NSUN2_HUMAN
ID NSUN2_HUMAN Reviewed; 767 AA.
AC Q08J23; A8K529; B2RNR4; B3KP09; B4DQW2; G3V1R4; Q9BVN4; Q9H858; Q9NXD9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=RNA cytosine C(5)-methyltransferase NSUN2 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:17071714, ECO:0000269|PubMed:22395603, ECO:0000269|PubMed:31186410, ECO:0000269|PubMed:31276587, ECO:0000269|PubMed:31358969};
DE AltName: Full=Myc-induced SUN domain-containing protein {ECO:0000303|PubMed:19596847};
DE Short=Misu {ECO:0000303|PubMed:19596847};
DE AltName: Full=NOL1/NOP2/Sun domain family member 2 {ECO:0000303|PubMed:17215513};
DE AltName: Full=Substrate of AIM1/Aurora kinase B {ECO:0000303|PubMed:17215513};
DE AltName: Full=mRNA cytosine C(5)-methyltransferase;
DE EC=2.1.1.- {ECO:0000269|PubMed:22395603, ECO:0000269|PubMed:28418038, ECO:0000269|PubMed:31358969, ECO:0000269|PubMed:34556860};
DE AltName: Full=tRNA cytosine C(5)-methyltransferase;
DE EC=2.1.1.- {ECO:0000269|PubMed:31276587};
DE EC=2.1.1.203 {ECO:0000269|PubMed:17071714};
DE AltName: Full=tRNA methyltransferase 4 homolog {ECO:0000303|PubMed:17071714};
DE Short=hTrm4 {ECO:0000303|PubMed:17071714};
GN Name=NSUN2 {ECO:0000303|PubMed:17215513, ECO:0000312|HGNC:HGNC:25994};
GN Synonyms=SAKI {ECO:0000303|PubMed:17215513},
GN TRM4 {ECO:0000303|PubMed:17071714};
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), PARTIAL PROTEIN SEQUENCE,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-139, INTERACTION WITH NPM1 AND
RP NCL, AND MUTAGENESIS OF SER-139.
RX PubMed=17215513; DOI=10.1091/mbc.e06-11-1021;
RA Sakita-Suto S., Kanda A., Suzuki F., Sato S., Takata T., Tatsuka M.;
RT "Aurora-B regulates RNA methyltransferase NSUN2.";
RL Mol. Biol. Cell 18:1107-1117(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Placenta;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=17071714; DOI=10.1093/nar/gkl765;
RA Brzezicha B., Schmidt M., Makalowska I., Jarmolowski A., Pienkowska J.,
RA Szweykowska-Kulinska Z.;
RT "Identification of human tRNA:m5C methyltransferase catalysing intron-
RT dependent m5C formation in the first position of the anticodon of the pre-
RT tRNA Leu (CAA).";
RL Nucleic Acids Res. 34:6034-6043(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-473; SER-743 AND
RP SER-751, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19596847; DOI=10.1083/jcb.200810180;
RA Hussain S., Benavente S.B., Nascimento E., Dragoni I., Kurowski A.,
RA Gillich A., Humphreys P., Frye M.;
RT "The nucleolar RNA methyltransferase Misu (NSun2) is required for mitotic
RT spindle stability.";
RL J. Cell Biol. 186:27-40(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-593 AND SER-743, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP MALONYLATION AT LYS-586.
RX PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-593, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP INVOLVEMENT IN MRT5, AND TISSUE SPECIFICITY.
RX PubMed=22541559; DOI=10.1016/j.ajhg.2012.03.021;
RA Abbasi-Moheb L., Mertel S., Gonsior M., Nouri-Vahid L., Kahrizi K.,
RA Cirak S., Wieczorek D., Motazacker M.M., Esmaeeli-Nieh S., Cremer K.,
RA Weissmann R., Tzschach A., Garshasbi M., Abedini S.S., Najmabadi H.,
RA Ropers H.H., Sigrist S.J., Kuss A.W.;
RT "Mutations in NSUN2 cause autosomal-recessive intellectual disability.";
RL Am. J. Hum. Genet. 90:847-855(2012).
