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UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC 2.4.1.255) (O-GlcNAc transferase subunit p110) (O-linked N-acetylglucosamine transferase 110 kDa subunit) (OGT)

 OGT1_HUMAN              Reviewed;        1046 AA.
O15294; Q7Z3K0; Q8WWM8; Q96CC1; Q9UG57;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 3.
18-JUL-2018, entry version 205.
RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;
EC=2.4.1.255 {ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259, ECO:0000269|PubMed:21285374, ECO:0000305|PubMed:26678539};
AltName: Full=O-GlcNAc transferase subunit p110;
AltName: Full=O-linked N-acetylglucosamine transferase 110 kDa subunit;
Short=OGT;
Name=OGT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 227-236
AND 955-971, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9083068; DOI=10.1074/jbc.272.14.9316;
Lubas W.A., Frank D.W., Krause M., Hanover J.A.;
"O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein
containing tetratricopeptide repeats.";
J. Biol. Chem. 272:9316-9324(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
PubMed=11773972; DOI=10.1007/s00335-001-2108-9;
Nolte D., Muller U.;
"Human O-GlcNAc transferase (OGT): genomic structure, analysis of
splice variants, fine mapping in Xq13.1.";
Mamm. Genome 13:62-64(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Endometrium, Fetal brain, and Spinal cord;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Colon, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-17; 31-42; 161-168; 244-250; 339-348; 734-752;
868-877 AND 1002-1010, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Dhillon A.S., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[6]
INTERACTION WITH SIN3A, AND FUNCTION.
PubMed=12150998; DOI=10.1016/S0092-8674(02)00810-3;
Yang X., Zhang F., Kudlow J.E.;
"Recruitment of O-GlcNAc transferase to promoters by corepressor
mSin3A: coupling protein O-GlcNAcylation to transcriptional
repression.";
Cell 110:69-80(2002).
[7]
INTERACTION WITH HCFC1.
PubMed=12670868; DOI=10.1101/gad.252103;
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
methyltransferase are tethered together selectively by the cell-
proliferation factor HCF-1.";
Genes Dev. 17:896-911(2003).
[8]
SUBCELLULAR LOCATION, FUNCTION, PHOSPHATIDYLINOSITOL-BINDING, AND
MUTAGENESIS OF 991-LYS-LYS-992; ARG-994; LYS-996; LYS-999; ARG-1001
AND LYS-1010.
PubMed=18288188; DOI=10.1038/nature06668;
Yang X., Ongusaha P.P., Miles P.D., Havstad J.C., Zhang F., So W.V.,
Kudlow J.E., Michell R.H., Olefsky J.M., Field S.J., Evans R.M.;
"Phosphoinositide signalling links O-GlcNAc transferase to insulin
resistance.";
Nature 451:964-969(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
FUNCTION, AND ASSOCIATION WITH ALZHEIMER DISEASE.
PubMed=19451179; DOI=10.1093/brain/awp099;
Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I.,
Iqbal K., Gong C.X.;
"Reduced O-GlcNAcylation links lower brain glucose metabolism and tau
pathology in Alzheimer's disease.";
Brain 132:1820-1832(2009).
[12]
INDUCTION.
PubMed=19073609; DOI=10.1074/jbc.M803198200;
Taylor R.P., Geisler T.S., Chambers J.H., McClain D.A.;
"Up-regulation of O-GlcNAc transferase with glucose deprivation in
HepG2 cells is mediated by decreased hexosamine pathway flux.";
J. Biol. Chem. 284:3425-3432(2009).
[13]
CAUTION.
PubMed=19377461; DOI=10.1038/nature07954;
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
Kitagawa H., Kato S.;
"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
granulopoiesis.";
Nature 459:455-459(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
CAUTION AND RETRACTION.
PubMed=24336203; DOI=10.1038/nature12896;
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
Kitagawa H., Kato S.;
"Retraction: GlcNAcylation of a histone methyltransferase in retinoic-
acid-induced granulopoiesis.";
Nature 505:574-574(2014).
[18]
FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=20018852; DOI=10.1074/jbc.C109.087981;
Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
Washburn M.P., Conaway J.W., Conaway R.C.;
"Subunit composition and substrate specificity of a MOF-containing
histone acetyltransferase distinct from the male-specific lethal (MSL)
complex.";
J. Biol. Chem. 285:4268-4272(2010).
[19]
FUNCTION, AND POSSIBLE ASSOCIATION WITH DIABETES.
PubMed=20018868; DOI=10.1074/jbc.M109.077818;
Whelan S.A., Dias W.B., Thiruneelakantapillai L., Lane M.D.,
Hart G.W.;
"Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-
mediated insulin signaling by O-Linked beta-N-acetylglucosamine in
3T3-L1 adipocytes.";
J. Biol. Chem. 285:5204-5211(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT
COMPLEX, INTERACTION WITH HCFC1; THAP1 AND THAP3, AND FUNCTION.
PubMed=20200153; DOI=10.1074/jbc.M109.072579;
Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L.,
Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B.,
Kristie T.M., Girard J.P.;
"The THAP-zinc finger protein THAP1 associates with coactivator HCF-1
and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias.";
J. Biol. Chem. 285:13364-13371(2010).
[21]
FUNCTION (ISOFORM 2).
