ANM1_HUMAN
ID ANM1_HUMAN Reviewed; 371 AA.
AC Q99873; A0A087X1W2; B4E3C3; G5E9B6; H7C2I1; Q15529; Q2VP93; Q6LEU5; Q8WUW5;
AC Q99872; Q99874; Q9NZ04; Q9NZ05; Q9NZ06;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Protein arginine N-methyltransferase 1 {ECO:0000305};
DE EC=2.1.1.319 {ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:22095282, ECO:0000269|PubMed:26575292, ECO:0000269|PubMed:28040436};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT1;
DE AltName: Full=Interferon receptor 1-bound protein 4;
GN Name=PRMT1 {ECO:0000312|HGNC:HGNC:5187};
GN Synonyms=HMT2, HRMT1L2 {ECO:0000303|PubMed:11097842,
GN ECO:0000303|PubMed:9545638}, IR1B4;
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], AND ALTERNATIVE SPLICING.
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].
RC TISSUE=Glial cell;
RX PubMed=8675017; DOI=10.1016/0378-1119(96)00073-x;
RA Nikawa J., Nakano H., Ohi N.;
RT "Structural and functional conservation of human and yeast HCP1 genes which
RT can suppress the growth defect of the Saccharomyces cerevisiae ire15
RT mutant.";
RL Gene 171:107-111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=11097842; DOI=10.1006/bbrc.2000.3807;
RA Scorilas A., Black M.H., Talieri M., Diamandis E.P.;
RT "Genomic organization, physical mapping, and expression analysis of the
RT human protein arginine methyltransferase 1 gene.";
RL Biochem. Biophys. Res. Commun. 278:349-359(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lung;
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 [9]
RP FUNCTION, INTERACTION WITH ILF3, AND SUBCELLULAR LOCATION.
RX PubMed=10749851; DOI=10.1074/jbc.m000023200;
RA Tang J., Kao P.N., Herschman H.R.;
RT "Protein-arginine methyltransferase I, the predominant protein-arginine
RT methyltransferase in cells, interacts with and is regulated by interleukin
RT enhancer-binding factor 3.";
RL J. Biol. Chem. 275:19866-19876(2000).
RN [10]
RP SUBUNIT.
RX PubMed=11101900; DOI=10.1038/82028;
RA Weiss V.H., McBride A.E., Soriano M.A., Filman D.J., Silver P.A.,
RA Hogle J.M.;
RT "The structure and oligomerization of the yeast arginine methyltransferase,
RT Hmt1.";
RL Nat. Struct. Biol. 7:1165-1171(2000).
RN [11]
RP FUNCTION IN METHYLATION OF HISTONE H4, AND CATALYTIC ACTIVITY.
RX PubMed=11448779; DOI=10.1016/s0960-9822(01)00294-9;
RA Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H.,
RA Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.;
RT "Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by
RT the nuclear receptor coactivator PRMT1.";
RL Curr. Biol. 11:996-1000(2001).
RN [12]
RP FUNCTION IN METHYLATION OF HISTONE H4, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11387442; DOI=10.1126/science.1060781;
RA Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H., Strahl B.D.,
RA Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.;
RT "Methylation of histone H4 at arginine 3 facilitating transcriptional
RT activation by nuclear hormone receptor.";
RL Science 293:853-857(2001).
RN [13]
RP FUNCTION, AND INTERACTION WITH SUPT5H.
RX PubMed=12718890; DOI=10.1016/s1097-2765(03)00101-1;
RA Kwak Y.T., Guo J., Prajapati S., Park K.-J., Surabhi R.M., Miller B.,
RA Gehrig P., Gaynor R.B.;
RT "Methylation of SPT5 regulates its interaction with RNA polymerase II and
RT transcriptional elongation properties.";
RL Mol. Cell 11:1055-1066(2003).
RN [14]
RP INTERACTION WITH DHX9.
