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Protein arginine N-methyltransferase 2 (EC 2.1.1.319) (Histone-arginine N-methyltransferase PRMT2)

 ANM2_HUMAN              Reviewed;         433 AA.
P55345; B7U630; B7U631; B7U632; P78350; Q498Y5; Q5U7D4; Q6FHF0;
Q99781; Q9BW15; Q9UMC2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
28-FEB-2018, entry version 160.
RecName: Full=Protein arginine N-methyltransferase 2;
EC=2.1.1.319 {ECO:0000269|PubMed:19405910};
AltName: Full=Histone-arginine N-methyltransferase PRMT2;
Name=PRMT2; Synonyms=HMT1, HRMT1L1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9545638; DOI=10.1006/geno.1997.5190;
Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A.,
Henry M.F.;
"Identification and characterization of two putative human arginine
methyltransferases (HRMT1L1 and HRMT1L2).";
Genomics 48:330-340(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9196002; DOI=10.1007/s003359900491;
Katsanis N., Yaspo M.-L., Fisher E.M.C.;
"Identification and mapping of a novel human gene, HRMT1L1, homologous
to the rat protein arginine N-methyltransferase 1 (PRMT1) gene.";
Mamm. Genome 8:526-529(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PRMT2L2), AND SUBCELLULAR LOCATION
(ISOFORM PRMT2L2).
PubMed=21820040; DOI=10.1016/j.gene.2011.06.022;
Zhong J., Cao R.X., Hong T., Yang J., Zu X.Y., Xiao X.H., Liu J.H.,
Wen G.B.;
"Identification and expression analysis of a novel transcript of the
human PRMT2 gene resulted from alternative polyadenylation in breast
cancer.";
Gene 487:1-9(2011).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PRMT2ALPHA; PRMT2BETA AND
PRMT2GAMMA), SUBCELLULAR LOCATION, AND INTERACTION WITH AR AND ESR1.
PubMed=22093364; DOI=10.1111/j.1742-4658.2011.08426.x;
Zhong J., Cao R.X., Zu X.Y., Hong T., Yang J., Liu L., Xiao X.H.,
Ding W.J., Zhao Q., Liu J.H., Wen G.B.;
"Identification and characterization of novel spliced variants of
PRMT2 in breast carcinoma.";
FEBS J. 279:316-335(2012).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9110174;
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Chondrosarcoma, and Kidney;
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-277 (ISOFORM 1).
The European IMAGE consortium;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[12]
INTERACTION WITH HNRNPUL1, AND SUBCELLULAR LOCATION.
PubMed=11513728; DOI=10.1042/0264-6021:3580305;
Kzhyshkowska J., Schuett H., Liss M., Kremmer E., Stauber R., Wolf H.,
Dobner T.;
"Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its
Arg-Gly-Gly (RGG) box and interacts with human arginine
methyltransferase HRMT1L1.";
Biochem. J. 358:305-314(2001).
[13]
FUNCTION, AND INTERACTION WITH ESR1; ESR2; NCOA1; NCOA6; PGR; PPARG;
RARA; RXRA AND THRB.
PubMed=12039952; DOI=10.1074/jbc.M201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a
coactivator for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[14]
FUNCTION, AND INTERACTION WITH NFKBIA.
PubMed=16648481; DOI=10.1128/MCB.26.10.3864-3874.2006;
Ganesh L., Yoshimoto T., Moorthy N.C., Akahata W., Boehm M.,
Nabel E.G., Nabel G.J.;
"Protein methyltransferase 2 inhibits NF-kappaB function and promotes
apoptosis.";
Mol. Cell. Biol. 26:3864-3874(2006).
[15]
INTERACTION WITH PRMT8.
