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Histone-arginine methyltransferase CARM1 (EC 2.1.1.319) (Coactivator-associated arginine methyltransferase 1) (Protein arginine N-methyltransferase 4)

 CARM1_MOUSE             Reviewed;         608 AA.
Q9WVG6; Q3TYB9; Q8K1Y5; Q91W24; Q99KX8;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 2.
30-AUG-2017, entry version 142.
RecName: Full=Histone-arginine methyltransferase CARM1;
EC=2.1.1.319 {ECO:0000269|PubMed:11341840, ECO:0000269|PubMed:17882261, ECO:0000269|PubMed:19843527, ECO:0000269|PubMed:19897492, ECO:0000269|PubMed:21138967};
AltName: Full=Coactivator-associated arginine methyltransferase 1;
AltName: Full=Protein arginine N-methyltransferase 4;
Name=Carm1; Synonyms=Prmt4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF
189-VAL--ASP-191, FUNCTION, TISSUE SPECIFICITY, METHYLATION OF HISTONE
H3, AND INTERACTION WITH NCOA1; NCOA2 AND NCOA3.
TISSUE=Embryo;
PubMed=10381882; DOI=10.1126/science.284.5423.2174;
Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T.,
Aswad D.W., Stallcup M.R.;
"Regulation of transcription by a protein methyltransferase.";
Science 284:2174-2177(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 261-608 (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary gland, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-608 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Visual cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
FUNCTION IN METHYLATION OF HISTONE H3, AND CATALYTIC ACTIVITY.
PubMed=11341840; DOI=10.1021/bi002631b;
Schurter B.T., Koh S.S., Chen D., Bunick G.J., Harp J.M., Hanson B.L.,
Henschen-Edman A., Mackay D.R., Stallcup M.R., Aswad D.W.;
"Methylation of histone H3 by coactivator-associated arginine
methyltransferase 1.";
Biochemistry 40:5747-5756(2001).
[5]
METHYLATION OF HISTONE H3.
PubMed=11747826; DOI=10.1016/S0960-9822(01)00600-5;
Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A.,
Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R.;
"Hormone-dependent, CARM1-directed, arginine-specific methylation of
histone H3 on a steroid-regulated promoter.";
Curr. Biol. 11:1981-1985(2001).
[6]
FUNCTION, METHYLATION OF EP300 AND CREBBP, MUTAGENESIS OF
189-VAL--ASP-191, AND INTERACTION WITH EP300 AND CREBBP.
PubMed=11701890; DOI=10.1126/science.1065961;
Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M.,
Evans R.M.;
"A transcriptional switch mediated by cofactor methylation.";
Science 294:2507-2511(2001).
[7]
METHYLATION OF HISTONE H3.
PubMed=12498683; DOI=10.1016/S0960-9822(02)01387-8;
Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.;
"Crosstalk between CARM1 methylation and CBP acetylation on histone
H3.";
Curr. Biol. 12:2090-2097(2002).
[8]
METHYLATION OF HISTONE H3.
PubMed=11751582; DOI=10.1093/embo-reports/kvf013;
Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.;
"Methylation at arginine 17 of histone H3 is linked to gene
activation.";
EMBO Rep. 3:39-44(2002).
[9]
METHYLATION OF PABPC1.
PubMed=11850402; DOI=10.1093/embo-reports/kvf052;
Lee J., Bedford M.T.;
"PABP1 identified as an arginine methyltransferase substrate using
high-density protein arrays.";
EMBO Rep. 3:268-273(2002).
[10]
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION
WITH MEF2C.
PubMed=11713257; DOI=10.1074/jbc.M109835200;
Chen S.L., Loffler K.A., Chen D., Stallcup M.R., Muscat G.E.;
"The coactivator-associated arginine methyltransferase is necessary
for muscle differentiation: CARM1 coactivates myocyte enhancer factor-
2.";
J. Biol. Chem. 277:4324-4333(2002).
[11]
FUNCTION, MUTAGENESIS OF GLU-267, AND INTERACTION WITH CTNNB1.