RX PubMed=15084609; DOI=10.1074/jbc.c300512200;
RA Smith W.A., Schurter B.T., Wong-Staal F., David M.;
RT "Arginine methylation of RNA helicase a determines its subcellular
RT localization.";
RL J. Biol. Chem. 279:22795-22798(2004).
RN [15]
RP FUNCTION IN METHYLATION OF HABP4 AND SERBP1, SUBUNIT, INTERACTION WITH
RP HABP4, AND SUBCELLULAR LOCATION.
RX PubMed=16879614; DOI=10.1111/j.1742-4658.2006.05399.x;
RA Passos D.O., Bressan G.C., Nery F.C., Kobarg J.;
RT "Ki-1/57 interacts with PRMT1 and is a substrate for arginine
RT methylation.";
RL FEBS J. 273:3946-3961(2006).
RN [16]
RP FUNCTION.
RX PubMed=18657504; DOI=10.1016/j.molcel.2008.05.025;
RA Le Romancer M., Treilleux I., Leconte N., Robin-Lespinasse Y., Sentis S.,
RA Bouchekioua-Bouzaghou K., Goddard S., Gobert-Gosse S., Corbo L.;
RT "Regulation of estrogen rapid signaling through arginine methylation by
RT PRMT1.";
RL Mol. Cell 31:212-221(2008).
RN [17]
RP FUNCTION, INTERACTION WITH FOXO1, AND MUTAGENESIS OF VAL-92; LEU-93 AND
RP ASP-94.
RX PubMed=18951090; DOI=10.1016/j.molcel.2008.09.013;
RA Yamagata K., Daitoku H., Takahashi Y., Namiki K., Hisatake K., Kako K.,
RA Mukai H., Kasuya Y., Fukamizu A.;
RT "Arginine methylation of FOXO transcription factors inhibits their
RT phosphorylation by Akt.";
RL Mol. Cell 32:221-231(2008).
RN [18]
RP FUNCTION.
RX PubMed=18773938; DOI=10.1016/j.neulet.2008.08.065;
RA Miyata S., Mori Y., Tohyama M.;
RT "PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells.";
RL Neurosci. Lett. 445:162-165(2008).
RN [19]
RP FUNCTION, AND INTERACTION WITH EWS AND PRMT8.
RX PubMed=18320585; DOI=10.1002/prot.22004;
RA Pahlich S., Zakaryan R.P., Gehring H.;
RT "Identification of proteins interacting with protein arginine
RT methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of
RT its methylation state.";
RL Proteins 72:1125-1137(2008).
RN [20]
RP FUNCTION.
RX PubMed=19124016; DOI=10.1016/j.yexcr.2008.12.008;
RA Jobert L., Argentini M., Tora L.;
RT "PRMT1 mediated methylation of TAF15 is required for its positive gene
RT regulatory function.";
RL Exp. Cell Res. 315:1273-1286(2009).
RN [21]
RP RETRACTED PAPER.
RX PubMed=19136629; DOI=10.1101/gad.489409;
RA Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.;
RT "PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling.";
RL Genes Dev. 23:118-132(2009).
RN [22]
RP RETRACTION NOTICE OF PUBMED:19136629.
RX PubMed=21724836;
RA Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.;
RT "Retraction. PRMT1-mediated arginine methylation of PIAS1 regulates STAT1
RT signaling.";
RL Genes Dev. 25:1451-1451(2011).
RN [23]
RP FUNCTION.
RX PubMed=20442406; DOI=10.1074/jbc.m109.092411;
RA Chang Y.I., Hua W.K., Yao C.L., Hwang S.M., Hung Y.C., Kuan C.J.,
RA Leou J.S., Lin W.J.;
RT "Protein-arginine methyltransferase 1 suppresses megakaryocytic
RT differentiation via modulation of the p38 MAPK pathway in K562 cells.";
RL J. Biol. Chem. 285:20595-20606(2010).
RN [24]
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 [25]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH MAP3K5.