PubMed=20824293; DOI=10.1007/s00726-010-0719-8;
Shin S.H., Love D.C., Hanover J.A.;
"Elevated O-GlcNAc-dependent signaling through inducible mOGT
expression selectively triggers apoptosis.";
Amino Acids 40:885-893(2011).
[22]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION,
AND INTERACTION WITH HCFC1.
PubMed=21285374; DOI=10.1073/pnas.1013822108;
Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G.,
Vogel J.L., Kristie T.M., Affar E.B.;
"Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates
the host cell factor-1 maturation pathway.";
Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011).
[23]
FUNCTION, AND INTERACTION WITH H2B.
PubMed=22121020; DOI=10.1038/nature10656;
Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S.,
Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F.,
Kitagawa H., Roeder R.G., Brown M., Kato S.;
"GlcNAcylation of histone H2B facilitates its monoubiquitination.";
Nature 480:557-560(2011).
[24]
FUNCTION.
PubMed=22923583; DOI=10.1126/science.1222278;
Yi W., Clark P.M., Mason D.E., Keenan M.C., Hill C., Goddard W.A. III,
Peters E.C., Driggers E.M., Hsieh-Wilson L.C.;
"Phosphofructokinase 1 glycosylation regulates cell growth and
metabolism.";
Science 337:975-980(2012).
[25]
FUNCTION, AND INTERACTION WITH HCFC1; TET2 AND TET3.
PubMed=23353889; DOI=10.1038/emboj.2012.357;
Deplus R., Delatte B., Schwinn M.K., Defrance M., Mendez J.,
Murphy N., Dawson M.A., Volkmar M., Putmans P., Calonne E., Shih A.H.,
Levine R.L., Bernard O., Mercher T., Solary E., Urh M., Daniels D.L.,
Fuks F.;
"TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT
and SET1/COMPASS.";
EMBO J. 32:645-655(2013).
[26]
INTERACTION WITH KMT2E.
PubMed=23629655; DOI=10.1074/jbc.M112.439729;
Zhou P., Wang Z., Yuan X., Zhou C., Liu L., Wan X., Zhang F., Ding X.,
Wang C., Xiong S., Wang Z., Yuan J., Li Q., Zhang Y.;
"Mixed lineage leukemia 5 (MLL5) protein regulates cell cycle
progression and E2F1-responsive gene expression via association with
host cell factor-1 (HCF-1).";
J. Biol. Chem. 288:17532-17543(2013).
[27]
FUNCTION, AND INTERACTION WITH TET2 AND TET3.
PubMed=23222540; DOI=10.1038/nature11742;
Chen Q., Chen Y., Bian C., Fujiki R., Yu X.;
"TET2 promotes histone O-GlcNAcylation during gene transcription.";
Nature 493:561-564(2013).
[28]
FUNCTION.
PubMed=24474760; DOI=10.1073/pnas.1323226111;
Chu C.S., Lo P.W., Yeh Y.H., Hsu P.H., Peng S.H., Teng Y.C.,
Kang M.L., Wong C.H., Juan L.J.;
"O-GlcNAcylation regulates EZH2 protein stability and function.";
Proc. Natl. Acad. Sci. U.S.A. 111:1355-1360(2014).
[29]
FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN A COMPLEX WITH KMT2E
AND USP7, INTERACTION WITH KMT2E AND USP7, SUBCELLULAR LOCATION,
ACTIVE SITE, AND MUTAGENESIS OF HIS-508 AND HIS-568.
PubMed=26678539; DOI=10.1371/journal.pone.0145023;
Ding X., Jiang W., Zhou P., Liu L., Wan X., Yuan X., Wang X., Chen M.,
Chen J., Yang J., Kong C., Li B., Peng C., Wong C.C., Hou F.,
Zhang Y.;
"Mixed lineage leukemia 5 (MLL5) protein stability is cooperatively
regulated by O-GlcNac transferase (OGT) and ubiquitin specific
protease 7 (USP7).";
PLoS ONE 10:E0145023-E0145023(2015).
[30]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 26-400, FUNCTION, CATALYTIC
ACTIVITY, DOMAIN, AND MUTAGENESIS OF TRP-208 AND ILE-211.
PubMed=15361863; DOI=10.1038/nsmb833;
Jinek M., Rehwinkel J., Lazarus B.D., Izaurralde E., Hanover J.A.,
Conti E.;
"The superhelical TPR-repeat domain of O-linked GlcNAc transferase
exhibits structural similarities to importin alpha.";
Nat. Struct. Mol. Biol. 11:1001-1007(2004).
[31]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 323-1041 IN COMPLEXES WITH
UDP AND PEPTIDE SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, AND
MUTAGENESIS OF HIS-508; HIS-568 AND HIS-911.
PubMed=21240259; DOI=10.1038/nature09638;
Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S.;
"Structure of human O-GlcNAc transferase and its complex with a
peptide substrate.";
Nature 469:564-567(2011).
[32]
VARIANT MRX106 THR-319.
PubMed=26273451; DOI=10.1002/ccr3.301;
Bouazzi H., Lesca G., Trujillo C., Alwasiyah M.K., Munnich A.;
"Nonsyndromic X-linked intellectual deficiency in three brothers with
a novel MED12 missense mutation [c.5922G>T (p.Glu1974His)].";
Clin. Case Rep. 3:604-609(2015).