PubMed=17925405; DOI=10.1074/jbc.M704650200;
Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G.;
"Regulation of protein arginine methyltransferase 8 (PRMT8) activity
by its N-terminal domain.";
J. Biol. Chem. 282:36444-36453(2007).
[16]
FUNCTION, INTERACTION WITH AR AND ESR1, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=17587566; DOI=10.1016/j.jsbmb.2007.05.006;
Meyer R., Wolf S.S., Obendorf M.;
"PRMT2, a member of the protein arginine methyltransferase family, is
a coactivator of the androgen receptor.";
J. Steroid Biochem. Mol. Biol. 107:1-14(2007).
[17]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19405910; DOI=10.1042/BJ20090268;
Lakowski T.M., Frankel A.;
"Kinetic analysis of human protein arginine N-methyltransferase 2:
formation of monomethyl- and asymmetric dimethyl-arginine residues on
histone H4.";
Biochem. J. 421:253-261(2009).
[18]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-61 AND ARG-72, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[19]
STRUCTURE BY NMR OF 33-87.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH3 domain of the protein arginine N-
methyltransferase 2.";
Submitted (OCT-2005) to the PDB data bank.
-!- FUNCTION: Arginine methyltransferase that methylates the guanidino
nitrogens of arginyl residues in proteins such as STAT3, FBL,
histone H4. Acts as a coactivator (with NCOA2) of the androgen
receptor (AR)-mediated transactivation. Acts as a coactivator
(with estrogen) of estrogen receptor (ER)-mediated
transactivation. Enhances PGR, PPARG, RARA-mediated
transactivation. May inhibit NF-kappa-B transcription and promote
apoptosis. Represses E2F1 transcriptional activity (in a RB1-
dependent manner). May be involved in growth regulation.
{ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:16648481,
ECO:0000269|PubMed:17587566, ECO:0000269|PubMed:19405910}.
-!- 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:19405910}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.6 uM for AdoMet {ECO:0000269|PubMed:19405910};
KM=3.3 uM for H4 {ECO:0000269|PubMed:19405910};
Vmax=1.4 nmol/min/mg enzyme toward AdoMet
{ECO:0000269|PubMed:19405910};
Vmax=1.5 nmol/min/mg enzyme toward H4
{ECO:0000269|PubMed:19405910};
-!- SUBUNIT: Self-associates. Interacts with RB1 and E2F1 (By
similarity). Interacts with NCOA6 coactivator. Interacts (via SH3
domain) with PRMT8. Interacts with AR. Interacts with NFKBIA.
Interacts with ESR1, ESR2, PGR, PPARG, RARA, RXRA and THRB.
Interacts with HNRNPUL1. {ECO:0000250,
ECO:0000269|PubMed:11513728, ECO:0000269|PubMed:12039952,
ECO:0000269|PubMed:16648481, ECO:0000269|PubMed:17587566,
ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:22093364}.
-!- INTERACTION:
Q13191:CBLB; NbExp=3; IntAct=EBI-78458, EBI-744027;
P03372:ESR1; NbExp=9; IntAct=EBI-78458, EBI-78473;
P06400:RB1; NbExp=3; IntAct=EBI-78458, EBI-491274;
Q9NTZ6:RBM12; NbExp=3; IntAct=EBI-78458, EBI-310707;
Q15637:SF1; NbExp=5; IntAct=EBI-78458, EBI-744603;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
Note=Translocates from the cytoplasm to the nucleus, after hormone
exposure. Excluded from nucleolus.
-!- SUBCELLULAR LOCATION: Isoform PRMT2Alpha: Nucleus. Note=Excluded
from nucleolus.
-!- SUBCELLULAR LOCATION: Isoform PRMT2Beta: Cytoplasm. Nucleus.
Nucleus, nucleolus.
-!- SUBCELLULAR LOCATION: Isoform PRMT2Gamma: Nucleus. Note=Excluded
from nucleolus.
