OGT1_MOUSE
ID OGT1_MOUSE Reviewed; 1046 AA.
AC Q8CGY8; A2ALY1; Q6PG10; Q8BXH6; Q91Y38;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;
DE EC=2.4.1.255 {ECO:0000269|PubMed:29465778};
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=12504895; DOI=10.1016/s0003-9861(02)00578-7;
RA Hanover J.A., Yu S., Lubas W.B., Shin S.H., Ragano-Caracciola M.,
RA Kochran J., Love D.C.;
RT "Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc
RT transferase encoded by a single mammalian gene.";
RL Arch. Biochem. Biophys. 409:287-297(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RA Rumberger J.M., Wu T., Hering M.A., Marshall S.;
RT "Molecular cloning of the mouse O-GlcNAc transferase.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 894-1046 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP PROTEIN SEQUENCE OF 217-236 AND 421-440, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP INTERACTION WITH ATXN10.
RX PubMed=16182253; DOI=10.1016/j.bbrc.2005.09.026;
RA Andrali S.S., Maerz P., Ozcan S.;
RT "Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic beta
RT cells.";
RL Biochem. Biophys. Res. Commun. 337:149-153(2005).
RN [8]
RP INTERACTION WITH NSD2.
RX PubMed=19483677; DOI=10.1038/nature08086;
RA Nimura K., Ura K., Shiratori H., Ikawa M., Okabe M., Schwartz R.J.,
RA Kaneda Y.;
RT "A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf-
RT Hirschhorn syndrome.";
RL Nature 460:287-291(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH ARNTL/BMAL1.
RX PubMed=23337503; DOI=10.1016/j.bbrc.2013.01.043;
RA Ma Y.T., Luo H., Guan W.J., Zhang H., Chen C., Wang Z., Li J.D.;
RT "O-GlcNAcylation of BMAL1 regulates circadian rhythms in NIH3T3
RT fibroblasts.";
RL Biochem. Biophys. Res. Commun. 431:382-387(2013).
RN [11]
RP PHOSPHORYLATION AT SER-3 AND SER-4, AND GLYCOSYLATION AT SER-3 AND SER-4.
RX PubMed=23395175; DOI=10.1016/j.cmet.2012.12.017;
RA Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K.,
RA Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.;
RT "Glucose sensor O-GlcNAcylation coordinates with phosphorylation to
RT regulate circadian clock.";
RL Cell Metab. 17:291-302(2013).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=23395176; DOI=10.1016/j.cmet.2012.12.015;
RA Li M.D., Ruan H.B., Hughes M.E., Lee J.S., Singh J.P., Jones S.P.,
RA Nitabach M.N., Yang X.;
RT "O-GlcNAc signaling entrains the circadian clock by inhibiting BMAL1/CLOCK
RT ubiquitination.";
RL Cell Metab. 17:303-310(2013).
RN [13]
RP INTERACTION WITH TET1 AND TET2.
RX PubMed=23352454; DOI=10.1016/j.molcel.2012.12.019;
RA Vella P., Scelfo A., Jammula S., Chiacchiera F., Williams K., Cuomo A.,
RA Roberto A., Christensen J., Bonaldi T., Helin K., Pasini D.;
RT "Tet proteins connect the O-linked N-acetylglucosamine transferase Ogt to
RT chromatin in embryonic stem cells.";
RL Mol. Cell 49:645-656(2013).
RN [14]
RP IDENTIFICATION IN A COMPLEX WITH SIN3A; SINHCAF; HDAC1; RBBP4; SAP30 AND
RP TET1, AND INTERACTION WITH SINHCAF.
RX PubMed=28554894; DOI=10.15252/embj.201696307;
RA Streubel G., Fitzpatrick D.J., Oliviero G., Scelfo A., Moran B., Das S.,
RA Munawar N., Watson A., Wynne K., Negri G.L., Dillon E.T., Jammula S.,
RA Hokamp K., O'Connor D.P., Pasini D., Cagney G., Bracken A.P.;
RT "Fam60a defines a variant Sin3a-Hdac complex in embryonic stem cells
RT required for self-renewal.";
RL EMBO J. 36:2216-2232(2017).
