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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_MOUSE              Reviewed;        1046 AA.
Q8CGY8; A2ALY1; Q6PG10; Q8BXH6; Q91Y38;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
18-JUL-2018, entry version 137.
RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;
EC=2.4.1.255 {ECO:0000250|UniProtKB:O15294};
AltName: Full=O-GlcNAc transferase subunit p110;
AltName: Full=O-linked N-acetylglucosamine transferase 110 kDa subunit;
Short=OGT;
Name=Ogt;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=12504895; DOI=10.1016/S0003-9861(02)00578-7;
Hanover J.A., Yu S., Lubas W.B., Shin S.H., Ragano-Caracciola M.,
Kochran J., Love D.C.;
"Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc
transferase encoded by a single mammalian gene.";
Arch. Biochem. Biophys. 409:287-297(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
Rumberger J.M., Wu T., Hering M.A., Marshall S.;
"Molecular cloning of the mouse O-GlcNAc transferase.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 894-1046 (ISOFORMS 1/2).
STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
PROTEIN SEQUENCE OF 217-236 AND 421-440, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[7]
INTERACTION WITH ATXN10.
PubMed=16182253; DOI=10.1016/j.bbrc.2005.09.026;
Andrali S.S., Maerz P., Ozcan S.;
"Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic beta
cells.";
Biochem. Biophys. Res. Commun. 337:149-153(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, AND INTERACTION WITH ARNTL/BMAL1.
PubMed=23337503; DOI=10.1016/j.bbrc.2013.01.043;
Ma Y.T., Luo H., Guan W.J., Zhang H., Chen C., Wang Z., Li J.D.;
"O-GlcNAcylation of BMAL1 regulates circadian rhythms in NIH3T3
fibroblasts.";
Biochem. Biophys. Res. Commun. 431:382-387(2013).
[10]
PHOSPHORYLATION AT SER-3 AND SER-4, AND GLYCOSYLATION AT SER-3 AND
SER-4.
PubMed=23395175; DOI=10.1016/j.cmet.2012.12.017;
Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K.,
Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.;
"Glucose sensor O-GlcNAcylation coordinates with phosphorylation to
regulate circadian clock.";
Cell Metab. 17:291-302(2013).
[11]
FUNCTION, AND INDUCTION.
PubMed=23395176; DOI=10.1016/j.cmet.2012.12.015;
Li M.D., Ruan H.B., Hughes M.E., Lee J.S., Singh J.P., Jones S.P.,
Nitabach M.N., Yang X.;
"O-GlcNAc signaling entrains the circadian clock by inhibiting
BMAL1/CLOCK ubiquitination.";
Cell Metab. 17:303-310(2013).
[12]
INTERACTION WITH TET1 AND TET2.
PubMed=23352454; DOI=10.1016/j.molcel.2012.12.019;
Vella P., Scelfo A., Jammula S., Chiacchiera F., Williams K.,
Cuomo A., Roberto A., Christensen J., Bonaldi T., Helin K., Pasini D.;
"Tet proteins connect the O-linked N-acetylglucosamine transferase Ogt
to chromatin in embryonic stem cells.";
Mol. Cell 49:645-656(2013).
[13]
IDENTIFICATION IN A COMPLEX WITH SIN3A; SINHCAF; HDAC1; RBBP4; SAP30
AND TET1, AND INTERACTION WITH SINHCAF.
PubMed=28554894; DOI=10.15252/embj.201696307;
Streubel G., Fitzpatrick D.J., Oliviero G., Scelfo A., Moran B.,
Das S., Munawar N., Watson A., Wynne K., Negri G.L., Dillon E.T.,
Jammula S., Hokamp K., O'Connor D.P., Pasini D., Cagney G.,
Bracken A.P.;
"Fam60a defines a variant Sin3a-Hdac complex in embryonic stem cells
required for self-renewal.";
EMBO J. 36:2216-2232(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). Glycosylates a large and
diverse number of proteins including histone H2B, AKT1, EZH2,
PFKL, KMT2E, MAPT/TAU and HCFC1. Can regulate their cellular
processes via cross-talk between glycosylation and phosphorylation
or by affecting proteolytic processing. Probably by glycosylating
KMT2E, stabilizes KMT2E by preventing its ubiquitination (By
similarity).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. 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). As part of the NSL complex indirectly involved in
acetylation of nucleosomal histone H4 on several lysine residues.
O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and
facilitating the formation of H3K27me3 by the PRC2/EED-EZH2
complex (By similarity). 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:23337503, PubMed:23395176). O-glycosylates HCFC1 and
regulates its proteolytic processing and transcriptional activity
(By similarity). {ECO:0000250|UniProtKB:O15294,
ECO:0000269|PubMed:23337503, ECO:0000269|PubMed:23395176}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-
serine. {ECO:0000250|UniProtKB:O15294}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-threonine. {ECO:0000250|UniProtKB:O15294}.