[33]
VARIANT MRX106 PHE-254, CHARACTERIZATION OF VARIANT MRX106 PHE-254,
AND FUNCTION.
PubMed=28302723; DOI=10.1074/jbc.M116.771030;
Vaidyanathan K., Niranjan T., Selvan N., Teo C.F., May M., Patel S.,
Weatherly B., Skinner C., Opitz J., Carey J., Viskochil D., Gecz J.,
Shaw M., Peng Y., Alexov E., Wang T., Schwartz C., Wells L.;
"Identification and characterization of a missense mutation in the O-
linked beta-N-acetylglucosamine (O-GlcNAc) transferase gene that
segregates with X-linked intellectual disability.";
J. Biol. Chem. 292:8948-8963(2017).
[34]
VARIANT MRX106 PRO-284, CHARACTERIZATION OF VARIANT MRX106 PRO-284,
AND FUNCTION.
PubMed=28584052; DOI=10.1074/jbc.M117.790097;
Willems A.P., Gundogdu M., Kempers M.J.E., Giltay J.C., Pfundt R.,
Elferink M., Loza B.F., Fuijkschot J., Ferenbach A.T.,
van Gassen K.L.I., van Aalten D.M.F., Lefeber D.J.;
"Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients
with X-linked intellectual disability.";
J. Biol. Chem. 292:12621-12631(2017).
-!- FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine
from UDP-GlcNAc to a serine or threonine residue in cytoplasmic
and nuclear proteins resulting in their modification with a beta-
linked N-acetylglucosamine (O-GlcNAc) (PubMed:26678539).
Glycosylates a large and diverse number of proteins including
histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1
(PubMed:26678539). Can regulate their cellular processes via
cross-talk between glycosylation and phosphorylation or by
affecting proteolytic processing (PubMed:26678539). Probably by
glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its
ubiquitination (PubMed:26678539). Involved in insulin resistance
in muscle and adipocyte cells via glycosylating insulin signaling
components and inhibiting the 'Thr-308' phosphorylation of AKT1,
enhancing IRS1 phosphorylation and attenuating insulin signaling.
Involved in glycolysis regulation by mediating glycosylation of 6-
phosphofructokinase PFKL, inhibiting its activity
(PubMed:22923583). Component of a THAP1/THAP3-HCFC1-OGT complex
that is required for the regulation of the transcriptional
activity of RRM1. Plays a key role in chromatin structure by
mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited
to CpG-rich transcription start sites of active genes via its
interaction with TET proteins (TET1, TET2 or TET3)
(PubMed:22121020, PubMed:23353889). As part of the NSL complex
indirectly involved in acetylation of nucleosomal histone H4 on
several lysine residues (PubMed:20018852). O-GlcNAcylation of
'Ser-75' of EZH2 increases its stability, and facilitating the
formation of H3K27me3 by the PRC2/EED-EZH2 complex
(PubMed:24474760). Regulates circadian oscillation of the clock
genes and glucose homeostasis in the liver. Stabilizes clock
proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which
prevents their ubiquitination and subsequent degradation. Promotes
the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the
negative loop of the circadian clock such as PER1/2 and CRY1/2
(PubMed:12150998, PubMed:18288188, PubMed:19377461,
PubMed:19451179, PubMed:20018868, PubMed:20200153,
PubMed:21285374, PubMed:15361863). O-glycosylates HCFC1 and
regulates its proteolytic processing and transcriptional activity
(PubMed:21285374, PubMed:28584052, PubMed:28302723).
{ECO:0000269|PubMed:12150998, ECO:0000269|PubMed:15361863,
ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:19451179,
ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20018868,
ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:21285374,
ECO:0000269|PubMed:22121020, ECO:0000269|PubMed:22923583,
ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:24474760,
ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:28302723,
ECO:0000269|PubMed:28584052}.
-!- FUNCTION: Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic
and triggers apoptosis in several cell types including INS1, an
insulinoma cell line.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-
serine. {ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259,
ECO:0000269|PubMed:21285374, ECO:0000305|PubMed:26678539}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-threonine. {ECO:0000269|PubMed:15361863,
ECO:0000269|PubMed:21240259, ECO:0000269|PubMed:21285374,
ECO:0000305|PubMed:26678539}.
-!- ENZYME REGULATION: Subject to product inhibition by UDP.
{ECO:0000269|PubMed:21240259}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.8 uM for UDP-N-acetyl-D-glucosamine
{ECO:0000269|PubMed:21240259};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Heterotrimer; consists of one 78 kDa subunit and two 110
kDa subunits dimerized via TPR repeats 6 and 7. Component of a
THAP1/THAP3-HCFC1-OGT complex (PubMed:20200153). Component of the
NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3,
MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:20018852).
Interacts directly with HCFC1; the interaction O-glycosylates
HCFC1, regulates its proteolytic processing and transcriptional
activity and, in turn, stabilizes OGT in the nucleus
(PubMed:12670868, PubMed:20200153, PubMed:21285374,
PubMed:23353889). Interacts (via TPRs 1-6) with SIN3A; the
interaction mediates transcriptional repression in parallel with
histone deacetylase (PubMed:12150998). Interacts (via TPR 5-6)
with TET1, TET2 and TET3 (PubMed:23353889, PubMed:23222540).