PubMed=11983685; DOI=10.1074/jbc.M110865200;
Koh S.S., Li H., Lee Y.-H., Widelitz R.B., Chuong C.-M.,
Stallcup M.R.;
"Synergistic coactivator function by coactivator-associated arginine
methyltransferase (CARM) 1 and beta-catenin with two different classes
of DNA-binding transcriptional activators.";
J. Biol. Chem. 277:26031-26035(2002).
[12]
METHYLATION OF ELAVL1.
PubMed=12237300; DOI=10.1074/jbc.M206187200;
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).
[13]
CHARACTERIZATION, AND HOMOOLIGOMERIZATION.
PubMed=12351636; DOI=10.1074/jbc.M207623200;
Teyssier C., Chen D., Stallcup M.R.;
"Requirement for multiple domains of the protein arginine
methyltransferase CARM1 in its transcriptional coactivator function.";
J. Biol. Chem. 277:46066-46072(2002).
[14]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH EP300 AND NCOA2, AND
MUTAGENESIS OF GLU-267.
PubMed=11997499; DOI=10.1128/MCB.22.11.3621-3632.2002;
Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R.;
"Synergy among nuclear receptor coactivators: selective requirement
for protein methyltransferase and acetyltransferase activities.";
Mol. Cell. Biol. 22:3621-3632(2002).
[15]
FUNCTION, DISRUPTION PHENOTYPE, AND METHYLATION OF PABPC1.
PubMed=12756295; DOI=10.1073/pnas.1232272100;
Yadav N., Lee J., Kim J., Shen J., Hu M.C.-T., Aldaz C.M.,
Bedford M.T.;
"Specific protein methylation defects and gene expression
perturbations in coactivator-associated arginine methyltransferase 1-
deficient mice.";
Proc. Natl. Acad. Sci. U.S.A. 100:6464-6468(2003).
[16]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=15186775; DOI=10.1016/j.cell.2004.05.009;
An W., Kim J., Roeder R.G.;
"Ordered cooperative functions of PRMT1, p300, and CARM1 in
transcriptional activation by p53.";
Cell 117:735-748(2004).
[17]
METHYLATION OF HISTONE H3.
PubMed=15339660; DOI=10.1016/j.cell.2004.08.020;
Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H.,
Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P.,
Bannister A.J., Kouzarides T.;
"Histone deimination antagonizes arginine methylation.";
Cell 118:545-553(2004).
[18]
FUNCTION, AND INTERACTION WITH FLII.
PubMed=14966289; DOI=10.1128/MCB.24.5.2103-2117.2004;
Lee Y.-H., Campbell H.D., Stallcup M.R.;
"Developmentally essential protein flightless I is a nuclear receptor
coactivator with actin binding activity.";
Mol. Cell. Biol. 24:2103-2117(2004).
[19]
METHYLATION OF HISTONE H3, FUNCTION, AND INTERACTION WITH RELA.
PubMed=15616592; DOI=10.1038/sj.emboj.7600500;
Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,
Imhof R., Bedford M.T., Natoli G., Hottiger M.O.;
"Arginine methyltransferase CARM1 is a promoter-specific regulator of
NF-kappaB-dependent gene expression.";
EMBO J. 24:85-96(2005).
[20]
TISSUE SPECIFICITY.
PubMed=16508003; DOI=10.1128/MCB.26.6.2273-2285.2006;
Fujiwara T., Mori Y., Chu D.L., Koyama Y., Miyata S., Tanaka H.,
Yachi K., Kubo T., Yoshikawa H., Tohyama M.;
"CARM1 regulates proliferation of PC12 cells by methylating HuD.";
Mol. Cell. Biol. 26:2273-2285(2006).
[21]
FUNCTION, INTERACTION WITH TRIM24, AND IDENTIFICATION IN A COMPLEX
WITH TRIM24 AND NCOA2.
PubMed=16322096; DOI=10.1210/me.2005-0393;
Teyssier C., Ou C.Y., Khetchoumian K., Losson R., Stallcup M.R.;
"Transcriptional intermediary factor 1alpha mediates physical
interaction and functional synergy between the coactivator-associated
arginine methyltransferase 1 and glucocorticoid receptor-interacting
protein 1 nuclear receptor coactivators.";
Mol. Endocrinol. 20:1276-1286(2006).
