OGT1_HUMAN
ID OGT1_HUMAN Reviewed; 1046 AA.
AC O15294; Q7Z3K0; Q8WWM8; Q96CC1; Q9UG57;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;
DE EC=2.4.1.255 {ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:30699359, ECO:0000305|PubMed:26678539};
DE AltName: Full=O-GlcNAc transferase subunit p110;
DE AltName: Full=O-linked N-acetylglucosamine transferase 110 kDa subunit;
DE Short=OGT;
GN Name=OGT;
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 2), PROTEIN SEQUENCE OF 227-236 AND
RP 955-971, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9083068; DOI=10.1074/jbc.272.14.9316;
RA Lubas W.A., Frank D.W., Krause M., Hanover J.A.;
RT "O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein
RT containing tetratricopeptide repeats.";
RL J. Biol. Chem. 272:9316-9324(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=11773972; DOI=10.1007/s00335-001-2108-9;
RA Nolte D., Muller U.;
RT "Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice
RT variants, fine mapping in Xq13.1.";
RL Mamm. Genome 13:62-64(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Endometrium, Fetal brain, and Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Colon, and Pancreas;
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 [5]
RP PROTEIN SEQUENCE OF 2-17; 31-42; 161-168; 244-250; 339-348; 734-752;
RP 868-877 AND 1002-1010, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Dhillon A.S., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [6]
RP FUNCTION, AND INTERACTION WITH SIN3A.
RX PubMed=12150998; DOI=10.1016/s0092-8674(02)00810-3;
RA Yang X., Zhang F., Kudlow J.E.;
RT "Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A:
RT coupling protein O-GlcNAcylation to transcriptional repression.";
RL Cell 110:69-80(2002).
RN [7]
RP INTERACTION WITH HCFC1.
RX PubMed=12670868; DOI=10.1101/gad.252103;
RA Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
RT "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
RT methyltransferase are tethered together selectively by the cell-
RT proliferation factor HCF-1.";
RL Genes Dev. 17:896-911(2003).
RN [8]
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP FUNCTION, AND ASSOCIATION WITH ALZHEIMER DISEASE.
RX PubMed=19451179; DOI=10.1093/brain/awp099;
RA Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I., Iqbal K.,
RA Gong C.X.;
RT "Reduced O-GlcNAcylation links lower brain glucose metabolism and tau
RT pathology in Alzheimer's disease.";
RL Brain 132:1820-1832(2009).
RN [11]
RP INDUCTION.
RX PubMed=19073609; DOI=10.1074/jbc.m803198200;
RA Taylor R.P., Geisler T.S., Chambers J.H., McClain D.A.;
RT "Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2
RT cells is mediated by decreased hexosamine pathway flux.";
RL J. Biol. Chem. 284:3425-3432(2009).
RN [12]
RP CAUTION.
RX PubMed=19377461; DOI=10.1038/nature07954;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
RT granulopoiesis.";
RL Nature 459:455-459(2009).
RN [13]
RP CAUTION, AND RETRACTION NOTICE OF PUBMED:19377461.
RX PubMed=24336203; DOI=10.1038/nature12896;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "Retraction: GlcNAcylation of a histone methyltransferase in retinoic-acid-
RT induced granulopoiesis.";
RL Nature 505:574-574(2014).
RN [14]
RP FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20018852; DOI=10.1074/jbc.c109.087981;
RA Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
RA Washburn M.P., Conaway J.W., Conaway R.C.;
RT "Subunit composition and substrate specificity of a MOF-containing histone
RT acetyltransferase distinct from the male-specific lethal (MSL) complex.";
RL J. Biol. Chem. 285:4268-4272(2010).
RN [15]
RP FUNCTION, AND POSSIBLE ASSOCIATION WITH DIABETES.
RX PubMed=20018868; DOI=10.1074/jbc.m109.077818;
RA Whelan S.A., Dias W.B., Thiruneelakantapillai L., Lane M.D., Hart G.W.;
RT "Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated
RT insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1
RT adipocytes.";
RL J. Biol. Chem. 285:5204-5211(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX,
RP INTERACTION WITH HCFC1; THAP1 AND THAP3, AND FUNCTION.
RX PubMed=20200153; DOI=10.1074/jbc.m109.072579;
RA Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L.,
RA Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B.,
RA Kristie T.M., Girard J.P.;
RT "The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and
RT O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias.";
RL J. Biol. Chem. 285:13364-13371(2010).
RN [17]
RP FUNCTION (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=20824293; DOI=10.1007/s00726-010-0719-8;
RA Shin S.H., Love D.C., Hanover J.A.;
RT "Elevated O-GlcNAc-dependent signaling through inducible mOGT expression
RT selectively triggers apoptosis.";
RL Amino Acids 40:885-893(2011).
RN [18]
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 [19]
RP FUNCTION, AND INTERACTION WITH H2B.
RX PubMed=22121020; DOI=10.1038/nature10656;
RA Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S.,
RA Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F., Kitagawa H.,
RA Roeder R.G., Brown M., Kato S.;
RT "GlcNAcylation of histone H2B facilitates its monoubiquitination.";
RL Nature 480:557-560(2011).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION, AND
RP INTERACTION WITH HCFC1.
RX PubMed=21285374; DOI=10.1073/pnas.1013822108;
RA Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G.,
RA Vogel J.L., Kristie T.M., Affar E.B.;
RT "Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the
RT host cell factor-1 maturation pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP FUNCTION.
RX PubMed=22923583; DOI=10.1126/science.1222278;
RA Yi W., Clark P.M., Mason D.E., Keenan M.C., Hill C., Goddard W.A. III,
RA Peters E.C., Driggers E.M., Hsieh-Wilson L.C.;
RT "Phosphofructokinase 1 glycosylation regulates cell growth and
RT metabolism.";
RL Science 337:975-980(2012).