RN [19]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22395603; DOI=10.1038/ncomms1692;
RA Zhang X., Liu Z., Yi J., Tang H., Xing J., Yu M., Tong T., Shang Y.,
RA Gorospe M., Wang W.;
RT "The tRNA methyltransferase NSun2 stabilizes p16INK[4] mRNA by methylating
RT the 3'-untranslated region of p16.";
RL Nat. Commun. 3:712-712(2012).
RN [20]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=22995836; DOI=10.4161/rna.22180;
RA Auxilien S., Guerineau V., Szweykowska-Kulinska Z., Golinelli-Pimpaneau B.;
RT "The human tRNA m (5) C methyltransferase Misu is multisite-specific.";
RL RNA Biol. 9:1331-1338(2012).
RN [21]
RP FUNCTION.
RX PubMed=23871666; DOI=10.1016/j.celrep.2013.06.029;
RA Hussain S., Sajini A.A., Blanco S., Dietmann S., Lombard P., Sugimoto Y.,
RA Paramor M., Gleeson J.G., Odom D.T., Ule J., Frye M.;
RT "NSun2-mediated cytosine-5 methylation of vault noncoding RNA determines
RT its processing into regulatory small RNAs.";
RL Cell Rep. 4:255-261(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-593; SER-743 AND
RP SER-751, AND 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-743 AND SER-751, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-640, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [25]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-271 AND
RP CYS-321.
RX PubMed=28418038; DOI=10.1038/cr.2017.55;
RA Yang X., Yang Y., Sun B.F., Chen Y.S., Xu J.W., Lai W.Y., Li A., Wang X.,
RA Bhattarai D.P., Xiao W., Sun H.Y., Zhu Q., Ma H.L., Adhikari S., Sun M.,
RA Hao Y.J., Zhang B., Huang C.M., Huang N., Jiang G.B., Zhao Y.L., Wang H.L.,
RA Sun Y.P., Yang Y.G.;
RT "5-methylcytosine promotes mRNA export - NSUN2 as the methyltransferase and
RT ALYREF as an m5C reader.";
RL Cell Res. 27:606-625(2017).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-464; LYS-470; LYS-511;
RP LYS-516; LYS-586; LYS-654 AND LYS-660, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-271 AND
RP CYS-321.
RX PubMed=31358969; DOI=10.1038/s41556-019-0361-y;
RA Chen X., Li A., Sun B.F., Yang Y., Han Y.N., Yuan X., Chen R.X., Wei W.S.,
RA Liu Y., Gao C.C., Chen Y.S., Zhang M., Ma X.D., Liu Z.W., Luo J.H., Lyu C.,
RA Wang H.L., Ma J., Zhao Y.L., Zhou F.J., Huang Y., Xie D., Yang Y.G.;
RT "5-methylcytosine promotes pathogenesis of bladder cancer through
RT stabilizing mRNAs.";
RL Nat. Cell Biol. 21:978-990(2019).
RN [28]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-190.
RX PubMed=31186410; DOI=10.1038/s41467-019-10020-7;
RA Sajini A.A., Choudhury N.R., Wagner R.E., Borneloev S., Selmi T.,
RA Spanos C., Dietmann S., Rappsilber J., Michlewski G., Frye M.;
RT "Loss of 5-methylcytosine alters the biogenesis of vault-derived small RNAs
RT to coordinate epidermal differentiation.";
RL Nat. Commun. 10:2550-2550(2019).
RN [29]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=31276587; DOI=10.1093/nar/gkz559;
RA Van Haute L., Lee S.Y., McCann B.J., Powell C.A., Bansal D.,
RA Vasiliauskaite L., Garone C., Shin S., Kim J.S., Frye M., Gleeson J.G.,
RA Miska E.A., Rhee H.W., Minczuk M.;
RT "NSUN2 introduces 5-methylcytosines in mammalian mitochondrial tRNAs.";
RL Nucleic Acids Res. 47:8720-8733(2019).
RN [30]
RP SUBCELLULAR LOCATION.
RX PubMed=31287866; DOI=10.1093/nar/gkz575;
RA Shinoda S., Kitagawa S., Nakagawa S., Wei F.Y., Tomizawa K., Araki K.,
RA Araki M., Suzuki T., Suzuki T.;
RT "Mammalian NSUN2 introduces 5-methylcytidines into mitochondrial tRNAs.";
RL Nucleic Acids Res. 47:8734-8745(2019).