[22]
FUNCTION.
PubMed=17218272; DOI=10.1016/j.molcel.2006.11.019;
Cheng D., Cote J., Shaaban S., Bedford M.T.;
"The arginine methyltransferase CARM1 regulates the coupling of
transcription and mRNA processing.";
Mol. Cell 25:71-83(2007).
[23]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=18188184; DOI=10.1038/sj.embor.7401151;
Yadav N., Cheng D., Richard S., Morel M., Iyer V.R., Aldaz C.M.,
Bedford M.T.;
"CARM1 promotes adipocyte differentiation by coactivating PPARgamma.";
EMBO Rep. 9:193-198(2008).
[24]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH EP300 AND
NCOA3, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-154; SER-217 AND
SER-229, AND PHOSPHORYLATION AT SER-217.
PubMed=19843527; DOI=10.1074/jbc.M109.065524;
Feng Q., He B., Jung S.Y., Song Y., Qin J., Tsai S.Y., Tsai M.J.,
O'Malley B.W.;
"Biochemical control of CARM1 enzymatic activity by phosphorylation.";
J. Biol. Chem. 284:36167-36174(2009).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[26]
FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBUNIT, AND
MUTAGENESIS OF ARG-169 AND TYR-173.
PubMed=19897492; DOI=10.1074/jbc.M109.035865;
Kim D., Lee J., Cheng D., Li J., Carter C., Richie E., Bedford M.T.;
"Enzymatic activity is required for the in vivo functions of CARM1.";
J. Biol. Chem. 285:1147-1152(2010).
[27]
METHYLATION AT ARG-551, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF
ARG-551, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21138967; DOI=10.1093/nar/gkq1246;
Kuhn P., Chumanov R., Wang Y., Ge Y., Burgess R.R., Xu W.;
"Automethylation of CARM1 allows coupling of transcription and mRNA
splicing.";
Nucleic Acids Res. 39:2717-2726(2011).
[28]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 147-490 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE, CATALYTIC ACTIVITY, FUNCTION, INTERACTION
WITH NCOA2/GRIP1, ENZYME REGULATION, AND SUBUNIT.
PubMed=17882261; DOI=10.1038/sj.emboj.7601856;
Yue W.W., Hassler M., Roe S.M., Thompson-Vale V., Pearl L.H.;
"Insights into histone code syntax from structural and biochemical
studies of CARM1 methyltransferase.";
EMBO J. 26:4402-4412(2007).
-!- 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 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. 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. {ECO:0000269|PubMed:10381882,
ECO:0000269|PubMed:11341840, ECO:0000269|PubMed:11701890,
ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:11983685,
ECO:0000269|PubMed:11997499, ECO:0000269|PubMed:12756295,
ECO:0000269|PubMed:14966289, ECO:0000269|PubMed:15186775,
ECO:0000269|PubMed:15616592, ECO:0000269|PubMed:16322096,
ECO:0000269|PubMed:17218272, ECO:0000269|PubMed:17882261,
ECO:0000269|PubMed:18188184, ECO:0000269|PubMed:19843527,
ECO:0000269|PubMed:19897492, ECO:0000269|PubMed:21138967}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + [protein]-L-
arginine = 2 S-adenosyl-L-homocysteine + [protein]-
N(omega),N(omega)-dimethyl-L-arginine.
{ECO:0000269|PubMed:11341840, ECO:0000269|PubMed:17882261,
ECO:0000269|PubMed:19843527, ECO:0000269|PubMed:19897492,
ECO:0000269|PubMed:21138967}.
-!- ENZYME REGULATION: Methylation of H3R17 (H3R17me) by CARM1 is
stimulated by preacetylation of H3 'Lys-18' (H3K18ac) H3 'Lys-23'
(H3K23ac) by EP300 and blocked by citrullination of H3 'Arg-17'
(H3R17ci) by PADI4. {ECO:0000269|PubMed:17882261}.