RN [23]
RP FUNCTION, AND INTERACTION WITH HCFC1; TET2 AND TET3.
RX PubMed=23353889; DOI=10.1038/emboj.2012.357;
RA Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J., Murphy N.,
RA Dawson M.A., Volkmar M., Putmans P., Calonne E., Shih A.H., Levine R.L.,
RA Bernard O., Mercher T., Solary E., Urh M., Daniels D.L., Fuks F.;
RT "TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and
RT SET1/COMPASS.";
RL EMBO J. 32:645-655(2013).
RN [24]
RP INTERACTION WITH KMT2E.
RX PubMed=23629655; DOI=10.1074/jbc.m112.439729;
RA Zhou P., Wang Z., Yuan X., Zhou C., Liu L., Wan X., Zhang F., Ding X.,
RA Wang C., Xiong S., Wang Z., Yuan J., Li Q., Zhang Y.;
RT "Mixed lineage leukemia 5 (MLL5) protein regulates cell cycle progression
RT and E2F1-responsive gene expression via association with host cell factor-1
RT (HCF-1).";
RL J. Biol. Chem. 288:17532-17543(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [26]
RP FUNCTION, AND INTERACTION WITH TET2 AND TET3.
RX PubMed=23222540; DOI=10.1038/nature11742;
RA Chen Q., Chen Y., Bian C., Fujiki R., Yu X.;
RT "TET2 promotes histone O-GlcNAcylation during gene transcription.";
RL Nature 493:561-564(2013).
RN [27]
RP INTERACTION WITH KIF5B; RHOT1; RHOT2 AND TRAK1.
RX PubMed=24995978; DOI=10.1016/j.cell.2014.06.007;
RA Pekkurnaz G., Trinidad J.C., Wang X., Kong D., Schwarz T.L.;
RT "Glucose regulates mitochondrial motility via Milton modification by O-
RT GlcNAc transferase.";
RL Cell 158:54-68(2014).
RN [28]
RP FUNCTION.
RX PubMed=24474760; DOI=10.1073/pnas.1323226111;
RA Chu C.S., Lo P.W., Yeh Y.H., Hsu P.H., Peng S.H., Teng Y.C., Kang M.L.,
RA Wong C.H., Juan L.J.;
RT "O-GlcNAcylation regulates EZH2 protein stability and function.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:1355-1360(2014).
RN [29]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN A COMPLEX WITH KMT2E AND
RP USP7, INTERACTION WITH KMT2E AND USP7, SUBCELLULAR LOCATION, ACTIVE SITE,
RP AND MUTAGENESIS OF HIS-508 AND HIS-568.
RX PubMed=26678539; DOI=10.1371/journal.pone.0145023;
RA Ding X., Jiang W., Zhou P., Liu L., Wan X., Yuan X., Wang X., Chen M.,
RA Chen J., Yang J., Kong C., Li B., Peng C., Wong C.C., Hou F., Zhang Y.;
RT "Mixed lineage leukemia 5 (MLL5) protein stability is cooperatively
RT regulated by O-GlcNac transferase (OGT) and ubiquitin specific protease 7
RT (USP7).";
RL PLoS ONE 10:E0145023-E0145023(2015).
RN [30]
RP FUNCTION.
RX PubMed=27527864; DOI=10.18632/oncotarget.11083;
RA Jo Y.K., Park N.Y., Park S.J., Kim B.G., Shin J.H., Jo D.S., Bae D.J.,
RA Suh Y.A., Chang J.H., Lee E.K., Kim S.Y., Kim J.C., Cho D.H.;
RT "O-GlcNAcylation of ATG4B positively regulates autophagy by increasing its
RT hydroxylase activity.";
RL Oncotarget 7:57186-57196(2016).
RN [31]
RP INTERACTION WITH HUMAN T-CELL LEUKEMIA VIRUS 1/HTLV-1 PROTEIN TAX.
RX PubMed=28742148; DOI=10.1371/journal.ppat.1006518;
RA Groussaud D., Khair M., Tollenaere A.I., Waast L., Kuo M.S., Mangeney M.,
RA Martella C., Fardini Y., Coste S., Souidi M., Benit L., Pique C., Issad T.;
RT "Hijacking of the O-GlcNAcZYME complex by the HTLV-1 Tax oncoprotein
RT facilitates viral transcription.";
RL PLoS Pathog. 13:E1006518-E1006518(2017).
RN [32]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30699359; DOI=10.1016/j.celrep.2019.01.018;
RA Sager R.A., Woodford M.R., Backe S.J., Makedon A.M., Baker-Williams A.J.,
RA DiGregorio B.T., Loiselle D.R., Haystead T.A., Zachara N.E., Prodromou C.,
RA Bourboulia D., Schmidt L.S., Linehan W.M., Bratslavsky G., Mollapour M.;
RT "Post-translational regulation of FNIP1 creates a rheostat for the
RT molecular chaperone Hsp90.";
RL Cell Rep. 26:1344-1356(2019).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 26-400, FUNCTION, CATALYTIC
RP ACTIVITY, DOMAIN, AND MUTAGENESIS OF TRP-208 AND ILE-211.
RX PubMed=15361863; DOI=10.1038/nsmb833;
RA Jinek M., Rehwinkel J., Lazarus B.D., Izaurralde E., Hanover J.A.,
RA Conti E.;
RT "The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits
RT structural similarities to importin alpha.";
RL Nat. Struct. Mol. Biol. 11:1001-1007(2004).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 323-1041 IN COMPLEXES WITH UDP
RP AND PEPTIDE SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF
RP HIS-508; HIS-568 AND HIS-911.