RN [15]
RP FUNCTION, INTERACTION WITH HOXA1, PATHWAY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 2-MET--LEU-473; 474-GLN--ALA-1046; 504-SER--ALA-1046 AND
RP 991-LYS--LYS-1046.
RX PubMed=29465778; DOI=10.1002/1873-3468.13015;
RA Draime A., Bridoux L., Belpaire M., Pringels T., Degand H., Morsomme P.,
RA Rezsohazy R.;
RT "The O-GlcNAc transferase OGT interacts with and post-translationally
RT modifies the transcription factor HOXA1.";
RL FEBS Lett. 592:1185-1201(2018).
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:29465778). Glycosylates a large
CC and diverse number of proteins including histone H2B, AKT1, ATG4B,
CC EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular
CC processes via cross-talk between glycosylation and phosphorylation or
CC by affecting proteolytic processing. Probably by glycosylating
CC KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination (By
CC similarity).Involved in insulin resistance in muscle and adipocyte
CC cells via glycosylating insulin signaling components and inhibiting the
CC 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and
CC attenuating insulin signaling (By similarity). Involved in glycolysis
CC regulation by mediating glycosylation of 6-phosphofructokinase PFKL,
CC inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex
CC that is required for the regulation of the transcriptional activity of
CC RRM1. Plays a key role in chromatin structure by mediating O-
CC 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). As part of the NSL complex indirectly
CC involved in acetylation of nucleosomal histone H4 on several lysine
CC residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability,
CC and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex
CC (By similarity). Regulates circadian oscillation of the clock genes and
CC glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1
CC and CLOCK through O-glycosylation, which prevents their ubiquitination
CC and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated
CC transcription of genes in the negative loop of the circadian clock such
CC as PER1/2 and CRY1/2 (PubMed:23337503, PubMed:23395176). O-glycosylates
CC HCFC1 and regulates its proteolytic processing and transcriptional
CC activity (By similarity). Regulates mitochondrial motility in neurons
CC by mediating glycosylation of TRAK1 (By similarity). Glycosylates HOXA1
CC (PubMed:29465778). O-glycosylates FNIP1 (By similarity). Promotes
CC autophagy by mediating O-glycosylation of ATG4B (By similarity).
CC {ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:P56558,
CC ECO:0000269|PubMed:23337503, ECO:0000269|PubMed:23395176,
CC ECO:0000269|PubMed:29465778}.
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:0000250|UniProtKB:O15294};
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:0000250|UniProtKB:O15294};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:29465778}.
CC -!- SUBUNIT: Homotrimer, oligomerizes via TPR repeats 6 and 7.
CC 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. Component of the NSL complex at least
CC composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT,
CC WDR5 and HCFC1. Interacts directly with HCFC1; the interaction O-
CC glycosylates HCFC1, regulates its proteolytic processing and
CC transcriptional activity and, in turn, stabilizes OGT in the nucleus.
CC Interacts (via TPRs 1-6) with SIN3A; the interaction mediates
CC transcriptional repression in parallel with histone deacetylase (By
CC similarity). Interacts (via TPR 5-6) with TET1, TET2 and TET3
CC (PubMed:23352454). Interacts (via TPR repeats 6 and 7) with ATXN10
CC (PubMed:16182253). Interacts with histone H2B (By similarity).
CC Interacts with ARNTL/BMAL1 (PubMed:23337503). Found in a complex
CC composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1
CC (PubMed:28554894). Interacts with SINHCAF (PubMed:28554894). Component
CC of a complex composed of KMT2E/MLL5, OGT and USP7; the complex
CC stabilizes KMT2E/MLL5, preventing KMT2E/MLL5 ubiquitination and
CC proteosomal-mediated degradation. Interacts (via TRP repeats) with
CC KMT2E/MLL5 (via N-terminus). Interacts with USP7 (By similarity).