RX PubMed=22095282; DOI=10.1038/cdd.2011.168;
RA Cho J.H., Lee M.K., Yoon K.W., Lee J., Cho S.G., Choi E.J.;
RT "Arginine methylation-dependent regulation of ASK1 signaling by PRMT1.";
RL Cell Death Differ. 19:859-870(2012).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP FUNCTION, INTERACTION WITH CHTOP, AND IDENTIFICATION IN THE METHYLOSOME
RP COMPLEX WITH PRMT5; WRD77 AND ERH.
RX PubMed=25284789; DOI=10.1016/j.celrep.2014.08.071;
RA Takai H., Masuda K., Sato T., Sakaguchi Y., Suzuki T., Suzuki T.,
RA Koyama-Nasu R., Nasu-Nishimura Y., Katou Y., Ogawa H., Morishita Y.,
RA Kozuka-Hata H., Oyama M., Todo T., Ino Y., Mukasa A., Saito N.,
RA Toyoshima C., Shirahige K., Akiyama T.;
RT "5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by
RT recruiting the CHTOP-methylosome complex.";
RL Cell Rep. 9:48-60(2014).
RN [28]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26575292; DOI=10.7554/elife.07938;
RA Zhang L., Tran N.T., Su H., Wang R., Lu Y., Tang H., Aoyagi S., Guo A.,
RA Khodadadi-Jamayran A., Zhou D., Qian K., Hricik T., Cote J., Han X.,
RA Zhou W., Laha S., Abdel-Wahab O., Levine R.L., Raffel G., Liu Y., Chen D.,
RA Li H., Townes T., Wang H., Deng H., Zheng Y.G., Leslie C., Luo M., Zhao X.;
RT "Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15
RT controls RNA splicing.";
RL Elife 4:0-0(2015).
RN [29]
RP INTERACTION WITH ATXN2L.
RX PubMed=25748791; DOI=10.1016/j.yexcr.2015.02.022;
RA Kaehler C., Guenther A., Uhlich A., Krobitsch S.;
RT "PRMT1-mediated arginine methylation controls ATXN2L localization.";
RL Exp. Cell Res. 334:114-125(2015).
RN [30]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, S-ADENOSYL-L-METHIONINE-BINDING,
RP AND MUTAGENESIS OF TYR-280; TYR-322 AND LEU-359.
RX PubMed=26876602; DOI=10.1016/j.jmb.2016.02.007;
RA Toma-Fukai S., Kim J.D., Park K.E., Kuwabara N., Shimizu N., Krayukhina E.,
RA Uchiyama S., Fukamizu A., Shimizu T.;
RT "Novel helical assembly in arginine methyltransferase 8.";
RL J. Mol. Biol. 428:1197-1208(2016).
RN [31]
RP INTERACTION WITH TRIM48, AND UBIQUITINATION.
RX PubMed=29186683; DOI=10.1016/j.celrep.2017.11.007;
RA Hirata Y., Katagiri K., Nagaoka K., Morishita T., Kudoh Y., Hatta T.,
RA Naguro I., Kano K., Udagawa T., Natsume T., Aoki J., Inada T., Noguchi T.,
RA Ichijo H., Matsuzawa A.;
RT "TRIM48 Promotes ASK1 Activation and Cell Death through Ubiquitination-
RT Dependent Degradation of the ASK1-Negative Regulator PRMT1.";
RL Cell Rep. 21:2447-2457(2017).
RN [32]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=28040436; DOI=10.1016/j.biocel.2016.12.013;
RA Akter K.A., Mansour M.A., Hyodo T., Senga T.;
RT "FAM98A associates with DDX1-C14orf166-FAM98B in a novel complex involved
RT in colorectal cancer progression.";
RL Int. J. Biochem. Cell Biol. 84:1-13(2017).