RX PubMed=21240259; DOI=10.1038/nature09638;
RA Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S.;
RT "Structure of human O-GlcNAc transferase and its complex with a peptide
RT substrate.";
RL Nature 469:564-567(2011).
RN [35] {ECO:0007744|PDB:4GYW, ECO:0007744|PDB:4GYY, ECO:0007744|PDB:4GZ3, ECO:0007744|PDB:4GZ5, ECO:0007744|PDB:4GZ6}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 323-1041 IN COMPLEXES WITH UDP;
RP PEPTIDE SUBSTRATE; SUBSTRATE ANALOGS; PRODUCT AND PRODUCT ANALOG, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, SUBSTRATE SPECIFICITY, AND REACTION MECHANISM.
RX PubMed=23103939; DOI=10.1038/nchembio.1109;
RA Lazarus M.B., Jiang J., Gloster T.M., Zandberg W.F., Whitworth G.E.,
RA Vocadlo D.J., Walker S.;
RT "Structural snapshots of the reaction coordinate for O-GlcNAc
RT transferase.";
RL Nat. Chem. Biol. 8:966-968(2012).
RN [36]
RP VARIANT XLID106 THR-319.
RX PubMed=26273451; DOI=10.1002/ccr3.301;
RA Bouazzi H., Lesca G., Trujillo C., Alwasiyah M.K., Munnich A.;
RT "Nonsyndromic X-linked intellectual deficiency in three brothers with a
RT novel MED12 missense mutation [c.5922G>T (p.Glu1974His)].";
RL Clin. Case Rep. 3:604-609(2015).
RN [37]
RP VARIANT XLID106 PHE-254, CHARACTERIZATION OF VARIANT XLID106 PHE-254, AND
RP FUNCTION.
RX PubMed=28302723; DOI=10.1074/jbc.m116.771030;
RA Vaidyanathan K., Niranjan T., Selvan N., Teo C.F., May M., Patel S.,
RA Weatherly B., Skinner C., Opitz J., Carey J., Viskochil D., Gecz J.,
RA Shaw M., Peng Y., Alexov E., Wang T., Schwartz C., Wells L.;
RT "Identification and characterization of a missense mutation in the O-linked
RT beta-N-acetylglucosamine (O-GlcNAc) transferase gene that segregates with
RT X-linked intellectual disability.";
RL J. Biol. Chem. 292:8948-8963(2017).
RN [38]
RP VARIANT XLID106 PRO-284, CHARACTERIZATION OF VARIANT XLID106 PRO-284, AND
RP FUNCTION.
RX PubMed=28584052; DOI=10.1074/jbc.m117.790097;
RA Willems A.P., Gundogdu M., Kempers M.J.E., Giltay J.C., Pfundt R.,
RA Elferink M., Loza B.F., Fuijkschot J., Ferenbach A.T., van Gassen K.L.I.,
RA van Aalten D.M.F., Lefeber D.J.;
RT "Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with
RT X-linked intellectual disability.";
RL J. Biol. Chem. 292:12621-12631(2017).
CC -!- FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from
CC UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear
CC proteins resulting in their modification with a beta-linked N-
CC acetylglucosamine (O-GlcNAc) (PubMed:26678539, PubMed:23103939,
CC PubMed:21240259, PubMed:21285374, PubMed:15361863). Glycosylates a
CC large and diverse number of proteins including histone H2B, AKT1,
CC ATG4B, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1 (PubMed:19451179,
CC PubMed:20200153, PubMed:21285374, PubMed:22923583, PubMed:23353889,
CC PubMed:24474760, PubMed:26678539, PubMed:27527864). Can regulate their
CC cellular processes via cross-talk between glycosylation and
CC phosphorylation or by affecting proteolytic processing
CC (PubMed:21285374). Probably by glycosylating KMT2E/MLL5, stabilizes
CC KMT2E/MLL5 by preventing its ubiquitination (PubMed:26678539). Involved
CC in insulin resistance in muscle and adipocyte cells via glycosylating
CC insulin signaling components and inhibiting the 'Thr-308'
CC phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating
CC insulin signaling (By similarity). Involved in glycolysis regulation by
CC mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its
CC activity (PubMed:22923583). Component of a THAP1/THAP3-HCFC1-OGT
CC complex that is required for the regulation of the transcriptional
CC activity of RRM1. Plays a key role in chromatin structure by mediating
CC O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich
CC transcription start sites of active genes via its interaction with TET
CC proteins (TET1, TET2 or TET3) (PubMed:22121020, PubMed:23353889). As
CC part of the NSL complex indirectly involved in acetylation of
CC nucleosomal histone H4 on several lysine residues (PubMed:20018852). O-
CC GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and
CC facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex
CC (PubMed:24474760). Regulates circadian oscillation of the clock genes
CC and glucose homeostasis in the liver. Stabilizes clock proteins
CC ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their
CC ubiquitination and subsequent degradation. Promotes the CLOCK-
CC ARNTL/BMAL1-mediated transcription of genes in the negative loop of the
CC circadian clock such as PER1/2 and CRY1/2 (PubMed:12150998,
CC PubMed:19451179, PubMed:20018868, PubMed:20200153, PubMed:21285374,
CC PubMed:15361863). O-glycosylates HCFC1 and regulates its proteolytic
CC processing and transcriptional activity (PubMed:21285374,
CC PubMed:28584052, PubMed:28302723). Regulates mitochondrial motility in
CC neurons by mediating glycosylation of TRAK1 (By similarity).
