ANM2_HUMAN
ID ANM2_HUMAN Reviewed; 433 AA.
AC P55345; B7U630; B7U631; B7U632; P78350; Q498Y5; Q5U7D4; Q6FHF0; Q99781;
AC Q9BW15; Q9UMC2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Protein arginine N-methyltransferase 2;
DE EC=2.1.1.319 {ECO:0000269|PubMed:19405910};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT2;
GN Name=PRMT2; Synonyms=HMT1, HRMT1L1;
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 [MRNA] (ISOFORM 1).
RX PubMed=9545638; DOI=10.1006/geno.1997.5190;
RA Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A.,
RA Henry M.F.;
RT "Identification and characterization of two putative human arginine
RT methyltransferases (HRMT1L1 and HRMT1L2).";
RL Genomics 48:330-340(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9196002; DOI=10.1007/s003359900491;
RA Katsanis N., Yaspo M.-L., Fisher E.M.C.;
RT "Identification and mapping of a novel human gene, HRMT1L1, homologous to
RT the rat protein arginine N-methyltransferase 1 (PRMT1) gene.";
RL Mamm. Genome 8:526-529(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PRMT2L2), AND SUBCELLULAR LOCATION
RP (ISOFORM PRMT2L2).
RX PubMed=21820040; DOI=10.1016/j.gene.2011.06.022;
RA Zhong J., Cao R.X., Hong T., Yang J., Zu X.Y., Xiao X.H., Liu J.H.,
RA Wen G.B.;
RT "Identification and expression analysis of a novel transcript of the human
RT PRMT2 gene resulted from alternative polyadenylation in breast cancer.";
RL Gene 487:1-9(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PRMT2ALPHA; PRMT2BETA AND PRMT2GAMMA),
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AR AND ESR1.
RX PubMed=22093364; DOI=10.1111/j.1742-4658.2011.08426.x;
RA Zhong J., Cao R.X., Zu X.Y., Hong T., Yang J., Liu L., Xiao X.H.,
RA Ding W.J., Zhao Q., Liu J.H., Wen G.B.;
RT "Identification and characterization of novel spliced variants of PRMT2 in
RT breast carcinoma.";
RL FEBS J. 279:316-335(2012).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Chondrosarcoma, and Kidney;
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-277 (ISOFORM 1).
RG The European IMAGE consortium;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP INTERACTION WITH HNRNPUL1, AND SUBCELLULAR LOCATION.
RX PubMed=11513728; DOI=10.1042/0264-6021:3580305;
RA Kzhyshkowska J., Schuett H., Liss M., Kremmer E., Stauber R., Wolf H.,
RA Dobner T.;
RT "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-
RT Gly-Gly (RGG) box and interacts with human arginine methyltransferase
RT HRMT1L1.";
RL Biochem. J. 358:305-314(2001).
RN [13]
RP FUNCTION, AND INTERACTION WITH ESR1; ESR2; NCOA1; NCOA6; PGR; PPARG; RARA;
RP RXRA AND THRB.
RX PubMed=12039952; DOI=10.1074/jbc.m201053200;
RA Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
RT "Identification of protein arginine methyltransferase 2 as a coactivator
RT for estrogen receptor alpha.";
RL J. Biol. Chem. 277:28624-28630(2002).
RN [14]
RP FUNCTION, AND INTERACTION WITH NFKBIA.
RX PubMed=16648481; DOI=10.1128/mcb.26.10.3864-3874.2006;
RA Ganesh L., Yoshimoto T., Moorthy N.C., Akahata W., Boehm M., Nabel E.G.,
RA Nabel G.J.;
RT "Protein methyltransferase 2 inhibits NF-kappaB function and promotes
RT apoptosis.";
RL Mol. Cell. Biol. 26:3864-3874(2006).
RN [15]
RP INTERACTION WITH PRMT8.
RX PubMed=17925405; DOI=10.1074/jbc.m704650200;
RA Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G.;
RT "Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its
RT N-terminal domain.";
RL J. Biol. Chem. 282:36444-36453(2007).
RN [16]
RP FUNCTION, INTERACTION WITH AR AND ESR1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17587566; DOI=10.1016/j.jsbmb.2007.05.006;
RA Meyer R., Wolf S.S., Obendorf M.;
RT "PRMT2, a member of the protein arginine methyltransferase family, is a
RT coactivator of the androgen receptor.";
RL J. Steroid Biochem. Mol. Biol. 107:1-14(2007).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-61 AND ARG-72, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [19]
RP STRUCTURE BY NMR OF 33-87.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of the protein arginine N-
RT methyltransferase 2.";
RL Submitted (OCT-2005) to the PDB data bank.