-!- SUBCELLULAR LOCATION: Isoform PRMT2L2: Cytoplasm
{ECO:0000269|PubMed:21820040}. Nucleus
{ECO:0000269|PubMed:21820040}. Note=Predominantly cytoplasmic.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1;
IsoId=P55345-1; Sequence=Displayed;
Name=2;
IsoId=P55345-2; Sequence=VSP_042680;
Note=No experimental confirmation available.;
Name=3;
IsoId=P55345-3; Sequence=VSP_043381;
Note=No experimental confirmation available.;
Name=PRMT2Alpha;
IsoId=P55345-4; Sequence=VSP_054930, VSP_054931;
Note=Higher expression in breast cancer tissues.;
Name=PRMT2Beta;
IsoId=P55345-5; Sequence=VSP_054928, VSP_054932;
Note=Higher expression in breast cancer tissues. Doesn't
interact with ESR1.;
Name=PRMT2Gamma;
IsoId=P55345-6; Sequence=VSP_054927;
Note=Higher expression in breast cancer tissues.;
Name=PRMT2L2;
IsoId=P55345-7; Sequence=VSP_054929;
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in androgen
target organs such as heart, prostate, skeletal muscle, ovary and
spinal cord. {ECO:0000269|PubMed:17587566}.
-!- 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; X99209; CAA67599.1; -; mRNA.
EMBL; U80213; AAB48437.1; -; mRNA.
EMBL; AY786414; AAV48568.2; -; mRNA.
EMBL; FJ436410; ACJ66866.1; -; mRNA.
EMBL; FJ436411; ACJ66867.1; -; mRNA.
EMBL; FJ436412; ACJ66868.1; -; mRNA.
EMBL; U79286; AAB50221.1; -; mRNA.
EMBL; CR541804; CAG46603.1; -; mRNA.
EMBL; AK123650; BAG53931.1; -; mRNA.
EMBL; AP000339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09259.1; -; Genomic_DNA.
EMBL; CH471079; EAX09265.1; -; Genomic_DNA.
EMBL; BC000727; AAH00727.1; -; mRNA.
EMBL; BC100026; AAI00027.1; -; mRNA.
EMBL; AL109794; CAB52454.1; -; mRNA.
CCDS; CCDS13737.1; -. [P55345-1]
CCDS; CCDS56219.1; -. [P55345-2]
CCDS; CCDS56220.1; -. [P55345-3]
CCDS; CCDS68230.1; -. [P55345-4]
CCDS; CCDS68231.1; -. [P55345-5]
CCDS; CCDS74806.1; -. [P55345-6]
RefSeq; NP_001229793.1; NM_001242864.2. [P55345-3]
RefSeq; NP_001229794.1; NM_001242865.2. [P55345-2]
RefSeq; NP_001229795.1; NM_001242866.2. [P55345-7]
RefSeq; NP_001273605.1; NM_001286676.1. [P55345-5]
RefSeq; NP_001273606.1; NM_001286677.1. [P55345-4]
RefSeq; NP_001273607.1; NM_001286678.1. [P55345-6]
RefSeq; NP_001526.2; NM_001535.4. [P55345-1]
RefSeq; NP_996845.1; NM_206962.3. [P55345-1]
RefSeq; XP_005261168.1; XM_005261111.3. [P55345-1]
RefSeq; XP_006724061.1; XM_006723998.3. [P55345-5]
RefSeq; XP_006724063.1; XM_006724000.2. [P55345-6]
UniGene; Hs.154163; -.
UniGene; Hs.661229; -.
PDB; 1X2P; NMR; -; A=33-87.
PDBsum; 1X2P; -.
ProteinModelPortal; P55345; -.
SMR; P55345; -.
BioGrid; 109511; 52.
CORUM; P55345; -.
IntAct; P55345; 25.
MINT; P55345; -.
STRING; 9606.ENSP00000347906; -.
iPTMnet; P55345; -.
PhosphoSitePlus; P55345; -.
SwissPalm; P55345; -.
DMDM; 2499805; -.