CC Glycosylates HOXA1 (By similarity). O-glycosylates FNIP1
CC (PubMed:30699359). Promotes autophagy by mediating O-glycosylation of
CC ATG4B (PubMed:27527864). {ECO:0000250|UniProtKB:P56558,
CC ECO:0000250|UniProtKB:Q8CGY8, ECO:0000269|PubMed:12150998,
CC ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:19451179,
CC ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20018868,
CC ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:21240259,
CC ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:22121020,
CC ECO:0000269|PubMed:22923583, ECO:0000269|PubMed:23103939,
CC ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:24474760,
CC ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:27527864,
CC ECO:0000269|PubMed:28302723, ECO:0000269|PubMed:28584052,
CC ECO:0000269|PubMed:30699359}.
CC -!- FUNCTION: [Isoform 2]: The mitochondrial isoform (mOGT) is cytotoxic
CC and triggers apoptosis in several cell types including INS1, an
CC insulinoma cell line. {ECO:0000269|PubMed:20824293}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-
CC acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.255;
CC Evidence={ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259,
CC ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:23103939,
CC ECO:0000269|PubMed:30699359, ECO:0000305|PubMed:26678539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48905;
CC Evidence={ECO:0000269|PubMed:30699359};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-
CC (N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:48908, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90840; EC=2.4.1.255;
CC Evidence={ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259,
CC ECO:0000269|PubMed:21285374, ECO:0000305|PubMed:26678539};
CC -!- ACTIVITY REGULATION: Subject to product inhibition by UDP.
CC {ECO:0000269|PubMed:21240259}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for UDP-N-acetyl-D-glucosamine
CC {ECO:0000269|PubMed:21240259};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259,
CC ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:23103939,
CC ECO:0000269|PubMed:26678539}.
CC -!- SUBUNIT: Monomer; may exist in different oligomerization states in
CC cells (PubMed:21240259). Homotrimer, oligomerizes via TPR repeats 6 and
CC 7. Trimerization is not necessary for activity in vitro, however it
CC increases affinity for UDP-GlcNAc (By similarity). Component of a
CC THAP1/THAP3-HCFC1-OGT complex (PubMed:20200153). Component of the NSL
CC complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1,
CC PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:20018852). Interacts directly
CC with HCFC1; the interaction O-glycosylates HCFC1, regulates its
CC proteolytic processing and transcriptional activity and, in turn,
CC stabilizes OGT in the nucleus (PubMed:12670868, PubMed:20200153,
CC PubMed:21285374, PubMed:23353889). Interacts (via TPRs 1-6) with SIN3A;
CC the interaction mediates transcriptional repression in parallel with
CC histone deacetylase (PubMed:12150998). Interacts (via TPR 5-6) with
CC TET1, TET2 and TET3 (PubMed:23353889, PubMed:23222540). Interacts (via
CC TPR repeats 6 and 7) with ATXN10 (By similarity). Interacts with
CC histone H2B (PubMed:22121020). Interacts with ARNTL/BMAL1. Found in a
CC complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT
CC and TET1. Interacts with SINHCAF (By similarity). Component of a
CC complex composed of KMT2E/MLL5 (isoform 3), OGT (isoform 1) and USP7;
CC the complex stabilizes KMT2E/MLL5, preventing KMT2E/MLL5 ubiquitination
CC and proteosomal-mediated degradation (PubMed:26678539). Isoform 1
CC interacts (via TRP repeats) with isoform 3 KMT2E/MLL5 (via N-terminus)
CC (PubMed:26678539, PubMed:23629655). Isoform 1 interacts with USP7
CC (PubMed:26678539). Interacts with TRAK1; this interaction is not
CC required for glycosylation of TRAK1 by this protein. Found in a complex
CC with KIF5B, RHOT1, RHOT2 and TRAK1 (PubMed:24995978). Interacts (via
CC TPR repeats domain) with HOXA1; the interaction takes place mainly in
CC the nucleus (By similarity). Interacts with NSD2 (By similarity).
CC {ECO:0000250|UniProtKB:P56558, ECO:0000250|UniProtKB:Q8CGY8,
CC ECO:0000269|PubMed:12150998, ECO:0000269|PubMed:12670868,
CC ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20200153,
CC ECO:0000269|PubMed:21240259, ECO:0000269|PubMed:21285374,
CC ECO:0000269|PubMed:22121020, ECO:0000269|PubMed:23222540,
CC ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:23629655,
CC ECO:0000269|PubMed:24995978, ECO:0000269|PubMed:26678539}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human T-cell leukemia
CC virus 1/HTLV-1 protein Tax; this interaction increases Tax interacting
CC partner CREB1 O-GlcNAcylation. {ECO:0000269|PubMed:28742148}.