CC -!- FUNCTION: Arginine methyltransferase that methylates the guanidino
CC nitrogens of arginyl residues in proteins such as STAT3, FBL, histone
CC H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-
CC mediated transactivation. Acts as a coactivator (with estrogen) of
CC estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG,
CC RARA-mediated transactivation. May inhibit NF-kappa-B transcription and
CC promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-
CC dependent manner). May be involved in growth regulation.
CC {ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:16648481,
CC ECO:0000269|PubMed:17587566, 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for AdoMet {ECO:0000269|PubMed:19405910};
CC KM=3.3 uM for H4 {ECO:0000269|PubMed:19405910};
CC Vmax=1.4 pmol/min/mg enzyme toward S-adenosyl-L-methionine (AdoMet)
CC {ECO:0000269|PubMed:19405910};
CC Vmax=1.5 pmol/min/mg enzyme toward histone H4
CC {ECO:0000269|PubMed:19405910};
CC -!- SUBUNIT: Self-associates. Interacts with RB1 and E2F1 (By similarity).
CC Interacts with NCOA6 coactivator. Interacts (via SH3 domain) with
CC PRMT8. Interacts with AR. Interacts with NFKBIA. Interacts with ESR1,
CC ESR2, PGR, PPARG, RARA, RXRA and THRB. Interacts with HNRNPUL1.
CC {ECO:0000250, ECO:0000269|PubMed:11513728, ECO:0000269|PubMed:12039952,
CC ECO:0000269|PubMed:16648481, ECO:0000269|PubMed:17587566,
CC ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:22093364}.
CC -!- INTERACTION:
CC P55345; Q13191: CBLB; NbExp=3; IntAct=EBI-78458, EBI-744027;
CC P55345; P03372: ESR1; NbExp=9; IntAct=EBI-78458, EBI-78473;
CC P55345; P42858: HTT; NbExp=3; IntAct=EBI-78458, EBI-466029;
CC P55345; P06400: RB1; NbExp=3; IntAct=EBI-78458, EBI-491274;
CC P55345; Q9NTZ6: RBM12; NbExp=3; IntAct=EBI-78458, EBI-310707;
CC P55345; Q15637: SF1; NbExp=5; IntAct=EBI-78458, EBI-744603;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus.
CC Note=Translocates from the cytoplasm to the nucleus, after hormone
CC exposure. Excluded from nucleolus.
CC -!- SUBCELLULAR LOCATION: [Isoform PRMT2Alpha]: Nucleus. Note=Excluded from
CC nucleolus.
CC -!- SUBCELLULAR LOCATION: [Isoform PRMT2Beta]: Cytoplasm. Nucleus. Nucleus,
CC nucleolus.
CC -!- SUBCELLULAR LOCATION: [Isoform PRMT2Gamma]: Nucleus. Note=Excluded from
CC nucleolus.
CC -!- SUBCELLULAR LOCATION: [Isoform PRMT2L2]: Cytoplasm
CC {ECO:0000269|PubMed:21820040}. Nucleus {ECO:0000269|PubMed:21820040}.
CC Note=Predominantly cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=P55345-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55345-2; Sequence=VSP_042680;
CC Name=3;
CC IsoId=P55345-3; Sequence=VSP_043381;
CC Name=PRMT2Alpha;
CC IsoId=P55345-4; Sequence=VSP_054930, VSP_054931;
CC Name=PRMT2Beta;
CC IsoId=P55345-5; Sequence=VSP_054928, VSP_054932;
CC Name=PRMT2Gamma;
CC IsoId=P55345-6; Sequence=VSP_054927;
CC Name=PRMT2L2;
CC IsoId=P55345-7; Sequence=VSP_054929;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in androgen
CC target organs such as heart, prostate, skeletal muscle, ovary and
CC spinal cord. {ECO:0000269|PubMed:17587566}.
CC -!- MISCELLANEOUS: [Isoform PRMT2Alpha]: Higher expression in breast cancer
CC tissues. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform PRMT2Beta]: Higher expression in breast cancer
CC tissues. Doesn't interact with ESR1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform PRMT2Gamma]: Higher expression in breast cancer
CC tissues. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; X99209; CAA67599.1; -; mRNA.
DR EMBL; U80213; AAB48437.1; -; mRNA.
DR EMBL; AY786414; AAV48568.2; -; mRNA.
DR EMBL; FJ436410; ACJ66866.1; -; mRNA.
DR EMBL; FJ436411; ACJ66867.1; -; mRNA.
DR EMBL; FJ436412; ACJ66868.1; -; mRNA.