RN [31]
RP FUNCTION, AND MUTAGENESIS OF LYS-190.
RX PubMed=31199786; DOI=10.1371/journal.pbio.3000297;
RA Gkatza N.A., Castro C., Harvey R.F., Heiss M., Popis M.C., Blanco S.,
RA Borneloev S., Sajini A.A., Gleeson J.G., Griffin J.L., West J.A.,
RA Kellner S., Willis A.E., Dietmann S., Frye M.;
RT "Cytosine-5 RNA methylation links protein synthesis to cell metabolism.";
RL PLoS Biol. 17:E3000297-E3000297(2019).
RN [32]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=34556860; DOI=10.1038/s41589-021-00874-8;
RA Dai W., Li A., Yu N.J., Nguyen T., Leach R.W., Wuehr M., Kleiner R.E.;
RT "Activity-based RNA-modifying enzyme probing reveals DUS3L-mediated
RT dihydrouridylation.";
RL Nat. Chem. Biol. 17:1178-1187(2021).
RN [33]
RP VARIANT MRT5 ARG-679, AND CHARACTERIZATION OF VARIANT MRT5 ARG-679.
RX PubMed=22541562; DOI=10.1016/j.ajhg.2012.03.023;
RA Khan M.A., Rafiq M.A., Noor A., Hussain S., Flores J.V., Rupp V.,
RA Vincent A.K., Malli R., Ali G., Khan F.S., Ishak G.E., Doherty D.,
RA Weksberg R., Ayub M., Windpassinger C., Ibrahim S., Frye M., Ansar M.,
RA Vincent J.B.;
RT "Mutation in NSUN2, which encodes an RNA methyltransferase, causes
RT autosomal-recessive intellectual disability.";
RL Am. J. Hum. Genet. 90:856-863(2012).
CC -!- FUNCTION: RNA cytosine C(5)-methyltransferase that methylates cytosine
CC to 5-methylcytosine (m5C) in various RNAs, such as tRNAs, mRNAs and
CC some long non-coding RNAs (lncRNAs) (PubMed:17071714, PubMed:22995836,
CC PubMed:31358969, PubMed:31199786). Involved in various processes, such
CC as epidermal stem cell differentiation, testis differentiation and
CC maternal to zygotic transition during early development: acts by
CC increasing protein synthesis; cytosine C(5)-methylation promoting tRNA
CC stability and preventing mRNA decay (PubMed:31199786). Methylates
CC cytosine to 5-methylcytosine (m5C) at positions 34 and 48 of intron-
CC containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of
CC tRNA(Gly)(GCC) precursors (PubMed:17071714, PubMed:22995836,
CC PubMed:31199786). tRNA methylation is required generation of RNA
CC fragments derived from tRNAs (tRFs) (PubMed:31199786). Also mediates
CC C(5)-methylation of mitochondrial tRNAs (PubMed:31276587). Catalyzes
CC cytosine C(5)-methylation of mRNAs, leading to stabilize them and
CC prevent mRNA decay: mRNA stabilization involves YBX1 that specifically
CC recognizes and binds m5C-modified transcripts (PubMed:22395603,
CC PubMed:31358969, PubMed:34556860). Cytosine C(5)-methylation of mRNAs
CC also regulates mRNA export: methylated transcripts are specifically
CC recognized by THOC4/ALYREF, which mediates mRNA nucleo-cytoplasmic
CC shuttling (PubMed:28418038). Also mediates cytosine C(5)-methylation of
CC non-coding RNAs, such as vault RNAs (vtRNAs), promoting their
CC processing into regulatory small RNAs (PubMed:23871666). Cytosine C(5)-
CC methylation of vtRNA VTRNA1.1 promotes its processing into small-vault
CC RNA4 (svRNA4) and regulates epidermal differentiation
CC (PubMed:31186410). May act downstream of Myc to regulate epidermal cell
CC growth and proliferation (By similarity). Required for proper spindle
CC assembly and chromosome segregation, independently of its
CC methyltransferase activity (PubMed:19596847).