Interacts (via TPR repeats 6 and 7) with ATXN10 (By similarity).
Interacts with histone H2B (PubMed:22121020). Interacts with
ARNTL/BMAL1 (By similarity). Found in a complex composed of at
least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (By
similarity). Interacts with SINHCAF (By similarity). Component of
a complex composed of KMT2E/MLL5 (isoform 3), OGT (isoform 1) and
USP7; the complex stabilizes KMT2E/MLL5, preventing KMT2E/MLL5
ubiquitination and proteosomal-mediated degradation
(PubMed:26678539). Isoform 1 interacts (via TRP repeats) with
isoform 3 KMT2E/MLL5 (via N-terminus) (PubMed:26678539,
PubMed:23629655). Isoform 1 interacts with USP7 (PubMed:26678539).
{ECO:0000250|UniProtKB:Q8CGY8, ECO:0000269|PubMed:12150998,
ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:20018852,
ECO:0000269|PubMed:20200153, ECO:0000269|PubMed:21285374,
ECO:0000269|PubMed:22121020, ECO:0000269|PubMed:23222540,
ECO:0000269|PubMed:23353889, ECO:0000269|PubMed:23629655,
ECO:0000269|PubMed:26678539}.
-!- INTERACTION:
Q12140:BSC1 (xeno); NbExp=3; IntAct=EBI-11536584, EBI-36401;
P51610:HCFC1; NbExp=10; IntAct=EBI-539828, EBI-396176;
P09022:Hoxa1 (xeno); NbExp=3; IntAct=EBI-539828, EBI-3957603;
O95644:NFATC1; NbExp=2; IntAct=EBI-539828, EBI-6907210;
A0A0S2Z5B5:NUP62CL; NbExp=3; IntAct=EBI-11536584, EBI-16439000;
Q9H1M0:NUP62CL; NbExp=4; IntAct=EBI-539828, EBI-751933;
Q8NDX5:PHC3; NbExp=3; IntAct=EBI-539828, EBI-1223801;
P36873:PPP1CC; NbExp=11; IntAct=EBI-539828, EBI-356283;
P63088:Ppp1cc (xeno); NbExp=3; IntAct=EBI-539828, EBI-80049;
P11464:PSG1; NbExp=3; IntAct=EBI-539828, EBI-716740;
Q04206:RELA; NbExp=2; IntAct=EBI-539828, EBI-73886;
O95721:SNAP29; NbExp=2; IntAct=EBI-539828, EBI-490676;
Q15750:TAB1; NbExp=3; IntAct=EBI-539828, EBI-358643;
E7EQS8:TET2; NbExp=3; IntAct=EBI-539828, EBI-10177000;
Q6N021:TET2; NbExp=7; IntAct=EBI-539828, EBI-310727;
O43151:TET3; NbExp=4; IntAct=EBI-539828, EBI-2831148;
Q8BG87:Tet3 (xeno); NbExp=2; IntAct=EBI-539828, EBI-9031997;
Q9UPV9:TRAK1; NbExp=3; IntAct=EBI-539828, EBI-1105048;
O94763:URI1; NbExp=10; IntAct=EBI-539828, EBI-357067;
O94763-1:URI1; NbExp=3; IntAct=EBI-539828, EBI-12590720;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26678539}.
Cytoplasm {ECO:0000269|PubMed:26678539}. Note=Predominantly
localizes to the nucleus. {ECO:0000269|PubMed:26678539}.
-!- SUBCELLULAR LOCATION: Isoform 2: Mitochondrion. Membrane.
Note=Associates with the mitochondrial inner membrane.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus. Cell
membrane. Note=Mostly in the nucleus. Retained in the nucleus via
interaction with HCFC1. After insulin induction, translocated from
the nucleus to the cell membrane via phophatidylinisotide binding.
Colocalizes with AKT1 at the plasma membrane.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=3; Synonyms=Nucleocytoplasmic isoform, ncOGT;
IsoId=O15294-1; Sequence=Displayed;
Name=2; Synonyms=Mitochondrial isoform, mOGT;
IsoId=O15294-2; Sequence=VSP_006553;
Name=1;
IsoId=O15294-3; Sequence=VSP_014164;
Name=4; Synonyms=Short isoform, sOGT;
IsoId=O15294-4; Sequence=VSP_040764;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in pancreas and to a lesser
extent in skeletal muscle, heart, brain and placenta. Present in
trace amounts in lung and liver. {ECO:0000269|PubMed:9083068}.
-!- INDUCTION: Induction of the nucleocytoplasmic OGT (ncOGT) isoform
in the liver on glucose deprivation is mediated by the decreased
hexosamine biosynthesis pathway (HBP) flux.
{ECO:0000269|PubMed:19073609}.
-!- DOMAIN: The TPR repeat domain is required for substrate binding
and oligomerization. {ECO:0000269|PubMed:15361863}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
{ECO:0000269|PubMed:21285374}.
-!- PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively
regulates its activity. {ECO:0000250}.
-!- DISEASE: Note=Regulation of OGT activity and altered O-
GlcNAcylations are implicated in diabetes and Alzheimer disease.