CC -!- FUNCTION: Arginine methyltransferase that methylates (mono and
CC asymmetric dimethylation) the guanidino nitrogens of arginyl residues
CC present in proteins such as ESR1, histone H2, H3 and H4, ILF3, HNRNPA1,
CC HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1,
CC CHTOP and MAP3K5/ASK1 (PubMed:10749851, PubMed:16879614,
CC PubMed:26876602, PubMed:22095282, PubMed:26575292, PubMed:18951090,
CC PubMed:25284789). Constitutes the main enzyme that mediates
CC monomethylation and asymmetric dimethylation of histone H4 'Arg-4'
CC (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic
CC transcriptional activation. May be involved in the regulation of TAF15
CC transcriptional activity, act as an activator of estrogen receptor
CC (ER)-mediated transactivation, play a key role in neurite outgrowth and
CC act as a negative regulator of megakaryocytic differentiation, by
CC modulating p38 MAPK pathway. Methylates RBM15, promoting ubiquitination
CC and degradation of RBM15 (PubMed:26575292). Methylates FOXO1 and
CC retains it in the nucleus increasing its transcriptional activity
CC (PubMed:18951090). Methylates CHTOP and this methylation is critical
CC for its 5-hydroxymethylcytosine (5hmC)-binding activity
CC (PubMed:25284789). Methylates MAP3K5/ASK1 at 'Arg-78' and 'Arg-80'
CC which promotes association of MAP3K5 with thioredoxin and negatively
CC regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation
CC and MAP3K5-induced activation of JNK (PubMed:22095282). Methylates H4R3
CC in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-
CC dependent manner (PubMed:25284789). Plays a role in regulating
CC alternative splicing in the heart (By similarity).
CC {ECO:0000250|UniProtKB:Q9JIF0, ECO:0000269|PubMed:10749851,
CC ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779,
CC ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:16879614,
CC ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:18657504,
CC ECO:0000269|PubMed:18773938, ECO:0000269|PubMed:19124016,
CC ECO:0000269|PubMed:20442406, ECO:0000269|PubMed:22095282,
CC ECO:0000269|PubMed:25284789, ECO:0000269|PubMed:26575292,
CC ECO:0000269|PubMed:26876602, ECO:0000269|PubMed:28040436}.
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:11387442, ECO:0000269|PubMed:11448779,
CC ECO:0000269|PubMed:22095282, ECO:0000269|PubMed:26575292,
CC ECO:0000269|PubMed:28040436};
CC -!- ACTIVITY REGULATION: By BTG1, BTG2 and ILF3.
CC -!- SUBUNIT: Homodimer (PubMed:16879614, PubMed:26876602). Homooctamer;
CC individual homodimers associates to form a homooctamer
CC (PubMed:26876602). Individual homodimers can associate to form a
CC homohexamer. Heterodimer with PRMT8. Interacts with BTG1, BTG2,
CC NFATC2IP and IFNAR1 (By similarity). Interacts with and methylates
CC CHTOP, thereby enabling the interaction of CHTOP with the 5FMC complex
CC (PubMed:25284789). Interacts with ILF3 and SUPT5H. Interacts with and
CC methylates FOXO1, leading to the nuclear retention of FOXO1 and the
CC stimulation of FOXO1 transcriptional activity. Methylation of FOXO1 is
CC increased upon oxidative stress. Interacts with and probably methylates
CC ATXN2L (PubMed:25748791). Component of the methylosome, a 20S complex
CC containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and
CC ERH (PubMed:25284789). Interacts with DHX9 (via RGG region)
CC (PubMed:15084609). Interacts (via N-terminus) with HABP4
CC (PubMed:16879614). Interacts with MAP3K5/ASK1; the interaction results
CC in MAP3K5 methylation by PRMT1 which inhibits MAP3K5 activation
CC (PubMed:22095282). Interacts with TRIM48; the interaction results in
CC ubiquitination of PRMT1 by TRIM48, leading to PRMT1 proteasomal
CC degradation and activation of MAP3K5 (PubMed:29186683).
CC {ECO:0000250|UniProtKB:Q9JIF0, ECO:0000269|PubMed:10749851,
CC ECO:0000269|PubMed:11101900, ECO:0000269|PubMed:12718890,
CC ECO:0000269|PubMed:15084609, ECO:0000269|PubMed:16879614,
CC ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:18951090,
CC ECO:0000269|PubMed:22095282, ECO:0000269|PubMed:25284789,
CC ECO:0000269|PubMed:25748791, ECO:0000269|PubMed:26876602,
CC ECO:0000269|PubMed:29186683}.