CC {ECO:0000250|UniProtKB:Q1HFZ0, ECO:0000269|PubMed:17071714,
CC ECO:0000269|PubMed:19596847, ECO:0000269|PubMed:22395603,
CC ECO:0000269|PubMed:22995836, ECO:0000269|PubMed:23871666,
CC ECO:0000269|PubMed:28418038, ECO:0000269|PubMed:31186410,
CC ECO:0000269|PubMed:31199786, ECO:0000269|PubMed:31276587,
CC ECO:0000269|PubMed:31358969, ECO:0000269|PubMed:34556860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(48) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(48) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42948, Rhea:RHEA-COMP:10293, Rhea:RHEA-COMP:10297,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:31276587};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42949;
CC Evidence={ECO:0000269|PubMed:31276587};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(49) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(49) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42952, Rhea:RHEA-COMP:10294, Rhea:RHEA-COMP:10385,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:31276587};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42953;
CC Evidence={ECO:0000269|PubMed:31276587};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(50) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(50) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61488, Rhea:RHEA-COMP:15838, Rhea:RHEA-COMP:15839,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:31276587};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61489;
CC Evidence={ECO:0000269|PubMed:31276587};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(34) in tRNA precursor + S-adenosyl-L-methionine = 5-
CC methylcytidine(34) in tRNA precursor + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:42940, Rhea:RHEA-COMP:10291, Rhea:RHEA-
CC COMP:10295, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.203;
CC Evidence={ECO:0000269|PubMed:17071714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42941;
CC Evidence={ECO:0000269|PubMed:17071714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in mRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61464, Rhea:RHEA-COMP:15145, Rhea:RHEA-COMP:15826,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:22395603, ECO:0000269|PubMed:28418038,
CC ECO:0000269|PubMed:31358969, ECO:0000269|PubMed:34556860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61465;
CC Evidence={ECO:0000269|PubMed:22395603, ECO:0000269|PubMed:28418038,
CC ECO:0000269|PubMed:31358969};
CC -!- ACTIVITY REGULATION: Inhibited by magnesium ions.
CC {ECO:0000269|PubMed:22995836}.
CC -!- SUBUNIT: Interacts with NPM1 and NCL during interphase; interaction is
CC disrupted following phosphorylation at Ser-139.
CC {ECO:0000269|PubMed:17215513}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17071714,
CC ECO:0000269|PubMed:17215513, ECO:0000269|PubMed:31276587}. Cytoplasm
CC {ECO:0000269|PubMed:17071714, ECO:0000269|PubMed:31276587}.
CC Mitochondrion {ECO:0000269|PubMed:31276587,
CC ECO:0000269|PubMed:31287866}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:19596847}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:Q1HFZ0}. Note=Concentrated in the nucleolus
CC during interphase and translocates to the spindle during mitosis as an
CC RNA-protein complex that includes 18S ribosomal RNA (PubMed:19596847).
CC In testis, localizes to the chromatoid body (By similarity).
CC {ECO:0000250|UniProtKB:Q1HFZ0, ECO:0000269|PubMed:19596847}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q08J23-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08J23-2; Sequence=VSP_042621;
CC Name=3;
CC IsoId=Q08J23-3; Sequence=VSP_053598;
CC -!- TISSUE SPECIFICITY: Expressed in adult and fetal brain and in
CC lymphoblastoid cells. {ECO:0000269|PubMed:22541559}.
CC -!- PTM: Phosphorylated at Ser-139 by AURKB during mitosis, leading to
CC abolish methyltransferase activity and the interaction with NPM1.
CC {ECO:0000269|PubMed:17215513}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 5
CC (MRT5) [MIM:611091]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:22541559, ECO:0000269|PubMed:22541562}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. TRM4 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU01023}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91075.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14762.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB255451; BAF34150.1; -; mRNA.
DR EMBL; AK000310; BAA91075.1; ALT_INIT; mRNA.
DR EMBL; AK023994; BAB14762.1; ALT_INIT; mRNA.
DR EMBL; AK055456; BAG51521.1; -; mRNA.
DR EMBL; AK291144; BAF83833.1; -; mRNA.
DR EMBL; AK298980; BAG61074.1; -; mRNA.
DR EMBL; AC010366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471102; EAX08105.1; -; Genomic_DNA.
DR EMBL; CH471102; EAX08106.1; -; Genomic_DNA.
DR EMBL; BC001041; AAH01041.3; -; mRNA.
DR EMBL; BC137083; AAI37084.1; -; mRNA.