O-GlcNAcylation of AKT1 affects insulin signaling and, possibly
diabetes. Reduced O-GlcNAcylations and resulting increased
phosphorylations of MAPT/TAU are observed in Alzheimer disease
(AD) brain cerebrum.
-!- DISEASE: Mental retardation, X-linked 106 (MRX106) [MIM:300997]: A
form of mental retardation, a disorder characterized by
significantly below average general intellectual functioning
associated with impairments in adaptive behavior and manifested
during the developmental period. Intellectual deficiency is the
only primary symptom of non-syndromic X-linked mental retardation,
while syndromic mental retardation presents with associated
physical, neurological and/or psychiatric manifestations.
{ECO:0000269|PubMed:26273451, ECO:0000269|PubMed:28302723,
ECO:0000269|PubMed:28584052}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
transferase subfamily. {ECO:0000305}.
-!- CAUTION: Was originally thought to be part of the MLL5-L complex,
at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1,
ACTB and OGT (PubMed:19377461). However, the corresponding article
has been retracted (PubMed:24336203).
{ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:24336203}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=UDP-
N-acetylglucosamine--peptide N-acetylglucosaminyltransferase
110kDa subunit;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_554";
-----------------------------------------------------------------------
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EMBL; U77413; AAB63466.1; -; mRNA.
EMBL; AJ315767; CAC86127.1; -; Genomic_DNA.
EMBL; AJ315767; CAC86128.1; -; Genomic_DNA.
EMBL; AJ315767; CAC86129.1; -; Genomic_DNA.
EMBL; AL050366; CAB62528.1; -; mRNA.
EMBL; AL833085; CAD89970.1; -; mRNA.
EMBL; BX537844; CAD97853.1; -; mRNA.
EMBL; BC014434; AAH14434.1; -; mRNA.
EMBL; BC038180; AAH38180.1; -; mRNA.
CCDS; CCDS14414.1; -. [O15294-1]
CCDS; CCDS35502.1; -. [O15294-3]
RefSeq; NP_858058.1; NM_181672.2. [O15294-1]
RefSeq; NP_858059.1; NM_181673.2. [O15294-3]
RefSeq; XP_016885396.1; XM_017029907.1. [O15294-4]
RefSeq; XP_016885397.1; XM_017029908.1. [O15294-4]
UniGene; Hs.405410; -.
PDB; 1W3B; X-ray; 2.85 A; A/B=26-410.
PDB; 3PE3; X-ray; 2.78 A; A/B/C/D=323-1041.
PDB; 3PE4; X-ray; 1.95 A; A/C=323-1041.
PDB; 3TAX; X-ray; 1.88 A; A/C=323-1041.
PDB; 4AY5; X-ray; 3.15 A; A/B/C/D=323-1041.
PDB; 4AY6; X-ray; 3.30 A; A/B/C/D=323-1041.
PDB; 4CDR; X-ray; 3.15 A; A/B/C/D=323-1041.
PDB; 4GYW; X-ray; 1.70 A; A/C=323-1041.
PDB; 4GYY; X-ray; 1.85 A; A/C=323-1041.
PDB; 4GZ3; X-ray; 1.90 A; A/C=323-1041.
PDB; 4GZ5; X-ray; 3.08 A; A/B/C/D=323-1041.
PDB; 4GZ6; X-ray; 2.98 A; A/B/C/D=323-1041.
PDB; 4N39; X-ray; 1.76 A; A=323-1041.
PDB; 4N3A; X-ray; 1.88 A; A=323-1041.
PDB; 4N3B; X-ray; 2.17 A; A=323-1041.
PDB; 4N3C; X-ray; 2.55 A; A=323-1041.
PDB; 4XI9; X-ray; 3.10 A; A/B/C/D=323-1041.
PDB; 4XIF; X-ray; 3.20 A; A/B/C/D=323-1041.
PDB; 5BNW; X-ray; 2.40 A; A=323-1041.
PDB; 5C1D; X-ray; 2.05 A; A=323-1041.
PDB; 5HGV; X-ray; 2.05 A; A/C=323-1041.
PDB; 5LVV; X-ray; 2.54 A; A=325-1046.
PDB; 5LWV; X-ray; 1.90 A; A=325-1046.
PDB; 5NPR; X-ray; 1.85 A; A=325-1041.
PDB; 5NPS; X-ray; 1.68 A; A=324-1041.
PDB; 5VIE; X-ray; 2.60 A; A/C=323-1041.
PDB; 5VIF; X-ray; 2.25 A; A=323-1041.
PDB; 6EOU; X-ray; 1.75 A; A=26-410.
PDBsum; 1W3B; -.
PDBsum; 3PE3; -.
PDBsum; 3PE4; -.
PDBsum; 3TAX; -.
PDBsum; 4AY5; -.
PDBsum; 4AY6; -.
PDBsum; 4CDR; -.
PDBsum; 4GYW; -.
PDBsum; 4GYY; -.
PDBsum; 4GZ3; -.
PDBsum; 4GZ5; -.
PDBsum; 4GZ6; -.
PDBsum; 4N39; -.
PDBsum; 4N3A; -.
PDBsum; 4N3B; -.
PDBsum; 4N3C; -.
PDBsum; 4XI9; -.
PDBsum; 4XIF; -.
PDBsum; 5BNW; -.
PDBsum; 5C1D; -.
PDBsum; 5HGV; -.