PaxDb; P55345; -.
PeptideAtlas; P55345; -.
PRIDE; P55345; -.
DNASU; 3275; -.
Ensembl; ENST00000291705; ENSP00000291705; ENSG00000160310. [P55345-6]
Ensembl; ENST00000334494; ENSP00000335490; ENSG00000160310. [P55345-2]
Ensembl; ENST00000355680; ENSP00000347906; ENSG00000160310. [P55345-1]
Ensembl; ENST00000397637; ENSP00000380759; ENSG00000160310. [P55345-1]
Ensembl; ENST00000397638; ENSP00000380760; ENSG00000160310. [P55345-1]
Ensembl; ENST00000440086; ENSP00000397266; ENSG00000160310. [P55345-3]
Ensembl; ENST00000451211; ENSP00000411984; ENSG00000160310. [P55345-4]
Ensembl; ENST00000458387; ENSP00000407463; ENSG00000160310. [P55345-5]
GeneID; 3275; -.
KEGG; hsa:3275; -.
UCSC; uc002zjx.5; human. [P55345-1]
CTD; 3275; -.
DisGeNET; 3275; -.
EuPathDB; HostDB:ENSG00000160310.16; -.
GeneCards; PRMT2; -.
HGNC; HGNC:5186; PRMT2.
HPA; HPA018976; -.
HPA; HPA029591; -.
MIM; 601961; gene.
neXtProt; NX_P55345; -.
OpenTargets; ENSG00000160310; -.
PharmGKB; PA29460; -.
eggNOG; KOG1499; Eukaryota.
eggNOG; ENOG410XQYH; LUCA.
GeneTree; ENSGT00550000074406; -.
HOGENOM; HOG000198521; -.
HOVERGEN; HBG105734; -.
InParanoid; P55345; -.
KO; K11435; -.
OMA; PCTILQL; -.
OrthoDB; EOG091G0A0U; -.
PhylomeDB; P55345; -.
TreeFam; TF332196; -.
BRENDA; 2.1.1.125; 2681.
ChiTaRS; PRMT2; human.
EvolutionaryTrace; P55345; -.
GeneWiki; PRMT2; -.
GenomeRNAi; 3275; -.
PRO; PR:P55345; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000160310; -.
CleanEx; HS_PRMT2; -.
ExpressionAtlas; P55345; baseline and differential.
Genevisible; P55345; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IDA:UniProtKB.
GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:UniProtKB.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:UniProtKB.
GO; GO:0033142; F:progesterone receptor binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISS:UniProtKB.
GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IBA:GO_Central.
GO; GO:0042974; F:retinoic acid receptor binding; IPI:UniProtKB.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0046966; F:thyroid hormone receptor binding; IPI:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0048588; P:developmental cell growth; ISS:UniProtKB.
GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IGI:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006479; P:protein methylation; TAS:ProtInc.
GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR007848; Small_mtfrase_dom.
Pfam; PF05175; MTS; 1.
Pfam; PF14604; SH3_9; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Methylation; Methyltransferase; Nucleus; Reference proteome;
S-adenosyl-L-methionine; SH3 domain; Transferase.
CHAIN 1 433 Protein arginine N-methyltransferase 2.
/FTId=PRO_0000212324.
DOMAIN 30 89 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 99 432 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
REGION 1 277 Interaction with ESR1.
REGION 83 207 Interaction with RB1. {ECO:0000250}.
REGION 133 275 Interaction with ESR1.
ACT_SITE 211 211 {ECO:0000250}.
ACT_SITE 220 220 {ECO:0000250}.
BINDING 112 112 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 121 121 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 145 145 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
BINDING 168 168 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 197 197 S-adenosyl-L-methionine. {ECO:0000250}.