CC -!- INTERACTION:
CC O15294; P51610: HCFC1; NbExp=10; IntAct=EBI-539828, EBI-396176;
CC O15294; O95644: NFATC1; NbExp=2; IntAct=EBI-539828, EBI-6907210;
CC O15294; Q9H1M0: NUP62CL; NbExp=4; IntAct=EBI-539828, EBI-751933;
CC O15294; Q8NDX5: PHC3; NbExp=3; IntAct=EBI-539828, EBI-1223801;
CC O15294; P36873: PPP1CC; NbExp=11; IntAct=EBI-539828, EBI-356283;
CC O15294; P11464: PSG1; NbExp=3; IntAct=EBI-539828, EBI-716740;
CC O15294; Q04206: RELA; NbExp=2; IntAct=EBI-539828, EBI-73886;
CC O15294; O95721: SNAP29; NbExp=2; IntAct=EBI-539828, EBI-490676;
CC O15294; Q15750: TAB1; NbExp=3; IntAct=EBI-539828, EBI-358643;
CC O15294; E7EQS8: TET2; NbExp=3; IntAct=EBI-539828, EBI-10177000;
CC O15294; Q6N021: TET2; NbExp=7; IntAct=EBI-539828, EBI-310727;
CC O15294; Q6N021-1: TET2; NbExp=5; IntAct=EBI-539828, EBI-20717492;
CC O15294; O43151: TET3; NbExp=7; IntAct=EBI-539828, EBI-2831148;
CC O15294; Q9UPV9: TRAK1; NbExp=3; IntAct=EBI-539828, EBI-1105048;
CC O15294; O94763: URI1; NbExp=10; IntAct=EBI-539828, EBI-357067;
CC O15294; O94763-1: URI1; NbExp=3; IntAct=EBI-539828, EBI-12590720;
CC O15294; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-539828, EBI-3957603;
CC O15294; P63088: Ppp1cc; Xeno; NbExp=3; IntAct=EBI-539828, EBI-80049;
CC O15294; Q8BG87: Tet3; Xeno; NbExp=2; IntAct=EBI-539828, EBI-9031997;
CC O15294-3; A0A0S2Z5B5: NUP62CL; NbExp=3; IntAct=EBI-11536584, EBI-16439000;
CC O15294-3; Q9H1M0: NUP62CL; NbExp=3; IntAct=EBI-11536584, EBI-751933;
CC O15294-3; Q9UHR5: SAP30BP; NbExp=3; IntAct=EBI-11536584, EBI-751683;
CC O15294-3; Q8N9R8: SCAI; NbExp=3; IntAct=EBI-11536584, EBI-4395514;
CC O15294-3; Q15973: ZNF124; NbExp=3; IntAct=EBI-11536584, EBI-2555767;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26678539}. Cytoplasm
CC {ECO:0000269|PubMed:26678539}. Note=Predominantly localizes to the
CC nucleus. {ECO:0000269|PubMed:26678539}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion
CC {ECO:0000269|PubMed:20824293}. Membrane {ECO:0000269|PubMed:20824293}.
CC Note=Associates with the mitochondrial inner membrane.
CC {ECO:0000269|PubMed:20824293}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:21285374}. Nucleus {ECO:0000269|PubMed:20018852,
CC ECO:0000269|PubMed:21285374}. Cell membrane
CC {ECO:0000250|UniProtKB:P56558}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:P56558}. Cell projection
CC {ECO:0000250|UniProtKB:P56558}. Note=Mostly in the nucleus. Retained in
CC the nucleus via interaction with HCFC1 (PubMed:21285374). After insulin
CC induction, translocated from the nucleus to the cell membrane via
CC phosphatidylinositide binding. Colocalizes with AKT1 at the plasma
CC membrane. TRAK1 recruits this protein to mitochondria. In the absence
CC of TRAK1, localizes in cytosol and nucleus (By similarity).
CC {ECO:0000250|UniProtKB:P56558, ECO:0000269|PubMed:21285374}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3; Synonyms=Nucleocytoplasmic isoform, ncOGT;
CC IsoId=O15294-1; Sequence=Displayed;
CC Name=2; Synonyms=Mitochondrial isoform, mOGT;
CC IsoId=O15294-2; Sequence=VSP_006553;
CC Name=1;
CC IsoId=O15294-3; Sequence=VSP_014164;
CC Name=4; Synonyms=Short isoform, sOGT;
CC IsoId=O15294-4; Sequence=VSP_040764;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and to a lesser extent
CC in skeletal muscle, heart, brain and placenta. Present in trace amounts
CC in lung and liver. {ECO:0000269|PubMed:9083068}.
CC -!- INDUCTION: Induction of the nucleocytoplasmic OGT (ncOGT) isoform in
CC the liver on glucose deprivation is mediated by the decreased
CC hexosamine biosynthesis pathway (HBP) flux.
CC {ECO:0000269|PubMed:19073609}.
CC -!- DOMAIN: The TPR repeat domain is required for substrate binding and
CC oligomerization. {ECO:0000269|PubMed:15361863}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000269|PubMed:21285374}.
CC -!- PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively
CC regulates its activity. {ECO:0000250}.
CC -!- DISEASE: Note=Regulation of OGT activity and altered O-GlcNAcylations
CC are implicated in diabetes and Alzheimer disease. O-GlcNAcylation of
CC AKT1 affects insulin signaling and, possibly diabetes. Reduced O-
CC GlcNAcylations and resulting increased phosphorylations of MAPT/TAU are
CC observed in Alzheimer disease (AD) brain cerebrum.
CC {ECO:0000269|PubMed:19451179}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked 106 (XLID106)
CC [MIM:300997]: A form of intellectual disability, a disorder
CC characterized by significantly below average general intellectual
CC functioning associated with impairments in adaptive behavior and
CC manifested during the developmental period. Intellectual deficiency is
CC the only primary symptom of non-syndromic X-linked forms, while
CC syndromic forms present with associated physical, neurological and/or
CC psychiatric manifestations. {ECO:0000269|PubMed:26273451,
CC ECO:0000269|PubMed:28302723, ECO:0000269|PubMed:28584052}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be part of the MLL5-L complex, at
CC least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and
CC OGT (PubMed:19377461). However, the corresponding article has been
CC retracted (PubMed:24336203). {ECO:0000269|PubMed:19377461,
CC ECO:0000269|PubMed:24336203}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=UDP-N-
CC acetylglucosamine--peptide N-acetylglucosaminyltransferase 110kDa
CC subunit;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_554";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U77413; AAB63466.1; -; mRNA.
DR EMBL; AJ315767; CAC86127.1; -; Genomic_DNA.
DR EMBL; AJ315767; CAC86128.1; -; Genomic_DNA.
DR EMBL; AJ315767; CAC86129.1; -; Genomic_DNA.
DR EMBL; AL050366; CAB62528.1; -; mRNA.
DR EMBL; AL833085; CAD89970.1; -; mRNA.
DR EMBL; BX537844; CAD97853.1; -; mRNA.