PDBsum; 5LVV; -.
PDBsum; 5LWV; -.
PDBsum; 5NPR; -.
PDBsum; 5NPS; -.
PDBsum; 5VIE; -.
PDBsum; 5VIF; -.
PDBsum; 6EOU; -.
ProteinModelPortal; O15294; -.
SMR; O15294; -.
BioGrid; 114049; 111.
ComplexPortal; CPX-809; NSL histone acetyltransferase complex.
CORUM; O15294; -.
DIP; DIP-33491N; -.
IntAct; O15294; 104.
MINT; O15294; -.
STRING; 9606.ENSP00000362824; -.
BindingDB; O15294; -.
ChEMBL; CHEMBL5955; -.
CAZy; GT41; Glycosyltransferase Family 41.
iPTMnet; O15294; -.
PhosphoSitePlus; O15294; -.
BioMuta; OGT; -.
EPD; O15294; -.
MaxQB; O15294; -.
PaxDb; O15294; -.
PeptideAtlas; O15294; -.
PRIDE; O15294; -.
ProteomicsDB; 48562; -.
ProteomicsDB; 48563; -. [O15294-2]
ProteomicsDB; 48564; -. [O15294-3]
ProteomicsDB; 48565; -. [O15294-4]
DNASU; 8473; -.
Ensembl; ENST00000373701; ENSP00000362805; ENSG00000147162. [O15294-3]
Ensembl; ENST00000373719; ENSP00000362824; ENSG00000147162. [O15294-1]
GeneID; 8473; -.
KEGG; hsa:8473; -.
UCSC; uc004eaa.3; human. [O15294-1]
CTD; 8473; -.
DisGeNET; 8473; -.
EuPathDB; HostDB:ENSG00000147162.13; -.
GeneCards; OGT; -.
HGNC; HGNC:8127; OGT.
HPA; CAB034099; -.
HPA; HPA030751; -.
HPA; HPA030752; -.
HPA; HPA030753; -.
HPA; HPA030754; -.
MalaCards; OGT; -.
MIM; 300255; gene.
MIM; 300997; phenotype.
neXtProt; NX_O15294; -.
OpenTargets; ENSG00000147162; -.
PharmGKB; PA31914; -.
eggNOG; KOG1124; Eukaryota.
eggNOG; KOG4626; Eukaryota.
eggNOG; COG3914; LUCA.
GeneTree; ENSGT00550000074327; -.
HOGENOM; HOG000003765; -.
HOVERGEN; HBG000351; -.
InParanoid; O15294; -.
KO; K09667; -.
OMA; PFMDYII; -.
OrthoDB; EOG091G024Y; -.
PhylomeDB; O15294; -.
TreeFam; TF105785; -.
BioCyc; MetaCyc:ENSG00000147162-MONOMER; -.
BRENDA; 2.4.1.255; 2681.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-5689603; UCH proteinases.
SABIO-RK; O15294; -.
SignaLink; O15294; -.
SIGNOR; O15294; -.
UniPathway; UPA00378; -.
ChiTaRS; OGT; human.
EvolutionaryTrace; O15294; -.
GeneWiki; OGT_(gene); -.
GenomeRNAi; 8473; -.
PRO; PR:O15294; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000147162; -.
CleanEx; HS_OGT; -.
ExpressionAtlas; O15294; baseline and differential.
Genevisible; O15294; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0008375; F:acetylglucosaminyltransferase activity; TAS:ProtInc.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
GO; GO:0097363; F:protein O-GlcNAc transferase activity; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
GO; GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
GO; GO:0016485; P:protein processing; IMP:UniProtKB.
GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
GO; GO:0006110; P:regulation of glycolytic process; IDA:UniProtKB.
GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0035020; P:regulation of Rac protein signal transduction; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0032868; P:response to insulin; IDA:UniProtKB.
GO; GO:0007584; P:response to nutrient; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 1.25.40.10; -; 2.
InterPro; IPR037919; OGT.
InterPro; IPR029489; OGT/SEC/SPY_C.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR001440; TPR_1.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR44366; PTHR44366; 1.
Pfam; PF13844; Glyco_transf_41; 1.
Pfam; PF00515; TPR_1; 2.
Pfam; PF13181; TPR_8; 2.
SMART; SM00028; TPR; 12.
SUPFAM; SSF48452; SSF48452; 4.
PROSITE; PS50005; TPR; 12.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Biological rhythms; Cell membrane; Chromatin regulator;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Glycoprotein; Glycosyltransferase; Lipid-binding;
Membrane; Mental retardation; Mitochondrion; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; TPR repeat; Transferase;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
CHAIN 2 1046 UDP-N-acetylglucosamine--peptide N-
acetylglucosaminyltransferase 110 kDa
subunit.
/FTId=PRO_0000191772.
REPEAT 21 54 TPR 1.
REPEAT 89 122 TPR 2.
REPEAT 123 156 TPR 3.
REPEAT 157 190 TPR 4.
REPEAT 191 224 TPR 5.
REPEAT 225 258 TPR 6.
REPEAT 259 292 TPR 7.
REPEAT 293 326 TPR 8.
REPEAT 327 360 TPR 9.
REPEAT 361 394 TPR 10.
REPEAT 395 428 TPR 11.
REPEAT 429 462 TPR 12.
