 1.88 A; A/B/C/D=140-480.
DR PDB; 6ARJ; X-ray; 1.92 A; A/B/C/D=134-479.
DR PDB; 6ARV; X-ray; 2.00 A; A/B/C/D=134-479.
DR PDB; 6D2L; X-ray; 2.00 A; A/B/C/D/E/F=146-489.
DR PDB; 6DVR; X-ray; 1.54 A; A/B=146-489.
DR PDB; 6IZQ; X-ray; 2.45 A; A/B/C/D=145-477.
DR PDB; 6S70; X-ray; 2.30 A; A/B/C/D=135-479.
DR PDB; 6S71; X-ray; 2.06 A; A/B/C/D=135-479.
DR PDB; 6S74; X-ray; 2.10 A; A/B/C/D=135-479.
DR PDB; 6S77; X-ray; 2.12 A; A/B/C/D=135-479.
DR PDB; 6S79; X-ray; 2.10 A; A/B/C/D=135-479.
DR PDB; 6S7A; X-ray; 1.86 A; A/B/C/D=135-479.
DR PDB; 6S7B; X-ray; 2.66 A; A/B/C/D=135-479.
DR PDB; 6S7C; X-ray; 2.30 A; A/B/C/D=135-479.
DR PDB; 7FAI; X-ray; 2.10 A; A/B/C/D=142-477.
DR PDB; 7FAJ; X-ray; 2.25 A; A/B/C/D=142-477.
DR PDBsum; 2Y1W; -.
DR PDBsum; 2Y1X; -.
DR PDBsum; 4IKP; -.
DR PDBsum; 5DWQ; -.
DR PDBsum; 5DX0; -.
DR PDBsum; 5DX1; -.
DR PDBsum; 5DX8; -.
DR PDBsum; 5DXA; -.
DR PDBsum; 5DXJ; -.
DR PDBsum; 5U4X; -.
DR PDBsum; 6ARJ; -.
DR PDBsum; 6ARV; -.
DR PDBsum; 6D2L; -.
DR PDBsum; 6DVR; -.
DR PDBsum; 6IZQ; -.
DR PDBsum; 6S70; -.
DR PDBsum; 6S71; -.
DR PDBsum; 6S74; -.
DR PDBsum; 6S77; -.
DR PDBsum; 6S79; -.
DR PDBsum; 6S7A; -.
DR PDBsum; 6S7B; -.
DR PDBsum; 6S7C; -.
DR PDBsum; 7FAI; -.
DR PDBsum; 7FAJ; -.
DR AlphaFoldDB; Q86X55; -.
DR SMR; Q86X55; -.
DR BioGRID; 115760; 256.
DR CORUM; Q86X55; -.
DR DIP; DIP-44071N; -.
DR IntAct; Q86X55; 86.
DR MINT; Q86X55; -.
DR STRING; 9606.ENSP00000325690; -.
DR BindingDB; Q86X55; -.
DR ChEMBL; CHEMBL5406; -.
DR GuidetoPHARMACOLOGY; 1255; -.
DR GlyGen; Q86X55; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86X55; -.
DR PhosphoSitePlus; Q86X55; -.
DR BioMuta; CARM1; -.
DR DMDM; 308153622; -.
DR EPD; Q86X55; -.
DR jPOST; Q86X55; -.
DR MassIVE; Q86X55; -.
DR MaxQB; Q86X55; -.
DR PaxDb; Q86X55; -.
DR PeptideAtlas; Q86X55; -.
DR PRIDE; Q86X55; -.
DR ProteomicsDB; 70241; -. [Q86X55-3]
DR ProteomicsDB; 70242; -. [Q86X55-1]
DR ProteomicsDB; 70243; -. [Q86X55-2]
DR Antibodypedia; 25589; 654 antibodies from 40 providers.
DR DNASU; 10498; -.
DR Ensembl; ENST00000327064.9; ENSP00000325690.4; ENSG00000142453.12. [Q86X55-3]
DR Ensembl; ENST00000344150.8; ENSP00000340934.3; ENSG00000142453.12. [Q86X55-1]
DR GeneID; 10498; -.
DR KEGG; hsa:10498; -.
DR MANE-Select; ENST00000327064.9; ENSP00000325690.4; NM_199141.2; NP_954592.1.
DR UCSC; uc002mpz.4; human. [Q86X55-3]
DR CTD; 10498; -.
DR DisGeNET; 10498; -.
DR GeneCards; CARM1; -.
DR HGNC; HGNC:23393; CARM1.
DR HPA; ENSG00000142453; Tissue enhanced (skeletal).