DR CCDS; CCDS3869.1; -. [Q08J23-1]
DR CCDS; CCDS54832.1; -. [Q08J23-2]
DR RefSeq; NP_001180384.1; NM_001193455.1. [Q08J23-2]
DR RefSeq; NP_060225.4; NM_017755.5. [Q08J23-1]
DR AlphaFoldDB; Q08J23; -.
DR SMR; Q08J23; -.
DR BioGRID; 120236; 178.
DR DIP; DIP-52456N; -.
DR IntAct; Q08J23; 62.
DR MINT; Q08J23; -.
DR STRING; 9606.ENSP00000264670; -.
DR ChEMBL; CHEMBL4739683; -.
DR GlyConnect; 1859; 1 N-Linked glycan (1 site).
DR GlyGen; Q08J23; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q08J23; -.
DR MetOSite; Q08J23; -.
DR PhosphoSitePlus; Q08J23; -.
DR SwissPalm; Q08J23; -.
DR BioMuta; NSUN2; -.
DR DMDM; 148887180; -.
DR CPTAC; CPTAC-984; -.
DR EPD; Q08J23; -.
DR jPOST; Q08J23; -.
DR MassIVE; Q08J23; -.
DR MaxQB; Q08J23; -.
DR PaxDb; Q08J23; -.
DR PeptideAtlas; Q08J23; -.
DR PRIDE; Q08J23; -.
DR ProteomicsDB; 32415; -.
DR ProteomicsDB; 58697; -. [Q08J23-1]
DR ProteomicsDB; 58698; -. [Q08J23-2]
DR Antibodypedia; 22399; 188 antibodies from 27 providers.
DR DNASU; 54888; -.
DR Ensembl; ENST00000264670.11; ENSP00000264670.6; ENSG00000037474.15. [Q08J23-1]
DR Ensembl; ENST00000506139.5; ENSP00000420957.1; ENSG00000037474.15. [Q08J23-2]
DR GeneID; 54888; -.
DR KEGG; hsa:54888; -.
DR MANE-Select; ENST00000264670.11; ENSP00000264670.6; NM_017755.6; NP_060225.4.
DR UCSC; uc003jdu.4; human. [Q08J23-1]
DR CTD; 54888; -.
DR DisGeNET; 54888; -.
DR GeneCards; NSUN2; -.
DR HGNC; HGNC:25994; NSUN2.
DR HPA; ENSG00000037474; Low tissue specificity.
DR MalaCards; NSUN2; -.
DR MIM; 610916; gene.
DR MIM; 611091; phenotype.
DR neXtProt; NX_Q08J23; -.
DR OpenTargets; ENSG00000037474; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR Orphanet; 235; Dubowitz syndrome.
DR PharmGKB; PA134953940; -.
DR VEuPathDB; HostDB:ENSG00000037474; -.
DR eggNOG; KOG2198; Eukaryota.
DR GeneTree; ENSGT00940000153665; -.
DR HOGENOM; CLU_005316_4_3_1; -.
DR InParanoid; Q08J23; -.
DR OMA; QLFTEYV; -.
DR OrthoDB; 911098at2759; -.
DR PhylomeDB; Q08J23; -.
DR TreeFam; TF300702; -.
DR BioCyc; MetaCyc:HS12087-MON; -.
DR BRENDA; 2.1.1.202; 2681.
DR BRENDA; 2.1.1.203; 2681.
DR PathwayCommons; Q08J23; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q08J23; -.
DR SIGNOR; Q08J23; -.
DR BioGRID-ORCS; 54888; 19 hits in 1089 CRISPR screens.
DR ChiTaRS; NSUN2; human.
DR GeneWiki; NSUN2; -.
DR GenomeRNAi; 54888; -.
DR Pharos; Q08J23; Tbio.
DR PRO; PR:Q08J23; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q08J23; protein.
DR Bgee; ENSG00000037474; Expressed in upper arm skin and 181 other tissues.
DR ExpressionAtlas; Q08J23; baseline and differential.
DR Genevisible; Q08J23; HS.
DR GO; GO:0033391; C:chromatoid body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0062152; F:mRNA (cytidine-5-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048820; P:hair follicle maturation; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0033313; P:meiotic cell cycle checkpoint signaling; IEA:Ensembl.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:2000736; P:regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; TAS:Reactome.