-!- 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 (By similarity).
Component of a THAP1/THAP3-HCFC1-OGT complex (By similarity).
Component of the NSL complex at least composed of MOF/KAT8,
KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (By
similarity). Interacts directly with HCFC1; the interaction O-
glycosylates HCFC1, regulates its proteolytic processing and
transcriptional activity and, in turn, stabilizes OGT in the
nucleus (By similarity). Interacts (via TPRs 1-6) with SIN3A; the
interaction mediates transcriptional repression in parallel with
histone deacetylase (By similarity). Interacts (via TPR 5-6) with
TET1, TET2 and TET3 (PubMed:23352454). Interacts (via TPR repeats
6 and 7) with ATXN10 (PubMed:16182253). Interacts with histone H2B
(By similarity). Interacts with ARNTL/BMAL1 (PubMed:23337503).
Found in a complex composed of at least SINHCAF, SIN3A, HDAC1,
SAP30, RBBP4, OGT and TET1 (PubMed:28554894). Interacts with
SINHCAF (PubMed:28554894). Component of a complex composed of
KMT2E, OGT and USP7; the complex stabilizes KMT2E, preventing
KMT2E ubiquitination and proteosomal-mediated degradation (By
similarity). Interacts (via TRP repeats) with KMT2E (via N-
terminus) (By similarity). Interacts with USP7 (By similarity).
{ECO:0000250|UniProtKB:O15294, ECO:0000269|PubMed:16182253,
ECO:0000269|PubMed:23337503, ECO:0000269|PubMed:23352454,
ECO:0000269|PubMed:28554894}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15294}.
Nucleus {ECO:0000250|UniProtKB:O15294}. Cell membrane
{ECO:0000250|UniProtKB:O15294}. 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. {ECO:0000250|UniProtKB:O15294}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8CGY8-1; Sequence=Displayed;
Name=2;
IsoId=Q8CGY8-2; Sequence=VSP_024844;
-!- INDUCTION: Expression in the liver oscillates in a circadian
manner. {ECO:0000269|PubMed:23395176}.
-!- DOMAIN: The TPR repeat domain is required for substrate binding
and oligomerization. {ECO:0000250}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
{ECO:0000250}.
-!- PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively
regulates its activity. {ECO:0000269|PubMed:23395175}.
-!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
transferase subfamily. {ECO:0000305}.
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EMBL; AF539527; AAO17363.1; -; Genomic_DNA.
EMBL; AF363030; AAK39123.1; -; mRNA.
EMBL; AL806534; CAM21281.1; -; Genomic_DNA.
EMBL; AL805980; CAM21281.1; JOINED; Genomic_DNA.
EMBL; AL806534; CAM21282.1; -; Genomic_DNA.
EMBL; AL805980; CAM21282.1; JOINED; Genomic_DNA.
EMBL; AL805980; CAM25748.1; -; Genomic_DNA.
EMBL; AL806534; CAM25748.1; JOINED; Genomic_DNA.
EMBL; AL805980; CAM25749.1; -; Genomic_DNA.
EMBL; AL806534; CAM25749.1; JOINED; Genomic_DNA.
EMBL; BC057319; AAH57319.1; -; mRNA.
EMBL; AK047095; BAC32961.1; -; mRNA.
CCDS; CCDS30318.1; -. [Q8CGY8-1]
CCDS; CCDS72415.1; -. [Q8CGY8-2]
RefSeq; NP_001277464.1; NM_001290535.1. [Q8CGY8-2]
RefSeq; NP_631883.2; NM_139144.4. [Q8CGY8-1]
RefSeq; XP_006527799.1; XM_006527736.3. [Q8CGY8-1]
RefSeq; XP_011245805.1; XM_011247503.2. [Q8CGY8-2]
UniGene; Mm.487332; -.
UniGene; Mm.491168; -.
ProteinModelPortal; Q8CGY8; -.
SMR; Q8CGY8; -.
BioGrid; 223870; 16.
ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DIP; DIP-35700N; -.
IntAct; Q8CGY8; 9.
MINT; Q8CGY8; -.
STRING; 10090.ENSMUSP00000045409; -.
CAZy; GT41; Glycosyltransferase Family 41.
iPTMnet; Q8CGY8; -.
PhosphoSitePlus; Q8CGY8; -.
PaxDb; Q8CGY8; -.
PeptideAtlas; Q8CGY8; -.
PRIDE; Q8CGY8; -.