DR EMBL; U79286; AAB50221.1; -; mRNA.
DR EMBL; CR541804; CAG46603.1; -; mRNA.
DR EMBL; AK123650; BAG53931.1; -; mRNA.
DR EMBL; AP000339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09259.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09265.1; -; Genomic_DNA.
DR EMBL; BC000727; AAH00727.1; -; mRNA.
DR EMBL; BC100026; AAI00027.1; -; mRNA.
DR EMBL; AL109794; CAB52454.1; -; mRNA.
DR CCDS; CCDS13737.1; -. [P55345-1]
DR CCDS; CCDS56219.1; -. [P55345-2]
DR CCDS; CCDS56220.1; -. [P55345-3]
DR CCDS; CCDS68230.1; -. [P55345-4]
DR CCDS; CCDS68231.1; -. [P55345-5]
DR CCDS; CCDS74806.1; -. [P55345-6]
DR RefSeq; NP_001229793.1; NM_001242864.2. [P55345-3]
DR RefSeq; NP_001229794.1; NM_001242865.2. [P55345-2]
DR RefSeq; NP_001229795.1; NM_001242866.2. [P55345-7]
DR RefSeq; NP_001273605.1; NM_001286676.1. [P55345-5]
DR RefSeq; NP_001273606.1; NM_001286677.1. [P55345-4]
DR RefSeq; NP_001273607.1; NM_001286678.1. [P55345-6]
DR RefSeq; NP_001526.2; NM_001535.4. [P55345-1]
DR RefSeq; NP_996845.1; NM_206962.3. [P55345-1]
DR RefSeq; XP_005261168.1; XM_005261111.3. [P55345-1]
DR RefSeq; XP_006724061.1; XM_006723998.3. [P55345-5]
DR RefSeq; XP_006724063.1; XM_006724000.2. [P55345-6]
DR PDB; 1X2P; NMR; -; A=33-87.
DR PDBsum; 1X2P; -.
DR AlphaFoldDB; P55345; -.
DR SMR; P55345; -.
DR BioGRID; 109511; 72.
DR CORUM; P55345; -.
DR IntAct; P55345; 54.
DR MINT; P55345; -.
DR STRING; 9606.ENSP00000380759; -.
DR iPTMnet; P55345; -.
DR PhosphoSitePlus; P55345; -.
DR SwissPalm; P55345; -.
DR BioMuta; PRMT2; -.
DR DMDM; 2499805; -.
DR EPD; P55345; -.
DR jPOST; P55345; -.
DR MassIVE; P55345; -.
DR PaxDb; P55345; -.
DR PeptideAtlas; P55345; -.
DR PRIDE; P55345; -.
DR ProteomicsDB; 56853; -. [P55345-1]
DR ProteomicsDB; 56854; -. [P55345-2]
DR ProteomicsDB; 56855; -. [P55345-3]
DR ProteomicsDB; 6261; -.
DR ProteomicsDB; 6262; -.
DR ProteomicsDB; 6263; -.
DR Antibodypedia; 10796; 473 antibodies from 31 providers.
DR DNASU; 3275; -.
DR Ensembl; ENST00000291705.11; ENSP00000291705.6; ENSG00000160310.19. [P55345-6]
DR Ensembl; ENST00000334494.8; ENSP00000335490.4; ENSG00000160310.19. [P55345-2]
DR Ensembl; ENST00000355680.8; ENSP00000347906.3; ENSG00000160310.19. [P55345-1]
DR Ensembl; ENST00000397637.5; ENSP00000380759.1; ENSG00000160310.19. [P55345-1]
DR Ensembl; ENST00000397638.6; ENSP00000380760.2; ENSG00000160310.19. [P55345-1]
DR Ensembl; ENST00000440086.5; ENSP00000397266.1; ENSG00000160310.19. [P55345-3]
DR Ensembl; ENST00000451211.6; ENSP00000411984.2; ENSG00000160310.19. [P55345-4]
DR Ensembl; ENST00000458387.6; ENSP00000407463.2; ENSG00000160310.19. [P55345-5]
DR GeneID; 3275; -.
DR KEGG; hsa:3275; -.
DR MANE-Select; ENST00000355680.8; ENSP00000347906.3; NM_206962.4; NP_996845.1.
DR UCSC; uc002zjx.5; human. [P55345-1]
DR CTD; 3275; -.
DR DisGeNET; 3275; -.
DR GeneCards; PRMT2; -.
DR HGNC; HGNC:5186; PRMT2.
DR HPA; ENSG00000160310; Low tissue specificity.
DR MIM; 601961; gene.
DR neXtProt; NX_P55345; -.
DR OpenTargets; ENSG00000160310; -.