-!- SUBUNIT: Homodimer. Interacts with NR1H4. Interacts with SNRPC (By
similarity). 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, TRIM24, CREBBP and CTNNB1. Interacts with
RELA. Identified in a complex containing CARM1, TRIM24 and
NCOA2/GRIP1. Interacts with NCOA3/SRC3. {ECO:0000250,
ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:11701890,
ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:11983685,
ECO:0000269|PubMed:11997499, ECO:0000269|PubMed:14966289,
ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15616592,
ECO:0000269|PubMed:16322096, ECO:0000269|PubMed:17882261,
ECO:0000269|PubMed:19843527, ECO:0000269|PubMed:19897492}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear
during the G1, S and G2 phases of the cell cycle. Cytoplasmic
during mitosis, after breakup of the nuclear membrane (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9WVG6-1; Sequence=Displayed;
Name=2;
IsoId=Q9WVG6-2; Sequence=VSP_012508;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Within the brain,
present in proliferating cells from lateral ventricular zone and
dentate gyrus (at protein level). {ECO:0000269|PubMed:10381882,
ECO:0000269|PubMed:16508003}.
-!- DEVELOPMENTAL STAGE: At E9, expression is prominent in the neural
tube and somites. {ECO:0000269|PubMed:11713257}.
-!- PTM: Phosphorylation at Ser-217 is strongly increased during
mitosis, and decreases rapidly to a very low, basal level after
entry into the G1 phase of the cell cycle (By similarity).
Phosphorylation at Ser-217 interferes with S-adenosyl-L-methionine
binding and strongly reduces methyltransferase activity.
Phosphorylation at Ser-217 may promote cytosolic location.
{ECO:0000250, ECO:0000269|PubMed:19843527}.
-!- PTM: Auto-methylated on Arg-551. Methylation enhances
transcription coactivator activity. Methylation is required for
its role in the regulation of pre-mRNA alternative splicing.
{ECO:0000269|PubMed:10381882, ECO:0000269|PubMed:11701890,
ECO:0000269|PubMed:11747826, ECO:0000269|PubMed:11751582,
ECO:0000269|PubMed:11850402, ECO:0000269|PubMed:12237300,
ECO:0000269|PubMed:12498683, ECO:0000269|PubMed:12756295,
ECO:0000269|PubMed:15339660, ECO:0000269|PubMed:15616592,
ECO:0000269|PubMed:21138967}.
-!- DISRUPTION PHENOTYPE: Neonatal lethality. The lungs of neonates do
not inflate and they do not breathe. The same neonate lethality is
observed with mutants that produce CARM1 protein without enzyme
activity. Embryos are distinctly smaller at 18.5 dpc. They show
reduced lipid accumulation in brown adipose tissue and reduced
amounts of brown adipose tissue. Thymocyte differentiation is
blocked at an early stage. Mutants display complete loss of
protein methylation of the CARM1 substrates PABPC1 and EP300/P300.
{ECO:0000269|PubMed:12756295, ECO:0000269|PubMed:18188184,
ECO:0000269|PubMed:19897492}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
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EMBL; AF117887; AAD41265.2; -; mRNA.
EMBL; BC003964; AAH03964.1; -; mRNA.
EMBL; BC008263; AAH08263.1; -; mRNA.
EMBL; BC036974; AAH36974.1; -; mRNA.
EMBL; AK158757; BAE34644.1; -; mRNA.
CCDS; CCDS22906.1; -. [Q9WVG6-1]
CCDS; CCDS52736.1; -. [Q9WVG6-2]
RefSeq; NP_067506.2; NM_021531.6. [Q9WVG6-1]
RefSeq; NP_694781.1; NM_153141.1. [Q9WVG6-2]
UniGene; Mm.178115; -.
PDB; 2V74; X-ray; 2.70 A; B/D/F/H=147-490.
PDB; 2V7E; X-ray; 2.70 A; A/B=147-490.
PDB; 5IH3; X-ray; 1.77 A; A/B/C/D=130-487.
PDB; 5IS6; X-ray; 2.01 A; A/B/C/D=130-487.
PDB; 5IS7; X-ray; 2.29 A; A/B/C/D=130-487.
PDB; 5IS8; X-ray; 2.71 A; A/B/C/D=130-507.
PDB; 5IS9; X-ray; 2.40 A; A/B/C/D=130-487.
PDB; 5ISA; X-ray; 2.40 A; A/B/C/D=130-490.