CC -!- INTERACTION:
CC Q99873; Q9Y3Y2: CHTOP; NbExp=2; IntAct=EBI-78738, EBI-347794;
CC Q99873; Q5TAQ9: DCAF8; NbExp=2; IntAct=EBI-78738, EBI-740686;
CC Q99873; Q08211: DHX9; NbExp=2; IntAct=EBI-78738, EBI-352022;
CC Q99873; Q01844: EWSR1; NbExp=2; IntAct=EBI-78738, EBI-739737;
CC Q99873; Q8IZU1: FAM9A; NbExp=2; IntAct=EBI-78738, EBI-8468186;
CC Q99873; P35637: FUS; NbExp=5; IntAct=EBI-78738, EBI-400434;
CC Q99873; P62805: H4C9; NbExp=2; IntAct=EBI-78738, EBI-302023;
CC Q99873; Q5JVS0: HABP4; NbExp=2; IntAct=EBI-78738, EBI-523625;
CC Q99873; P61978: HNRNPK; NbExp=3; IntAct=EBI-78738, EBI-304185;
CC Q99873; O43390: HNRNPR; NbExp=5; IntAct=EBI-78738, EBI-713419;
CC Q99873; Q12906: ILF3; NbExp=2; IntAct=EBI-78738, EBI-78756;
CC Q99873; P22736: NR4A1; NbExp=6; IntAct=EBI-78738, EBI-721550;
CC Q99873; P48552: NRIP1; NbExp=4; IntAct=EBI-78738, EBI-746484;
CC Q99873; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-78738, EBI-741158;
CC Q99873; Q8IZS5: OFCC1; NbExp=2; IntAct=EBI-78738, EBI-8477661;
CC Q99873; Q99873: PRMT1; NbExp=4; IntAct=EBI-78738, EBI-78738;
CC Q99873; Q9NR22: PRMT8; NbExp=3; IntAct=EBI-78738, EBI-745545;
CC Q99873; Q9NR22-2: PRMT8; NbExp=5; IntAct=EBI-78738, EBI-10186886;
CC Q99873; Q15772: SPEG; NbExp=3; IntAct=EBI-78738, EBI-1384196;
CC Q99873; Q96BD6: SPSB1; NbExp=2; IntAct=EBI-78738, EBI-2659201;
CC Q99873; Q99619: SPSB2; NbExp=2; IntAct=EBI-78738, EBI-2323209;
CC Q99873; O60506: SYNCRIP; NbExp=2; IntAct=EBI-78738, EBI-1024357;
CC Q99873; P40337: VHL; NbExp=2; IntAct=EBI-78738, EBI-301246;
CC Q99873; PRO_0000038596 [P04591]: gag; Xeno; NbExp=2; IntAct=EBI-78738, EBI-6179727;
CC Q99873; P0DTC9: N; Xeno; NbExp=3; IntAct=EBI-78738, EBI-25475856;
CC Q99873-2; Q01658: DR1; NbExp=3; IntAct=EBI-16399024, EBI-750300;
CC Q99873-3; Q16543: CDC37; NbExp=3; IntAct=EBI-17165527, EBI-295634;
CC Q99873-3; P35637: FUS; NbExp=3; IntAct=EBI-17165527, EBI-400434;
CC Q99873-3; Q99873-3: PRMT1; NbExp=3; IntAct=EBI-17165527, EBI-17165527;
CC Q99873-3; Q9NR22: PRMT8; NbExp=10; IntAct=EBI-17165527, EBI-745545;
CC Q99873-3; Q15772-4: SPEG; NbExp=3; IntAct=EBI-17165527, EBI-12175897;
CC Q99873-3; O60506-4: SYNCRIP; NbExp=4; IntAct=EBI-17165527, EBI-11123832;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10749851,
CC ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:16879614}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm
CC {ECO:0000269|PubMed:26876602}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JIF0}. Note=Mostly found in the cytoplasm.