DR PharmGKB; PA29460; -.
DR VEuPathDB; HostDB:ENSG00000160310; -.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000160683; -.
DR HOGENOM; CLU_017375_4_0_1; -.
DR InParanoid; P55345; -.
DR OMA; MWVAPIR; -.
DR PhylomeDB; P55345; -.
DR TreeFam; TF332196; -.
DR BioCyc; MetaCyc:HS08486-MON; -.
DR BRENDA; 2.1.1.319; 2681.
DR PathwayCommons; P55345; -.
DR SignaLink; P55345; -.
DR BioGRID-ORCS; 3275; 29 hits in 1096 CRISPR screens.
DR ChiTaRS; PRMT2; human.
DR EvolutionaryTrace; P55345; -.
DR GeneWiki; PRMT2; -.
DR GenomeRNAi; 3275; -.
DR Pharos; P55345; Tbio.
DR PRO; PR:P55345; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P55345; protein.
DR Bgee; ENSG00000160310; Expressed in cortical plate and 197 other tissues.
DR ExpressionAtlas; P55345; baseline and differential.
DR Genevisible; P55345; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:0033142; F:nuclear progesterone receptor binding; IPI:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:UniProtKB.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0048588; P:developmental cell growth; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006479; P:protein methylation; TAS:ProtInc.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Methylation;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW SH3 domain; Transferase.
FT CHAIN 1..433
FT /note="Protein arginine N-methyltransferase 2"
FT /id="PRO_0000212324"
FT DOMAIN 30..89
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 99..432
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 1..277
FT /note="Interaction with ESR1"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..207
FT /note="Interaction with RB1"
FT /evidence="ECO:0000250"
FT REGION 133..275
FT /note="Interaction with ESR1"
FT ACT_SITE 211
FT /evidence="ECO:0000250"
FT ACT_SITE 220
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 72
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 219..433
FT /note="FEFMIESILYARDAWLKEDGVIWPTMAALHLVPCSADKDYRSKVLFWDNAYE
FT FNLSALKSLAVKEFFSKPKYNHILKPEDCLSEPCTILQLDMRTVQISDLETLRGELRFD
FT IRKAGTLHGFTAWFSVHFQSLQEGQPPQVLSTGPFHPTTHWKQTLFMMDDPVPVHTGDV
FT VTGSVVLQRNPVWRRHMSVALSWAVTSRQDPTSQKVGEKVFPIWR -> AAPLLSCRIL
FT PCTCASGPLHVLLACCLPLPCTCASVPLHVLLACCLPVLRAPQPSGLHLSWPIFLL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9110174"
FT /id="VSP_042680"
FT VAR_SEQ 219..423
FT /note="Missing (in isoform PRMT2Gamma)"
FT /evidence="ECO:0000303|PubMed:22093364"
FT /id="VSP_054927"
FT VAR_SEQ 219..320
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043381"
FT VAR_SEQ 219..301
FT /note="FEFMIESILYARDAWLKEDGVIWPTMAALHLVPCSADKDYRSKVLFWDNAYE
FT FNLSALKSLAVKEFFSKPKYNHILKPEDCLS -> HHTLEADAVHDGRPSPCPYRRRGH
FT GFSCVAEKPSVEKAHVCGSELGCHFQTRPHISKSWRKSLPHLEMTVDALFGKQCAYLEG
FT (in isoform PRMT2Beta)"
FT /evidence="ECO:0000303|PubMed:22093364"
FT /id="VSP_054928"
FT VAR_SEQ 278..433
FT /note="Missing (in isoform PRMT2L2)"
FT /evidence="ECO:0000303|PubMed:21820040"
FT /id="VSP_054929"
FT VAR_SEQ 278..289
FT /note="SLAVKEFFSKPK -> LEKKSSPSGDDS (in isoform
FT PRMT2Alpha)"
FT /evidence="ECO:0000303|PubMed:22093364"
FT /id="VSP_054930"
FT VAR_SEQ 290..433
FT /note="Missing (in isoform PRMT2Alpha)"
FT /evidence="ECO:0000303|PubMed:22093364"
FT /id="VSP_054931"
FT VAR_SEQ 302..433
FT /note="Missing (in isoform PRMT2Beta)"
FT /evidence="ECO:0000303|PubMed:22093364"
FT /id="VSP_054932"
FT CONFLICT 256..260
FT /note="KDYRS -> RIIVA (in Ref. 2; AAB48437)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="R -> I (in Ref. 10; AAH00727)"
FT /evidence="ECO:0000305"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1X2P"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1X2P"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1X2P"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:1X2P"
SQ 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