PDB; 5ISB; X-ray; 2.00 A; A/B/C/D=130-487.
PDB; 5ISC; X-ray; 2.60 A; A/B/C/D=130-487.
PDB; 5ISD; X-ray; 2.60 A; A/B/C/D=130-487.
PDB; 5ISE; X-ray; 2.10 A; A/B/C/D=130-487.
PDB; 5ISF; X-ray; 2.22 A; A/B/C/D=130-487.
PDB; 5ISG; X-ray; 2.42 A; A/B/C/D=130-487.
PDB; 5ISH; X-ray; 2.15 A; A/B/C/D=130-487.
PDB; 5ISI; X-ray; 2.74 A; A/B/C/D=130-487.
PDB; 5K8V; X-ray; 2.25 A; A/B/C/D=130-487.
PDB; 5K8W; X-ray; 2.10 A; A/B/C/D=130-487.
PDB; 5K8X; X-ray; 1.99 A; A/B/C/D=130-487.
PDB; 5LGP; X-ray; 2.04 A; A/B/C/D=130-487.
PDB; 5LGQ; X-ray; 2.11 A; A/B/C/D=130-487.
PDB; 5LGR; X-ray; 2.00 A; A/B/C/D=130-487.
PDB; 5LGS; X-ray; 2.10 A; A/B/C/D=130-487.
PDBsum; 2V74; -.
PDBsum; 2V7E; -.
PDBsum; 5IH3; -.
PDBsum; 5IS6; -.
PDBsum; 5IS7; -.
PDBsum; 5IS8; -.
PDBsum; 5IS9; -.
PDBsum; 5ISA; -.
PDBsum; 5ISB; -.
PDBsum; 5ISC; -.
PDBsum; 5ISD; -.
PDBsum; 5ISE; -.
PDBsum; 5ISF; -.
PDBsum; 5ISG; -.
PDBsum; 5ISH; -.
PDBsum; 5ISI; -.
PDBsum; 5K8V; -.
PDBsum; 5K8W; -.
PDBsum; 5K8X; -.
PDBsum; 5LGP; -.
PDBsum; 5LGQ; -.
PDBsum; 5LGR; -.
PDBsum; 5LGS; -.
ProteinModelPortal; Q9WVG6; -.
SMR; Q9WVG6; -.
BioGrid; 208501; 7.
DIP; DIP-44593N; -.
IntAct; Q9WVG6; 4.
MINT; MINT-6166798; -.
STRING; 10090.ENSMUSP00000034703; -.
BindingDB; Q9WVG6; -.
ChEMBL; CHEMBL5538; -.
iPTMnet; Q9WVG6; -.
PhosphoSitePlus; Q9WVG6; -.
PaxDb; Q9WVG6; -.
PRIDE; Q9WVG6; -.
Ensembl; ENSMUST00000034703; ENSMUSP00000034703; ENSMUSG00000032185. [Q9WVG6-1]
Ensembl; ENSMUST00000115395; ENSMUSP00000111053; ENSMUSG00000032185. [Q9WVG6-2]
GeneID; 59035; -.
KEGG; mmu:59035; -.
UCSC; uc009olu.2; mouse. [Q9WVG6-1]
UCSC; uc009olw.2; mouse. [Q9WVG6-2]
CTD; 10498; -.
MGI; MGI:1913208; Carm1.
eggNOG; KOG1500; Eukaryota.
eggNOG; ENOG410XPDD; LUCA.
GeneTree; ENSGT00550000074406; -.
HOGENOM; HOG000198522; -.
HOVERGEN; HBG050797; -.
InParanoid; Q9WVG6; -.
KO; K05931; -.
PhylomeDB; Q9WVG6; -.
TreeFam; TF323332; -.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
ChiTaRS; Carm1; mouse.
EvolutionaryTrace; Q9WVG6; -.
PRO; PR:Q9WVG6; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032185; -.
ExpressionAtlas; Q9WVG6; baseline and differential.
Genevisible; Q9WVG6; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:MGI.
GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
GO; GO:0035642; F:histone methyltransferase activity (H3-R17 specific); IDA:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISO:MGI.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0008276; F:protein methyltransferase activity; IDA:MGI.
GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:UniProtKB.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IMP:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IMP:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0060350; P:endochondral bone morphogenesis; IMP:MGI.
GO; GO:0034969; P:histone arginine methylation; IDA:UniProtKB.
GO; GO:0034971; P:histone H3-R17 methylation; IDA:UniProtKB.
GO; GO:0034970; P:histone H3-R2 methylation; ISO:MGI.
GO; GO:0016571; P:histone methylation; IDA:MGI.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IGI:MGI.
GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:HGNC.
GO; GO:2000171; P:negative regulation of dendrite development; IEA:Ensembl.
GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0071168; P:protein localization to chromatin; IMP:MGI.
GO; GO:0006479; P:protein methylation; IMP:MGI.
GO; GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; IMP:MGI.
GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
GO; GO:1902415; P:regulation of mRNA binding; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR020989; Histone-Arg_MeTrfase_N.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF11531; CARM1; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Cytoplasm; Methylation; Methyltransferase; Nucleus;
Phosphoprotein; Reference proteome; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase.
CHAIN 1 608 Histone-arginine methyltransferase CARM1.
/FTId=PRO_0000212339.
DOMAIN 147 454 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
REGION 500 608 Transactivation domain.
BINDING 160 160 S-adenosyl-L-methionine.
BINDING 169 169 S-adenosyl-L-methionine.
BINDING 193 193 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 215 215 S-adenosyl-L-methionine.
BINDING 244 244 S-adenosyl-L-methionine.
BINDING 272 272 S-adenosyl-L-methionine.
MOD_RES 217 217 Phosphoserine.
{ECO:0000269|PubMed:19843527}.
MOD_RES 551 551 Dimethylated arginine.
{ECO:0000269|PubMed:21138967}.
VAR_SEQ 540 562 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012508.
MUTAGEN 154 154 Y->A,F,R: Loss of S-adenosyl-L-methionine
binding. Loss of protein
methyltransferase activity.
{ECO:0000269|PubMed:19843527}.
MUTAGEN 169 169 R->A: Loss of protein methyltransferase
activity. {ECO:0000269|PubMed:19897492}.
MUTAGEN 173 173 Y->A: Reduces protein methyltransferase
activity. {ECO:0000269|PubMed:19897492}.
MUTAGEN 189 191 VLD->AAA: Abolishes histone
methyltransferase activity and
coactivator activity.
{ECO:0000269|PubMed:10381882,
ECO:0000269|PubMed:11701890}.
MUTAGEN 217 217 S->A: Loss of S-adenosyl-L-methionine
binding. Loss of protein
methyltransferase activity. Localized in
the nucleus.
{ECO:0000269|PubMed:19843527}.
MUTAGEN 217 217 S->C,T: Loss of S-adenosyl-L-methionine
binding. Loss of protein
methyltransferase activity.
{ECO:0000269|PubMed:19843527}.
MUTAGEN 217 217 S->E: Loss of S-adenosyl-L-methionine
binding. Loss of protein
methyltransferase activity. Localized in
the cytosol.
{ECO:0000269|PubMed:19843527}.
MUTAGEN 229 229 S->E: Abolishes dimerization.
{ECO:0000269|PubMed:19843527}.
MUTAGEN 267 267 E->Q: Abolishes histone methyltransferase
activity and reduces coactivator
activity. {ECO:0000269|PubMed:11983685,
ECO:0000269|PubMed:11997499}.
MUTAGEN 551 551 R->K: Abolishes dimethylation. Impairs
transcription coactivator activity and
regulation of alternative splicing. No
effect on methyltransferase activity.
{ECO:0000269|PubMed:21138967}.
CONFLICT 400 400 I -> L (in Ref. 3; BAE34644).
{ECO:0000305}.
HELIX 137 141 {ECO:0000244|PDB:5IH3}.
HELIX 144 154 {ECO:0000244|PDB:5IH3}.
HELIX 157 164 {ECO:0000244|PDB:5IH3}.
HELIX 167 179 {ECO:0000244|PDB:5IH3}.
HELIX 181 183 {ECO:0000244|PDB:5IH3}.