REPEAT 463 473 TPR 13; truncated.
NP_BIND 905 908 UDP.
NP_BIND 911 914 UDP.
NP_BIND 929 931 UDP.
REGION 991 1010 Required for phosphatidylinositol 3,4,5-
triphosphate binding.
MOTIF 487 503 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 508 508 Proton acceptor.
{ECO:0000305|PubMed:21240259,
ECO:0000305|PubMed:26678539}.
BINDING 849 849 UDP.
BINDING 852 852 UDP.
BINDING 935 935 UDP.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
MOD_RES 3 3 Phosphoserine; by GSK3-beta; alternate.
{ECO:0000250|UniProtKB:Q8CGY8}.
MOD_RES 4 4 Phosphoserine; by GSK3-beta; alternate.
{ECO:0000250|UniProtKB:Q8CGY8}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 989 989 Phosphotyrosine.
{ECO:0000250|UniProtKB:P56558}.
CARBOHYD 3 3 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 4 4 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
VAR_SEQ 1 381 Missing (in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_040764.
VAR_SEQ 1 176 MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAE
RHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAI
KQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFI
DGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLG
NLLKALGRLEEA -> MLQGHFWLVREGIMISPSSPPPPNL
FFFPLQIFPFPFTSFPSHLLSLTPP (in isoform 2).
{ECO:0000303|PubMed:9083068}.
/FTId=VSP_006553.
VAR_SEQ 13 22 Missing (in isoform 1).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_014164.
VARIANT 254 254 L -> F (in MRX106; decreased protein
abundance; reduced protein stability;
dbSNP:rs1131692155).
{ECO:0000269|PubMed:28302723}.
/FTId=VAR_079254.
VARIANT 284 284 R -> P (in MRX106; decreased protein
abundance; decreased enzyme activity;
reduced protein stability;
dbSNP:rs1114167891).
{ECO:0000269|PubMed:28584052}.
/FTId=VAR_079183.
VARIANT 319 319 A -> T (in MRX106; unknown pathological
significance).
{ECO:0000269|PubMed:26273451}.
/FTId=VAR_074019.
VARIANT 538 538 L -> P (found in a renal cell carcinoma
sample; somatic mutation).
/FTId=VAR_064736.
MUTAGEN 208 208 W->E: Abolishes homodimerization of the
TPR domain. Slightly reduced enzyme
activity; when associated with D-211.
{ECO:0000269|PubMed:15361863}.
MUTAGEN 211 211 I->D: Abolishes homodimerization of the
TPR domain. Slightly reduced enzyme
activity; when associated with E-208.
{ECO:0000269|PubMed:15361863}.
MUTAGEN 508 508 H->A: Loss of enzyme activity. Moderate
increase in KMT2E ubiquitination.
Moderate increase in KMT2E
ubiquitination; when associated with A-
508. {ECO:0000269|PubMed:21240259,
ECO:0000269|PubMed:26678539}.
MUTAGEN 568 568 H->A: Reduces enzyme activity by about
95%. Moderate increase in KMT2E
ubiquitination; when associated with A-
508. {ECO:0000269|PubMed:21240259,
ECO:0000269|PubMed:26678539}.
MUTAGEN 911 911 H->A: Reduces enzyme activity by over
90%. {ECO:0000269|PubMed:21240259}.
MUTAGEN 991 992 KK->AA: Abolishes phosphatidylinisitol
binding, no translocation to the cell
membrane, and no effect on
phosphorylation of AKT1 nor IRS1.
{ECO:0000269|PubMed:18288188}.
MUTAGEN 994 994 R->A: No effect on phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
MUTAGEN 996 996 K->A: Reduced phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
MUTAGEN 999 999 K->A: Reduced phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
MUTAGEN 1001 1001 R->A: No effect on phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
MUTAGEN 1010 1010 K->A: No effect on phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
CONFLICT 308 308 S -> Q (in Ref. 3; CAB62528).
{ECO:0000305}.
CONFLICT 663 663 L -> P (in Ref. 3; CAD97853).
{ECO:0000305}.
HELIX 27 34 {ECO:0000244|PDB:1W3B}.
HELIX 37 50 {ECO:0000244|PDB:1W3B}.
HELIX 60 67 {ECO:0000244|PDB:6EOU}.
HELIX 71 83 {ECO:0000244|PDB:6EOU}.
HELIX 89 101 {ECO:0000244|PDB:6EOU}.
HELIX 105 118 {ECO:0000244|PDB:6EOU}.
HELIX 123 135 {ECO:0000244|PDB:6EOU}.
HELIX 139 152 {ECO:0000244|PDB:6EOU}.
HELIX 157 169 {ECO:0000244|PDB:6EOU}.
HELIX 173 186 {ECO:0000244|PDB:6EOU}.
HELIX 191 203 {ECO:0000244|PDB:6EOU}.
HELIX 207 220 {ECO:0000244|PDB:6EOU}.
HELIX 225 237 {ECO:0000244|PDB:6EOU}.
HELIX 241 254 {ECO:0000244|PDB:6EOU}.
HELIX 259 271 {ECO:0000244|PDB:6EOU}.
HELIX 275 288 {ECO:0000244|PDB:6EOU}.
HELIX 293 306 {ECO:0000244|PDB:6EOU}.