Ensembl; ENSMUST00000044475; ENSMUSP00000045409; ENSMUSG00000034160. [Q8CGY8-1]
Ensembl; ENSMUST00000119299; ENSMUSP00000113454; ENSMUSG00000034160. [Q8CGY8-2]
GeneID; 108155; -.
KEGG; mmu:108155; -.
UCSC; uc009tyc.3; mouse. [Q8CGY8-1]
UCSC; uc057ask.1; mouse. [Q8CGY8-2]
CTD; 8473; -.
MGI; MGI:1339639; Ogt.
eggNOG; KOG1124; Eukaryota.
eggNOG; KOG4626; Eukaryota.
eggNOG; COG3914; LUCA.
GeneTree; ENSGT00550000074327; -.
HOGENOM; HOG000003765; -.
HOVERGEN; HBG000351; -.
InParanoid; Q8CGY8; -.
KO; K09667; -.
OMA; PFMDYII; -.
OrthoDB; EOG091G024Y; -.
PhylomeDB; Q8CGY8; -.
TreeFam; TF105785; -.
BRENDA; 2.4.1.255; 3474.
Reactome; R-MMU-3214847; HATs acetylate histones.
Reactome; R-MMU-5689603; UCH proteinases.
UniPathway; UPA00378; -.
ChiTaRS; Ogt; mouse.
PRO; PR:Q8CGY8; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000034160; -.
Genevisible; Q8CGY8; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0000791; C:euchromatin; ISO:MGI.
GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; TAS:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0042588; C:zymogen granule; ISO:MGI.
GO; GO:0003824; F:catalytic activity; ISS:MGI.
GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); IEA:Ensembl.
GO; GO:0043995; F:histone acetyltransferase activity (H4-K5 specific); IEA:Ensembl.
GO; GO:0043996; F:histone acetyltransferase activity (H4-K8 specific); IEA:Ensembl.
GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
GO; GO:0008080; F:N-acetyltransferase activity; TAS:MGI.
GO; GO:0042277; F:peptide binding; ISO:MGI.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
GO; GO:0097363; F:protein O-GlcNAc transferase activity; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
GO; GO:0006041; P:glucosamine metabolic process; ISO:MGI.
GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:MGI.
GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
GO; GO:1900038; P:negative regulation of cellular response to hypoxia; ISO:MGI.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISO:MGI.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
GO; GO:0045793; P:positive regulation of cell size; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0070208; P:protein heterotrimerization; ISO:MGI.
GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
GO; GO:0016485; P:protein processing; ISS:UniProtKB.
GO; GO:0006111; P:regulation of gluconeogenesis; IMP:UniProtKB.
GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISO:MGI.
GO; GO:0035020; P:regulation of Rac protein signal transduction; ISO:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0032868; P:response to insulin; ISO:MGI.
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; 5.
PROSITE; PS50005; TPR; 12.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Biological rhythms; Cell membrane;
Chromatin regulator; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycoprotein; Glycosyltransferase;
Lipid-binding; Membrane; Nucleus; Phosphoprotein; Reference proteome;
Repeat; TPR repeat; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O15294}.
CHAIN 2 1046 UDP-N-acetylglucosamine--peptide N-
acetylglucosaminyltransferase 110 kDa
subunit.
/FTId=PRO_0000285216.
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. {ECO:0000250}.
NP_BIND 911 914 UDP. {ECO:0000250}.
NP_BIND 929 931 UDP. {ECO:0000250}.
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:0000250}.
BINDING 849 849 UDP. {ECO:0000250}.
BINDING 852 852 UDP. {ECO:0000250}.
BINDING 935 935 UDP. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O15294}.
MOD_RES 3 3 Phosphoserine; by GSK3-beta; alternate.
{ECO:0000269|PubMed:23395175}.
MOD_RES 4 4 Phosphoserine; by GSK3-beta; alternate.
{ECO:0000269|PubMed:23395175}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 989 989 Phosphotyrosine.
{ECO:0000250|UniProtKB:P56558}.
CARBOHYD 3 3 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:23395175}.
CARBOHYD 4 4 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:23395175}.
VAR_SEQ 13 22 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_024844.
CONFLICT 57 57 V -> A (in Ref. 1; AAO17363).
{ECO:0000305}.
CONFLICT 992 992 K -> R (in Ref. 2; AAK39123).
{ECO:0000305}.
SEQUENCE 1046 AA; 116952 MW; FD5EE12844E00097 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 SIVAEQLEKN 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 GGDNPDSSNT ALNMPVIPMN
TIAEAVIEMI NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED
AIVYCNFNQL YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI
IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL
TCLGCLELIA KSRQEYEDIA VKLGTDLEYL KKIRGKVWKQ RISSPLFNTK QYTMELERLY
LQMWEHYAAG NKPDHMIKPV EVTESA


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