DR GO; GO:0036416; P:tRNA stabilization; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; PTHR22808; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Differentiation; Direct protein sequencing; Disease variant;
KW Intellectual disability; Isopeptide bond; Methyltransferase; Mitochondrion;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Secreted; Spermatogenesis; Transferase;
KW tRNA processing; tRNA-binding; Ubl conjugation.
FT CHAIN 1..767
FT /note="RNA cytosine C(5)-methyltransferase NSUN2"
FT /id="PRO_0000289223"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023,
FT ECO:0000305|PubMed:28418038, ECO:0000305|PubMed:31358969"
FT BINDING 184..190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT MOD_RES 139
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:17215513"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 586
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q1HFZ0"
FT MOD_RES 586
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 718
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q1HFZ0"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1HFZ0"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 464
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 511
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 516
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 586
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 640
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..236
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053598"
FT VAR_SEQ 85..120
FT /note="SHAKEILHCLKNKYFKELEDLEVDGQKVEVPQPLSW -> R (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042621"
FT VARIANT 627
FT /note="V -> I (in dbSNP:rs2303708)"
FT /id="VAR_032604"
FT VARIANT 679
FT /note="G -> R (in MRT5; impairs proper intracellular
FT localization; dbSNP:rs587776908)"
FT /evidence="ECO:0000269|PubMed:22541562"
FT /id="VAR_068530"
FT MUTAGEN 139
FT /note="S->A: Induces a constitutive association with NPM1."
FT /evidence="ECO:0000269|PubMed:17215513"
FT MUTAGEN 139
FT /note="S->E: Mimicks constitutive phosphorylation and
FT abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:17215513"
FT MUTAGEN 190
FT /note="K->M: Loss of RNA methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31186410,
FT ECO:0000269|PubMed:31199786"
FT MUTAGEN 271
FT /note="C->A: Abolished mRNA methyltransferase activity;
FT when associated with A-321."
FT /evidence="ECO:0000269|PubMed:28418038,
FT ECO:0000269|PubMed:31358969"
FT MUTAGEN 321
FT /note="C->A: Abolished mRNA methyltransferase activity;
FT when associated with A-271."
FT /evidence="ECO:0000269|PubMed:28418038,
FT ECO:0000269|PubMed:31358969"
FT CONFLICT 316
FT /note="M -> V (in Ref. 2; BAA91075)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="E -> G (in Ref. 2; BAF83833)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="I -> V (in Ref. 2; BAG51521)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="G -> D (in Ref. 2; BAB14762)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="Q -> R (in Ref. 1; BAF34150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 767 AA; 86471 MW; FE4B34309978A8D2 CRC64;
MGRRSRGRRL QQQQRPEDAE DGAEGGGKRG EAGWEGGYPE IVKENKLFEH YYQELKIVPE
GEWGQFMDAL REPLPATLRI TGYKSHAKEI LHCLKNKYFK ELEDLEVDGQ KVEVPQPLSW
YPEELAWHTN LSRKILRKSP HLEKFHQFLV SETESGNISR QEAVSMIPPL LLNVRPHHKI
LDMCAAPGSK TTQLIEMLHA DMNVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN
HDASSIPRLQ IDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL
RIATRGAEQL AEGGRMVYST CSLNPIEDEA VIASLLEKSE GALELADVSN ELPGLKWMPG
ITQWKVMTKD GQWFTDWDAV PHSRHTQIRP TMFPPKDPEK LQAMHLERCL RILPHHQNTG
GFFVAVLVKK SSMPWNKRQP KLQGKSAETR ESTQLSPADL TEGKPTDPSK LESPSFTGTG
DTEIAHATED LENNGSKKDG VCGPPPSKKM KLFGFKEDPF VFIPEDDPLF PPIEKFYALD
PSFPRMNLLT RTTEGKKRQL YMVSKELRNV LLNNSEKMKV INTGIKVWCR NNSGEEFDCA
FRLAQEGIYT LYPFINSRII TVSMEDVKIL LTQENPFFRK LSSETYSQAK DLAKGSIVLK
YEPDSANPDA LQCPIVLCGW RGKASIRTFV PKNERLHYLR MMGLEVLGEK KKEGVILTNE
SAASTGQPDN DVTEGQRAGE PNSPDAEEAN SPDVTAGCDP AGVHPPR