CC Colocalizes with CHTOP within the nucleus. Low levels detected also in
CC the chromatin fraction (By similarity). {ECO:0000250|UniProtKB:Q9JIF0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=V2;
CC IsoId=Q99873-1; Sequence=Displayed;
CC Name=2; Synonyms=V3;
CC IsoId=Q99873-2; Sequence=VSP_005208;
CC Name=3; Synonyms=V1;
CC IsoId=Q99873-3; Sequence=VSP_005209;
CC Name=4;
CC IsoId=Q99873-5; Sequence=VSP_059419, VSP_059420;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:11097842). Expressed
CC strongly in colorectal cancer cells (at protein level)
CC (PubMed:28040436). Expressed strongly in colorectal cancer tissues
CC compared to wild-type colon samples (at protein level)
CC (PubMed:28040436). Expressed strongly in colorectal cancer tissues
CC compared to wild-type colon samples (PubMed:28040436).
CC {ECO:0000269|PubMed:11097842, ECO:0000269|PubMed:28040436}.
CC -!- PTM: Polyubiquitinated at Lys-145 by the SCF(FBXL17) complex, leading
CC to its subsequent degradation (By similarity). Ubiquitination is
CC regulated by acetylation at Lys-228 and Lys-233 (By similarity).
CC Polyubiquitinated by E3 ubiquitin-protein ligase TRIM48, leading to
CC suppression of MAP3K5/ASK1 methylation and subsequent MAP3K5 activation
CC (PubMed:29186683). {ECO:0000250|UniProtKB:Q9JIF0,
CC ECO:0000269|PubMed:29186683}.
CC -!- PTM: Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the
CC SCF(FBXL17) complex. Acetylated at Lys-233 by p300/EP300. Deacetylated
CC at Lys-228 and Lys-233 by SIRT1. {ECO:0000250|UniProtKB:Q9JIF0}.
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 -!- CAUTION: A paper showing that PRMT1-mediated arginine methylation of
CC PIAS1 regulates STAT1 signaling has been retracted, because some of the
CC data was found to be deliberately falsified.
CC {ECO:0000305|PubMed:19136629, ECO:0000305|PubMed:21724836}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF62894.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF62895.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI09283.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI09284.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA11029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA71764.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA71765.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y10805; CAA71763.1; -; mRNA.
DR EMBL; Y10806; CAA71764.1; ALT_INIT; mRNA.
DR EMBL; Y10807; CAA71765.1; ALT_INIT; mRNA.
DR EMBL; D66904; BAA11029.1; ALT_INIT; mRNA.
DR EMBL; AF222689; AAF62893.1; -; Genomic_DNA.
DR EMBL; AF222689; AAF62894.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF222689; AAF62895.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK304660; BAG65435.1; -; mRNA.
DR EMBL; CR407608; CAG28536.1; -; mRNA.
DR EMBL; AC011495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52521.1; -; Genomic_DNA.
DR EMBL; CH471177; EAW52519.1; -; Genomic_DNA.
DR EMBL; BC019268; AAH19268.2; -; mRNA.
DR EMBL; BC109282; AAI09283.2; ALT_INIT; mRNA.
DR EMBL; BC109283; AAI09284.2; ALT_INIT; mRNA.
DR CCDS; CCDS42592.1; -. [Q99873-3]
DR CCDS; CCDS46145.1; -. [Q99873-1]
DR CCDS; CCDS74425.1; -. [Q99873-5]
DR RefSeq; NP_001193971.1; NM_001207042.2. [Q99873-5]
DR RefSeq; NP_001527.3; NM_001536.5. [Q99873-1]
DR RefSeq; NP_938074.2; NM_198318.4. [Q99873-3]
DR RefSeq; XP_016882223.1; XM_017026734.1. [Q99873-2]
DR RefSeq; XP_016882224.1; XM_017026735.1. [Q99873-2]
DR PDB; 6NT2; X-ray; 2.48 A; A/B/C/D=1-371.