HELIX 309 322 {ECO:0000244|PDB:6EOU}.
HELIX 325 339 {ECO:0000244|PDB:4GYW}.
HELIX 343 356 {ECO:0000244|PDB:4GYW}.
HELIX 361 373 {ECO:0000244|PDB:4GYW}.
HELIX 377 390 {ECO:0000244|PDB:4GYW}.
HELIX 395 407 {ECO:0000244|PDB:4GYW}.
HELIX 411 424 {ECO:0000244|PDB:4GYW}.
HELIX 429 441 {ECO:0000244|PDB:4GYW}.
HELIX 445 458 {ECO:0000244|PDB:4GYW}.
HELIX 463 475 {ECO:0000244|PDB:4GYW}.
HELIX 482 498 {ECO:0000244|PDB:4GYW}.
HELIX 509 512 {ECO:0000244|PDB:4GYW}.
HELIX 517 536 {ECO:0000244|PDB:4GYW}.
TURN 537 539 {ECO:0000244|PDB:3TAX}.
STRAND 547 549 {ECO:0000244|PDB:4N39}.
TURN 550 554 {ECO:0000244|PDB:4GYW}.
STRAND 556 563 {ECO:0000244|PDB:4GYW}.
STRAND 565 568 {ECO:0000244|PDB:4GYW}.
HELIX 569 574 {ECO:0000244|PDB:4GYW}.
HELIX 577 580 {ECO:0000244|PDB:4GYW}.
TURN 583 585 {ECO:0000244|PDB:4GYW}.
STRAND 586 594 {ECO:0000244|PDB:4GYW}.
HELIX 600 608 {ECO:0000244|PDB:4GYW}.
STRAND 609 614 {ECO:0000244|PDB:4GYW}.
HELIX 615 617 {ECO:0000244|PDB:4GYW}.
HELIX 621 630 {ECO:0000244|PDB:4GYW}.
STRAND 634 639 {ECO:0000244|PDB:4GYW}.
STRAND 641 643 {ECO:0000244|PDB:4GYW}.
HELIX 649 652 {ECO:0000244|PDB:4GYW}.
STRAND 656 661 {ECO:0000244|PDB:4GYW}.
STRAND 676 679 {ECO:0000244|PDB:4GYW}.
TURN 681 683 {ECO:0000244|PDB:4GYW}.
HELIX 686 691 {ECO:0000244|PDB:4GYW}.
STRAND 693 698 {ECO:0000244|PDB:4GYW}.
HELIX 708 711 {ECO:0000244|PDB:4GYW}.
HELIX 713 715 {ECO:0000244|PDB:4GYW}.
STRAND 719 721 {ECO:0000244|PDB:4GYW}.
STRAND 731 737 {ECO:0000244|PDB:4GYW}.
HELIX 741 746 {ECO:0000244|PDB:4GYW}.
STRAND 748 750 {ECO:0000244|PDB:4GYW}.
STRAND 752 754 {ECO:0000244|PDB:4GYW}.
STRAND 774 777 {ECO:0000244|PDB:4GYW}.
HELIX 781 792 {ECO:0000244|PDB:4GYW}.
STRAND 796 799 {ECO:0000244|PDB:4GYW}.
STRAND 802 806 {ECO:0000244|PDB:4GYW}.
HELIX 807 809 {ECO:0000244|PDB:4GYY}.
HELIX 810 813 {ECO:0000244|PDB:4GYW}.
HELIX 815 818 {ECO:0000244|PDB:4GYW}.
STRAND 820 822 {ECO:0000244|PDB:4AY5}.
STRAND 826 831 {ECO:0000244|PDB:4GYW}.
HELIX 832 835 {ECO:0000244|PDB:4GYW}.
STRAND 841 845 {ECO:0000244|PDB:4GYW}.
HELIX 850 852 {ECO:0000244|PDB:4GYW}.
HELIX 855 867 {ECO:0000244|PDB:4GYW}.
STRAND 869 877 {ECO:0000244|PDB:4GYW}.
HELIX 880 882 {ECO:0000244|PDB:4GYW}.
HELIX 883 892 {ECO:0000244|PDB:4GYW}.
HELIX 897 899 {ECO:0000244|PDB:4GYW}.
STRAND 900 904 {ECO:0000244|PDB:4GYW}.
HELIX 908 914 {ECO:0000244|PDB:4GYW}.
HELIX 915 917 {ECO:0000244|PDB:4GYW}.
STRAND 919 922 {ECO:0000244|PDB:4GYW}.
STRAND 925 927 {ECO:0000244|PDB:4GYW}.
HELIX 931 938 {ECO:0000244|PDB:4GYW}.
STRAND 943 945 {ECO:0000244|PDB:4GYW}.
HELIX 951 953 {ECO:0000244|PDB:4GYW}.
HELIX 955 963 {ECO:0000244|PDB:4GYW}.
HELIX 966 968 {ECO:0000244|PDB:4GYW}.
HELIX 973 985 {ECO:0000244|PDB:4GYW}.
HELIX 987 1003 {ECO:0000244|PDB:4GYW}.
HELIX 1005 1007 {ECO:0000244|PDB:4N3C}.
HELIX 1009 1028 {ECO:0000244|PDB:4GYW}.
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


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