TURN 184 186 {ECO:0000244|PDB:5IH3}.
STRAND 188 193 {ECO:0000244|PDB:5IH3}.
TURN 195 197 {ECO:0000244|PDB:5K8V}.
HELIX 198 205 {ECO:0000244|PDB:5IH3}.
STRAND 209 215 {ECO:0000244|PDB:5IH3}.
HELIX 219 229 {ECO:0000244|PDB:5IH3}.
TURN 233 235 {ECO:0000244|PDB:5IH3}.
STRAND 236 241 {ECO:0000244|PDB:5IH3}.
TURN 243 245 {ECO:0000244|PDB:5IH3}.
STRAND 252 257 {ECO:0000244|PDB:5IH3}.
TURN 265 267 {ECO:0000244|PDB:5IH3}.
HELIX 269 275 {ECO:0000244|PDB:5IH3}.
HELIX 276 279 {ECO:0000244|PDB:5IH3}.
STRAND 280 288 {ECO:0000244|PDB:5IH3}.
STRAND 290 298 {ECO:0000244|PDB:5IH3}.
HELIX 301 311 {ECO:0000244|PDB:5IH3}.
HELIX 312 314 {ECO:0000244|PDB:5IH3}.
STRAND 319 321 {ECO:0000244|PDB:2V74}.
HELIX 325 327 {ECO:0000244|PDB:5IH3}.
HELIX 328 336 {ECO:0000244|PDB:5IH3}.
STRAND 340 342 {ECO:0000244|PDB:5IH3}.
HELIX 346 348 {ECO:0000244|PDB:5IH3}.
STRAND 354 359 {ECO:0000244|PDB:5IH3}.
TURN 360 362 {ECO:0000244|PDB:5IH3}.
HELIX 365 368 {ECO:0000244|PDB:5IH3}.
STRAND 369 378 {ECO:0000244|PDB:5IH3}.
STRAND 383 397 {ECO:0000244|PDB:5IH3}.
STRAND 402 406 {ECO:0000244|PDB:5IH3}.
STRAND 418 429 {ECO:0000244|PDB:5IH3}.
STRAND 434 444 {ECO:0000244|PDB:5IH3}.
TURN 445 447 {ECO:0000244|PDB:5IH3}.
STRAND 448 457 {ECO:0000244|PDB:5IH3}.
TURN 458 460 {ECO:0000244|PDB:5IH3}.
STRAND 463 469 {ECO:0000244|PDB:5IH3}.
TURN 494 496 {ECO:0000244|PDB:5IS8}.
SEQUENCE 608 AA; 65854 MW; C621F2AA9FBA2DA3 CRC64;
MAAAAATAVG PGAGSAGVAG PGGAGPCATV SVFPGARLLT IGDANGEIQR HAEQQALRLE
VRAGPDAAGI ALYSHEDVCV FKCSVSRETE CSRVGRQSFI ITLGCNSVLI QFATPHDFCS
FYNILKTCRG HTLERSVFSE RTEESSAVQY FQFYGYLSQQ QNMMQDYVRT GTYQRAILQN
HTDFKDKIVL DVGCGSGILS FFAAQAGARK IYAVEASTMA QHAEVLVKSN NLTDRIVVIP
GKVEEVSLPE QVDIIISEPM GYMLFNERML ESYLHAKKYL KPSGNMFPTI GDVHLAPFTD
EQLYMEQFTK ANFWYQPSFH GVDLSALRGA AVDEYFRQPV VDTFDIRILM AKSVKYTVNF
LEAKEGDLHR IEIPFKFHML HSGLVHGLAF WFDVAFIGSI MTVWLSTAPT EPLTHWYQVR
CLFQSPLFAK AGDTLSGTCL LIANKRQSYD ISIVAQVDQT GSKSSNLLDL KNPFFRYTGT
TPSPPPGSHY TSPSENMWNT GSTYNLSSGV AVAGMPTAYD LSSVIAGGSS VGHNNLIPLA
NTGIVNHTHS RMGSIMSTGI VQGSSGAQGG GGSSSAHYAV NNQFTMGGPA ISMASPMSIP
TNTMHYGS


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