DR PDBsum; 6NT2; -.
DR AlphaFoldDB; Q99873; -.
DR SMR; Q99873; -.
DR BioGRID; 109512; 333.
DR CORUM; Q99873; -.
DR DIP; DIP-30878N; -.
DR IntAct; Q99873; 131.
DR MINT; Q99873; -.
DR STRING; 9606.ENSP00000406162; -.
DR BindingDB; Q99873; -.
DR ChEMBL; CHEMBL5524; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR DrugCentral; Q99873; -.
DR GuidetoPHARMACOLOGY; 1252; -.
DR GlyGen; Q99873; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99873; -.
DR PhosphoSitePlus; Q99873; -.
DR SwissPalm; Q99873; -.
DR BioMuta; PRMT1; -.
DR DMDM; 161789011; -.
DR EPD; Q99873; -.
DR jPOST; Q99873; -.
DR MassIVE; Q99873; -.
DR MaxQB; Q99873; -.
DR PaxDb; Q99873; -.
DR PeptideAtlas; Q99873; -.
DR PRIDE; Q99873; -.
DR ProteomicsDB; 33891; -.
DR ProteomicsDB; 44996; -.
DR ProteomicsDB; 78511; -. [Q99873-1]
DR ProteomicsDB; 78512; -. [Q99873-2]
DR ProteomicsDB; 78513; -. [Q99873-3]
DR Antibodypedia; 18668; 552 antibodies from 40 providers.
DR DNASU; 3276; -.
DR Ensembl; ENST00000391851.8; ENSP00000375724.4; ENSG00000126457.22. [Q99873-3]
DR Ensembl; ENST00000454376.7; ENSP00000406162.2; ENSG00000126457.22. [Q99873-1]
DR Ensembl; ENST00000610806.4; ENSP00000484505.1; ENSG00000126457.22. [Q99873-5]
DR GeneID; 3276; -.
DR KEGG; hsa:3276; -.
DR MANE-Select; ENST00000454376.7; ENSP00000406162.2; NM_001536.6; NP_001527.3.
DR UCSC; uc002ppe.4; human. [Q99873-1]
DR UCSC; uc010enf.3; human.
DR CTD; 3276; -.
DR DisGeNET; 3276; -.
DR GeneCards; PRMT1; -.
DR HGNC; HGNC:5187; PRMT1.
DR HPA; ENSG00000126457; Low tissue specificity.
DR MIM; 602950; gene.
DR neXtProt; NX_Q99873; -.
DR OpenTargets; ENSG00000126457; -.
DR PharmGKB; PA29461; -.
DR VEuPathDB; HostDB:ENSG00000126457; -.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000154700; -.
DR InParanoid; Q99873; -.
DR OMA; TTDRMEV; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q99873; -.
DR TreeFam; TF300608; -.
DR BioCyc; MetaCyc:HS05019-MON; -.
DR BRENDA; 2.1.1.319; 2681.
DR PathwayCommons; Q99873; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR SABIO-RK; Q99873; -.
DR SignaLink; Q99873; -.
DR SIGNOR; Q99873; -.
DR BioGRID-ORCS; 3276; 777 hits in 1100 CRISPR screens.
DR ChiTaRS; PRMT1; human.
DR GeneWiki; PRMT1; -.
DR GenomeRNAi; 3276; -.
DR Pharos; Q99873; Tchem.
DR PRO; PR:Q99873; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q99873; protein.
DR Bgee; ENSG00000126457; Expressed in embryo and 193 other tissues.
DR ExpressionAtlas; Q99873; baseline and differential.
DR Genevisible; Q99873; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0034709; C:methylosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; TAS:ProtInc.
DR GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IPI:BHF-UCL.