DR EMBL; BC014434; AAH14434.1; -; mRNA.
DR EMBL; BC038180; AAH38180.1; -; mRNA.
DR CCDS; CCDS14414.1; -. [O15294-1]
DR CCDS; CCDS35502.1; -. [O15294-3]
DR RefSeq; NP_858058.1; NM_181672.2. [O15294-1]
DR RefSeq; NP_858059.1; NM_181673.2. [O15294-3]
DR RefSeq; XP_016885396.1; XM_017029907.1.
DR RefSeq; XP_016885397.1; XM_017029908.1. [O15294-4]
DR PDB; 1W3B; X-ray; 2.85 A; A/B=26-410.
DR PDB; 3PE3; X-ray; 2.78 A; A/B/C/D=323-1041.
DR PDB; 3PE4; X-ray; 1.95 A; A/C=323-1041.
DR PDB; 3TAX; X-ray; 1.88 A; A/C=323-1041.
DR PDB; 4AY5; X-ray; 3.15 A; A/B/C/D=323-1041.
DR PDB; 4AY6; X-ray; 3.30 A; A/B/C/D=323-1041.
DR PDB; 4CDR; X-ray; 3.15 A; A/B/C/D=323-1041.
DR PDB; 4GYW; X-ray; 1.70 A; A/C=323-1041.
DR PDB; 4GYY; X-ray; 1.85 A; A/C=323-1041.
DR PDB; 4GZ3; X-ray; 1.90 A; A/C=323-1041.
DR PDB; 4GZ5; X-ray; 3.08 A; A/B/C/D=323-1041.
DR PDB; 4GZ6; X-ray; 2.98 A; A/B/C/D=323-1041.
DR PDB; 4N39; X-ray; 1.76 A; A=323-1041.
DR PDB; 4N3A; X-ray; 1.88 A; A=323-1041.
DR PDB; 4N3B; X-ray; 2.17 A; A=323-1041.
DR PDB; 4N3C; X-ray; 2.55 A; A=323-1041.
DR PDB; 4XI9; X-ray; 3.10 A; A/B/C/D=323-1041.
DR PDB; 4XIF; X-ray; 3.20 A; A/B/C/D=323-1041.
DR PDB; 5BNW; X-ray; 2.40 A; A=323-1041.
DR PDB; 5C1D; X-ray; 2.05 A; A=323-1041.
DR PDB; 5HGV; X-ray; 2.05 A; A/C=323-1041.
DR PDB; 5LVV; X-ray; 2.54 A; A=325-1046.
DR PDB; 5LWV; X-ray; 1.90 A; A=325-1046.
DR PDB; 5NPR; X-ray; 1.85 A; A=325-1041.
DR PDB; 5NPS; X-ray; 1.68 A; A=324-1041.
DR PDB; 5VIE; X-ray; 2.60 A; A/C=323-1041.
DR PDB; 5VIF; X-ray; 2.25 A; A=323-1041.
DR PDB; 6E37; X-ray; 2.53 A; A=323-1041.
DR PDB; 6EOU; X-ray; 1.75 A; A=26-410.
DR PDB; 6IBO; X-ray; 2.17 A; A=323-1041.
DR PDB; 6MA1; X-ray; 2.75 A; A=323-1041.
DR PDB; 6MA2; X-ray; 2.10 A; A=323-1041.
DR PDB; 6MA3; X-ray; 2.00 A; A=323-1041.
DR PDB; 6MA4; X-ray; 2.00 A; A=323-1041.
DR PDB; 6MA5; X-ray; 2.00 A; A=323-1041.
DR PDB; 6Q4M; X-ray; 2.20 A; A=323-1041.
DR PDB; 6TKA; X-ray; 1.91 A; AAA=323-1046.
DR PDB; 7NTF; EM; 5.32 A; A/B=2-1046.
DR PDBsum; 1W3B; -.
DR PDBsum; 3PE3; -.
DR PDBsum; 3PE4; -.
DR PDBsum; 3TAX; -.
DR PDBsum; 4AY5; -.
DR PDBsum; 4AY6; -.
DR PDBsum; 4CDR; -.
DR PDBsum; 4GYW; -.
DR PDBsum; 4GYY; -.
DR PDBsum; 4GZ3; -.
DR PDBsum; 4GZ5; -.
DR PDBsum; 4GZ6; -.
DR PDBsum; 4N39; -.
DR PDBsum; 4N3A; -.
DR PDBsum; 4N3B; -.
DR PDBsum; 4N3C; -.
DR PDBsum; 4XI9; -.
DR PDBsum; 4XIF; -.
DR PDBsum; 5BNW; -.
DR PDBsum; 5C1D; -.
DR PDBsum; 5HGV; -.
DR PDBsum; 5LVV; -.
DR PDBsum; 5LWV; -.
DR PDBsum; 5NPR; -.
DR PDBsum; 5NPS; -.
DR PDBsum; 5VIE; -.
DR PDBsum; 5VIF; -.
DR PDBsum; 6E37; -.
DR PDBsum; 6EOU; -.
DR PDBsum; 6IBO; -.
DR PDBsum; 6MA1; -.
DR PDBsum; 6MA2; -.
DR PDBsum; 6MA3; -.
DR PDBsum; 6MA4; -.
DR PDBsum; 6MA5; -.
DR PDBsum; 6Q4M; -.
DR PDBsum; 6TKA; -.
DR PDBsum; 7NTF; -.
DR AlphaFoldDB; O15294; -.
DR SMR; O15294; -.
DR BioGRID; 114049; 885.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-809; NSL histone acetyltransferase complex.
DR CORUM; O15294; -.
DR DIP; DIP-33491N; -.
DR IntAct; O15294; 126.
DR MINT; O15294; -.
DR STRING; 9606.ENSP00000362824; -.