DR MIM; 603934; gene.
DR neXtProt; NX_Q86X55; -.
DR OpenTargets; ENSG00000142453; -.
DR PharmGKB; PA134959553; -.
DR VEuPathDB; HostDB:ENSG00000142453; -.
DR eggNOG; KOG1500; Eukaryota.
DR GeneTree; ENSGT00940000160377; -.
DR HOGENOM; CLU_017375_0_1_1; -.
DR InParanoid; Q86X55; -.
DR OMA; KWLKPQG; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q86X55; -.
DR TreeFam; TF323332; -.
DR BioCyc; MetaCyc:HS13925-MON; -.
DR BRENDA; 2.1.1.319; 2681.
DR PathwayCommons; Q86X55; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q86X55; -.
DR SIGNOR; Q86X55; -.
DR BioGRID-ORCS; 10498; 140 hits in 1102 CRISPR screens.
DR ChiTaRS; CARM1; human.
DR GenomeRNAi; 10498; -.
DR Pharos; Q86X55; Tchem.
DR PRO; PR:Q86X55; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q86X55; protein.
DR Bgee; ENSG00000142453; Expressed in hindlimb stylopod muscle and 191 other tissues.
DR ExpressionAtlas; Q86X55; baseline and differential.
DR Genevisible; Q86X55; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; TAS:AgBase.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035642; F:histone methyltransferase activity (H3-R17 specific); ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:CACAO.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:MGI.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034971; P:histone H3-R17 methylation; ISS:UniProtKB.
DR GO; GO:0034970; P:histone H3-R2 methylation; IMP:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:2000171; P:negative regulation of dendrite development; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1902415; P:regulation of mRNA binding; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR020989; Histone-Arg_MeTrfase_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF11531; CARM1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Cytoplasm; Host-virus interaction; Methylation; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..608
FT /note="Histone-arginine methyltransferase CARM1"
FT /id="PRO_0000212338"
FT DOMAIN 146..453
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 27..138
FT /note="Interaction with C9orf72"
FT /evidence="ECO:0000250|UniProtKB:Q9WVG6"
FT REGION 346..379
FT /note="Required for nuclear translocation"
FT /evidence="ECO:0000250|UniProtKB:Q9WVG6"
FT REGION 499..608
FT /note="Transactivation domain"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 192
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 214
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 271
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19843527"
FT MOD_RES 550
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVG6"
FT VAR_SEQ 369..384
FT /note="RIEIPFKFHMLHSGLV -> SACLASPAATALCLPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012506"
FT VAR_SEQ 385..608
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012507"
FT VAR_SEQ 539..561
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039876"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:6S7A"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:6DVR"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:6DVR"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6DVR"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:6DVR"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:6DVR"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:6DVR"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 369..380
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 382..396
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 417..428
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 433..443
FT /evidence="ECO:0007829|PDB:6DVR"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 447..456
FT /evidence="ECO:0007829|PDB:6DVR"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:6DVR"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:6DVR"
SQ SEQUENCE 608 AA; 65854 MW; 094AC60D4A70B263 CRC64;
MAAAAAAVGP GAGGAGSAVP GGAGPCATVS VFPGARLLTI GDANGEIQRH AEQQALRLEV
RAGPDSAGIA LYSHEDVCVF KCSVSRETEC SRVGKQSFII TLGCNSVLIQ FATPNDFCSF
YNILKTCRGH TLERSVFSER TEESSAVQYF QFYGYLSQQQ NMMQDYVRTG TYQRAILQNH
TDFKDKIVLD VGCGSGILSF FAAQAGARKI YAVEASTMAQ HAEVLVKSNN LTDRIVVIPG
KVEEVSLPEQ VDIIISEPMG YMLFNERMLE SYLHAKKYLK PSGNMFPTIG DVHLAPFTDE
QLYMEQFTKA NFWYQPSFHG VDLSALRGAA VDEYFRQPVV DTFDIRILMA KSVKYTVNFL
EAKEGDLHRI EIPFKFHMLH SGLVHGLAFW FDVAFIGSIM TVWLSTAPTE PLTHWYQVRC
LFQSPLFAKA GDTLSGTCLL IANKRQSYDI SIVAQVDQTG SKSSNLLDLK NPFFRYTGTT
PSPPPGSHYT SPSENMWNTG STYNLSSGMA VAGMPTAYDL SSVIASGSSV GHNNLIPLAN
TGIVNHTHSR MGSIMSTGIV QGSSGAQGSG GGSTSAHYAV NSQFTMGGPA ISMASPMSIP
TNTMHYGS