MOD_RES 61 61 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 72 72 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 219 433 FEFMIESILYARDAWLKEDGVIWPTMAALHLVPCSADKDYR
SKVLFWDNAYEFNLSALKSLAVKEFFSKPKYNHILKPEDCL
SEPCTILQLDMRTVQISDLETLRGELRFDIRKAGTLHGFTA
WFSVHFQSLQEGQPPQVLSTGPFHPTTHWKQTLFMMDDPVP
VHTGDVVTGSVVLQRNPVWRRHMSVALSWAVTSRQDPTSQK
VGEKVFPIWR -> AAPLLSCRILPCTCASGPLHVLLACCL
PLPCTCASVPLHVLLACCLPVLRAPQPSGLHLSWPIFLL
(in isoform 2).
{ECO:0000303|PubMed:9110174}.
/FTId=VSP_042680.
VAR_SEQ 219 423 Missing (in isoform PRMT2Gamma).
{ECO:0000303|PubMed:22093364}.
/FTId=VSP_054927.
VAR_SEQ 219 320 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043381.
VAR_SEQ 219 301 FEFMIESILYARDAWLKEDGVIWPTMAALHLVPCSADKDYR
SKVLFWDNAYEFNLSALKSLAVKEFFSKPKYNHILKPEDCL
S -> HHTLEADAVHDGRPSPCPYRRRGHGFSCVAEKPSVE
KAHVCGSELGCHFQTRPHISKSWRKSLPHLEMTVDALFGKQ
CAYLEG (in isoform PRMT2Beta).
{ECO:0000303|PubMed:22093364}.
/FTId=VSP_054928.
VAR_SEQ 278 433 Missing (in isoform PRMT2L2).
{ECO:0000303|PubMed:21820040}.
/FTId=VSP_054929.
VAR_SEQ 278 289 SLAVKEFFSKPK -> LEKKSSPSGDDS (in isoform
PRMT2Alpha).
{ECO:0000303|PubMed:22093364}.
/FTId=VSP_054930.
VAR_SEQ 290 433 Missing (in isoform PRMT2Alpha).
{ECO:0000303|PubMed:22093364}.
/FTId=VSP_054931.
VAR_SEQ 302 433 Missing (in isoform PRMT2Beta).
{ECO:0000303|PubMed:22093364}.
/FTId=VSP_054932.
CONFLICT 256 260 KDYRS -> RIIVA (in Ref. 2; AAB48437).
{ECO:0000305}.
CONFLICT 402 402 R -> I (in Ref. 10; AAH00727).
{ECO:0000305}.
STRAND 34 39 {ECO:0000244|PDB:1X2P}.
STRAND 56 61 {ECO:0000244|PDB:1X2P}.
STRAND 64 71 {ECO:0000244|PDB:1X2P}.
STRAND 77 85 {ECO:0000244|PDB:1X2P}.
SEQUENCE 433 AA; 49042 MW; 6DEE0350C15ECD4F CRC64;
MATSGDCPRS ESQGEEPAEC SEAGLLQEGV QPEEFVAIAD YAATDETQLS FLRGEKILIL
RQTTADWWWG ERAGCCGYIP ANHVGKHVDE YDPEDTWQDE EYFGSYGTLK LHLEMLADQP
RTTKYHSVIL QNKESLTDKV ILDVGCGTGI ISLFCAHYAR PRAVYAVEAS EMAQHTGQLV
LQNGFADIIT VYQQKVEDVV LPEKVDVLVS EWMGTCLLFE FMIESILYAR DAWLKEDGVI
WPTMAALHLV PCSADKDYRS KVLFWDNAYE FNLSALKSLA VKEFFSKPKY NHILKPEDCL
SEPCTILQLD MRTVQISDLE TLRGELRFDI RKAGTLHGFT AWFSVHFQSL QEGQPPQVLS
TGPFHPTTHW KQTLFMMDDP VPVHTGDVVT GSVVLQRNPV WRRHMSVALS WAVTSRQDPT
SQKVGEKVFP IWR


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