DR BindingDB; O15294; -.
DR ChEMBL; CHEMBL5955; -.
DR CAZy; GT41; Glycosyltransferase Family 41.
DR GlyGen; O15294; 8 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; O15294; -.
DR MetOSite; O15294; -.
DR PhosphoSitePlus; O15294; -.
DR BioMuta; OGT; -.
DR CPTAC; CPTAC-1261; -.
DR CPTAC; CPTAC-1262; -.
DR EPD; O15294; -.
DR jPOST; O15294; -.
DR MassIVE; O15294; -.
DR MaxQB; O15294; -.
DR PaxDb; O15294; -.
DR PeptideAtlas; O15294; -.
DR PRIDE; O15294; -.
DR ProteomicsDB; 48562; -. [O15294-1]
DR ProteomicsDB; 48563; -. [O15294-2]
DR ProteomicsDB; 48564; -. [O15294-3]
DR ProteomicsDB; 48565; -. [O15294-4]
DR Antibodypedia; 27791; 462 antibodies from 45 providers.
DR DNASU; 8473; -.
DR Ensembl; ENST00000373701.7; ENSP00000362805.3; ENSG00000147162.14. [O15294-3]
DR Ensembl; ENST00000373719.8; ENSP00000362824.3; ENSG00000147162.14. [O15294-1]
DR GeneID; 8473; -.
DR KEGG; hsa:8473; -.
DR MANE-Select; ENST00000373719.8; ENSP00000362824.3; NM_181672.3; NP_858058.1.
DR UCSC; uc004eaa.3; human. [O15294-1]
DR CTD; 8473; -.
DR DisGeNET; 8473; -.
DR GeneCards; OGT; -.
DR HGNC; HGNC:8127; OGT.
DR HPA; ENSG00000147162; Low tissue specificity.
DR MalaCards; OGT; -.
DR MIM; 300255; gene.
DR MIM; 300997; phenotype.
DR neXtProt; NX_O15294; -.
DR NIAGADS; ENSG00000147162; -.
DR OpenTargets; ENSG00000147162; -.
DR PharmGKB; PA31914; -.
DR VEuPathDB; HostDB:ENSG00000147162; -.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG4626; Eukaryota.
DR GeneTree; ENSGT00940000155085; -.
DR HOGENOM; CLU_001721_1_0_1; -.
DR InParanoid; O15294; -.
DR OMA; HAYSEKL; -.
DR OrthoDB; 1138059at2759; -.
DR PhylomeDB; O15294; -.
DR TreeFam; TF105785; -.
DR BioCyc; MetaCyc:ENSG00000147162-MON; -.
DR BRENDA; 2.4.1.255; 2681.
DR PathwayCommons; O15294; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR SABIO-RK; O15294; -.
DR SignaLink; O15294; -.
DR SIGNOR; O15294; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 8473; 378 hits in 711 CRISPR screens.
DR ChiTaRS; OGT; human.
DR EvolutionaryTrace; O15294; -.
DR GeneWiki; OGT_(gene); -.
DR GenomeRNAi; 8473; -.
DR Pharos; O15294; Tchem.
DR PRO; PR:O15294; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O15294; protein.
DR Bgee; ENSG00000147162; Expressed in middle temporal gyrus and 212 other tissues.
DR ExpressionAtlas; O15294; baseline and differential.
DR Genevisible; O15294; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044545; C:NSL complex; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0017122; C:protein N-acetylglucosaminyltransferase complex; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; TAS:ProtInc.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; ISS:ARUK-UCL.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0000423; P:mitophagy; ISS:ARUK-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:ComplexPortal.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; IMP:UniProtKB.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; IDA:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0060544; P:regulation of necroptotic process; TAS:Reactome.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IDA:UniProtKB.
DR GO; GO:0007584; P:response to nutrient; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR037919; OGT.
DR InterPro; IPR029489; OGT/SEC/SPY_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44366; PTHR44366; 1.
DR Pfam; PF13844; Glyco_transf_41; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 12.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 12.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW Biological rhythms; Cell membrane; Cell projection; Chromatin regulator;
KW Cytoplasm; Direct protein sequencing; Disease variant; Glycoprotein;
KW Glycosyltransferase; Host-virus interaction; Intellectual disability;
KW Lipid-binding; Membrane; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1046
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase 110 kDa subunit"
FT /id="PRO_0000191772"
FT REPEAT 21..54
FT /note="TPR 1"
FT REPEAT 89..122
FT /note="TPR 2"
FT REPEAT 123..156
FT /note="TPR 3"
FT REPEAT 157..190
FT /note="TPR 4"
FT REPEAT 191..224
FT /note="TPR 5"
FT REPEAT 225..258
FT /note="TPR 6"
FT REPEAT 259..292
FT /note="TPR 7"
FT REPEAT 293..326
FT /note="TPR 8"
FT REPEAT 327..360
FT /note="TPR 9"
FT REPEAT 361..394
FT /note="TPR 10"
FT REPEAT 395..428
FT /note="TPR 11"
FT REPEAT 429..462
FT /note="TPR 12"
FT REPEAT 463..473
FT /note="TPR 13; truncated"
FT REGION 991..1010
FT /note="Required for phosphatidylinositol 3,4,5-triphosphate
FT binding"
FT MOTIF 487..503
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 508
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21240259,
FT ECO:0000305|PubMed:26678539"
FT BINDING 849
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:23103939,
FT ECO:0007744|PDB:4GYW"
FT BINDING 852
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:23103939,
FT ECO:0007744|PDB:4GYW"
FT BINDING 906..908
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:23103939,
FT ECO:0007744|PDB:4GYW"
FT BINDING 911..914
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:23103939,
FT ECO:0007744|PDB:4GYW"
FT BINDING 930..932
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:23103939,
FT ECO:0007744|PDB:4GYW"
FT BINDING 935
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:23103939,
FT ECO:0007744|PDB:4GYW"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine; by GSK3-beta; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CGY8"
FT MOD_RES 4
FT /note="Phosphoserine; by GSK3-beta; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CGY8"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 989
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P56558"
FT CARBOHYD 3
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 4
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..381
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_040764"
FT VAR_SEQ 1..176
FT /note="MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEP
FT DNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEH
FT YRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKAL
FT GRLEEA -> MLQGHFWLVREGIMISPSSPPPPNLFFFPLQIFPFPFTSFPSHLLSLTP
FT P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9083068"
FT /id="VSP_006553"
FT VAR_SEQ 13..22
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_014164"
FT VARIANT 254
FT /note="L -> F (in XLID106; decreased protein abundance;
FT reduced protein stability; dbSNP:rs1131692155)"
FT /evidence="ECO:0000269|PubMed:28302723"
FT /id="VAR_079254"
FT VARIANT 284
FT /note="R -> P (in XLID106; decreased protein abundance;
FT decreased enzyme activity; reduced protein stability;
FT dbSNP:rs1114167891)"
FT /evidence="ECO:0000269|PubMed:28584052"
FT /id="VAR_079183"
FT VARIANT 319