DR GO; GO:0008170; F:N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA: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; IDA:UniProtKB.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0043985; P:histone H4-R3 methylation; IDA:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IDA:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; ISS:BHF-UCL.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:BHF-UCL.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IMP:UniProtKB.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR Pfam; PF13649; Methyltransf_25; 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; Cytoplasm;
KW Isopeptide bond; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT CHAIN 1..371
FT /note="Protein arginine N-methyltransferase 1"
FT /id="PRO_0000212321"
FT DOMAIN 50..361
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 162
FT /evidence="ECO:0000250"
FT ACT_SITE 171
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 134
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9JIF0"
FT VAR_SEQ 1..29
FT /note="MAAAEAANCIMENFVATLANGMSLQPPLE -> MVGVA (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_005208"
FT VAR_SEQ 11..30
FT /note="MENFVATLANGMSLQPPLEE -> ME (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_005209"
FT VAR_SEQ 13..30
FT /note="Missing (in isoform 4)"
FT /id="VSP_059419"
FT VAR_SEQ 186..253
FT /note="Missing (in isoform 4)"
FT /id="VSP_059420"
FT VARIANT 88
FT /note="K -> M (in dbSNP:rs1804486)"
FT /id="VAR_037501"
FT VARIANT 168
FT /note="L -> F (in dbSNP:rs11673683)"
FT /id="VAR_037502"
FT MUTAGEN 92
FT /note="V->A: Loss of FOXO1 methylation, its nuclear
FT retention, and transcriptional activity."
FT /evidence="ECO:0000269|PubMed:18951090"
FT MUTAGEN 93
FT /note="L->A: Loss of FOXO1 methylation, its nuclear
FT retention, and transcriptional activity."
FT /evidence="ECO:0000269|PubMed:18951090"
FT MUTAGEN 94
FT /note="D->A: Loss of FOXO1 methylation, its nuclear
FT retention, and transcriptional activity."
FT /evidence="ECO:0000269|PubMed:18951090"
FT MUTAGEN 280
FT /note="Y->A: No effect on S-adenosyl-L-methionine binding
FT but reduced EWS protein methylation; when associated with
FT A-322 and A-359. No effect on homodimerization but loss of
FT homooligomerization; when associated with A-322 and A-359."
FT /evidence="ECO:0000269|PubMed:26876602"
FT MUTAGEN 322
FT /note="Y->A: No effect on S-adenosyl-L-methionine binding
FT but reduced EWS protein methylation; when associated with
FT A-280 and A-359. No effect on homodimerization but loss of
FT homooligomerization; when associated with A-280 and A-359."
FT /evidence="ECO:0000269|PubMed:26876602"
FT MUTAGEN 359
FT /note="L->A: No effect on S-adenosyl-L-methionine binding
FT but reduced EWS protein methylation; when associated with
FT A-280 and A-322. No effect on homodimerization but loss of
FT homooligomerization; when associated with A-280 and A-322."
FT /evidence="ECO:0000269|PubMed:26876602"
FT CONFLICT 118
FT /note="E -> V (in Ref. 1; CAA71763/CAA71764/CAA71765 and 2;
FT BAA11029)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..185
FT /note="DIIISEWMGYCLFYESMLNTVLYARDKWL -> ASSSASGWATASSTSPCST
FT PCSMPGTSV (in Ref. 2; BAA11029)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="K -> E (in Ref. 4; BAG65435)"
FT /evidence="ECO:0000305"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:6NT2"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6NT2"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:6NT2"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:6NT2"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 277..291
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 314..325
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 330..339
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 346..356
FT /evidence="ECO:0007829|PDB:6NT2"
FT STRAND 361..370
FT /evidence="ECO:0007829|PDB:6NT2"
SQ SEQUENCE 371 AA; 42462 MW; 544349801B0E1396 CRC64;
MAAAEAANCI MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK DYYFDSYAHF
GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG ARKVIGIECS
SISDYAVKIV KANKLDHVVT IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVLYA
RDKWLAPDGL IFPDRATLYV TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV
DPKQLVTNAC LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG
FSTSPESPYT HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT IDLDFKGQLC
ELSCSTDYRM R