FT /note="A -> T (in XLID106; unknown pathological
FT significance; dbSNP:rs1602147851)"
FT /evidence="ECO:0000269|PubMed:26273451"
FT /id="VAR_074019"
FT VARIANT 538
FT /note="L -> P (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /id="VAR_064736"
FT MUTAGEN 208
FT /note="W->E: Abolishes homodimerization of the TPR domain.
FT Slightly reduced enzyme activity; when associated with D-
FT 211."
FT /evidence="ECO:0000269|PubMed:15361863"
FT MUTAGEN 211
FT /note="I->D: Abolishes homodimerization of the TPR domain.
FT Slightly reduced enzyme activity; when associated with E-
FT 208."
FT /evidence="ECO:0000269|PubMed:15361863"
FT MUTAGEN 508
FT /note="H->A: Loss of enzyme activity. Moderate increase in
FT KMT2E ubiquitination. Moderate increase in KMT2E
FT ubiquitination; when associated with A-508."
FT /evidence="ECO:0000269|PubMed:21240259,
FT ECO:0000269|PubMed:26678539"
FT MUTAGEN 568
FT /note="H->A: Reduces enzyme activity by about 95%. Moderate
FT increase in KMT2E ubiquitination; when associated with A-
FT 508."
FT /evidence="ECO:0000269|PubMed:21240259,
FT ECO:0000269|PubMed:26678539"
FT MUTAGEN 911
FT /note="H->A: Reduces enzyme activity by over 90%."
FT /evidence="ECO:0000269|PubMed:21240259"
FT CONFLICT 308
FT /note="S -> Q (in Ref. 3; CAB62528)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="L -> P (in Ref. 3; CAD97853)"
FT /evidence="ECO:0000305"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1W3B"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:1W3B"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 259..271
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 309..322
FT /evidence="ECO:0007829|PDB:6EOU"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 343..356
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 361..373
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 377..390
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 395..407
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 411..424
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 429..442
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 445..458
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 463..475
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 482..498
FT /evidence="ECO:0007829|PDB:5NPS"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 517..535
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:4GYY"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:5NPS"
FT TURN 550..554
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 556..563
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 569..574
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:5NPS"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 586..594
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 600..608
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 615..617
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 621..631
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 634..639
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 649..652
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 656..664
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:5NPS"
FT TURN 681..683
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 686..691
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 693..698
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 708..711
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 713..715
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 731..737
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 741..746
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:4GYW"
FT STRAND 752..755
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 773..780
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 781..792
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 795..799
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 802..806
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 807..809
FT /evidence="ECO:0007829|PDB:4GYY"
FT HELIX 810..813
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 815..818
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:4AY5"
FT STRAND 825..831
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 832..835
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:6MA5"
FT STRAND 843..845
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 850..852
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 855..867
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 872..877
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 880..882
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 883..892
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 897..899
FT /evidence="ECO:0007829|PDB:4GYW"
FT STRAND 900..904
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 908..914
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 915..917
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 919..922
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 925..927
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 931..938
FT /evidence="ECO:0007829|PDB:5NPS"
FT STRAND 943..945
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 951..953
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 955..963
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 966..968
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 973..985
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 987..1003
FT /evidence="ECO:0007829|PDB:5NPS"
FT HELIX 1005..1007
FT /evidence="ECO:0007829|PDB:6MA4"
FT HELIX 1009..1028
FT /evidence="ECO:0007829|PDB:5NPS"
SQ SEQUENCE 1046 AA; 116925 MW; 852ED68BDDE63363 CRC64;
MASSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA ERHCMQLWRQ EPDNTGVLLL
LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP
DFIDGYINLA AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY
LKAIETQPNF AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI
FDRAVAAYLR ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA
NALKEKGSVA EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF
AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR
AIQINPAFAD AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT
DYDERMKKLV SIVADQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK
PPYEHPKDLK LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN
FRVKVMAEAN HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA
MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP HTFFIGDHAN MFPHLKKKAV
IDFKSNGHIY DNRIVLNGID LKAFLDSLPD VKIVKMKCPD GGDNADSSNT ALNMPVIPMN
TIAEAVIEMI NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED
AIVYCNFNQL YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI
IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL
TCLGCLELIA KNRQEYEDIA VKLGTDLEYL KKVRGKVWKQ RISSPLFNTK QYTMELERLY
LQMWEHYAAG NKPDHMIKPV EVTESA