CC Interacts with TRAK1; this interaction is not required for
CC glycosylation of TRAK1 by this protein. Found in a complex with KIF5B,
CC RHOT1, RHOT2 and TRAK1 (By similarity). Interacts (via TPR repeats
CC domain) with HOXA1; the interaction takes place mainly in the nucleus
CC (PubMed:29465778). Interacts with NSD2 (PubMed:19483677).
CC {ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:P56558,
CC ECO:0000269|PubMed:16182253, ECO:0000269|PubMed:19483677,
CC ECO:0000269|PubMed:23337503, ECO:0000269|PubMed:23352454,
CC ECO:0000269|PubMed:28554894, ECO:0000269|PubMed:29465778}.
CC -!- INTERACTION:
CC Q8CGY8; Q4JK59: Tet2; NbExp=2; IntAct=EBI-928496, EBI-4291768;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15294}. Nucleus
CC {ECO:0000269|PubMed:29465778}. Cell membrane
CC {ECO:0000250|UniProtKB:O15294}. 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. After insulin induction,
CC translocated from the nucleus to the cell membrane via
CC phosphatidylinositide binding. Colocalizes with AKT1 at the plasma
CC membrane (By similarity). TRAK1 recruits this protein to mitochondria.
CC In the absence of TRAK1, localizes in cytosol and nucleus (By
CC similarity). {ECO:0000250|UniProtKB:O15294,
CC ECO:0000250|UniProtKB:P56558}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CGY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CGY8-2; Sequence=VSP_024844;
CC -!- INDUCTION: Expression in the liver oscillates in a circadian manner.
CC {ECO:0000269|PubMed:23395176}.
CC -!- DOMAIN: The TPR repeat domain is required for substrate binding and
CC oligomerization. {ECO:0000250|UniProtKB:O15294}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively
CC regulates its activity. {ECO:0000269|PubMed:23395175}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000305}.
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DR EMBL; AF539527; AAO17363.1; -; Genomic_DNA.
DR EMBL; AF363030; AAK39123.1; -; mRNA.
DR EMBL; AL805980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL806534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057319; AAH57319.1; -; mRNA.
DR EMBL; AK047095; BAC32961.1; -; mRNA.
DR CCDS; CCDS30318.1; -. [Q8CGY8-1]
DR CCDS; CCDS72415.1; -. [Q8CGY8-2]
DR RefSeq; NP_001277464.1; NM_001290535.1. [Q8CGY8-2]
DR RefSeq; NP_631883.2; NM_139144.4. [Q8CGY8-1]
DR RefSeq; XP_006527799.1; XM_006527736.3. [Q8CGY8-1]
DR RefSeq; XP_011245805.1; XM_011247503.2. [Q8CGY8-2]
DR AlphaFoldDB; Q8CGY8; -.
DR SMR; Q8CGY8; -.
DR BioGRID; 223870; 29.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DR DIP; DIP-35700N; -.
DR IntAct; Q8CGY8; 8.
DR STRING; 10090.ENSMUSP00000045409; -.
DR CAZy; GT41; Glycosyltransferase Family 41.
DR GlyGen; Q8CGY8; 2 sites.
DR iPTMnet; Q8CGY8; -.
DR PhosphoSitePlus; Q8CGY8; -.
DR EPD; Q8CGY8; -.
DR MaxQB; Q8CGY8; -.
DR PaxDb; Q8CGY8; -.
DR PeptideAtlas; Q8CGY8; -.
DR PRIDE; Q8CGY8; -.
DR ProteomicsDB; 293497; -. [Q8CGY8-1]
DR ProteomicsDB; 293498; -. [Q8CGY8-2]
DR Antibodypedia; 27791; 462 antibodies from 45 providers.
DR DNASU; 108155; -.
DR Ensembl; ENSMUST00000044475; ENSMUSP00000045409; ENSMUSG00000034160. [Q8CGY8-1]
DR Ensembl; ENSMUST00000119299; ENSMUSP00000113454; ENSMUSG00000034160. [Q8CGY8-2]
DR GeneID; 108155; -.
DR KEGG; mmu:108155; -.
DR UCSC; uc009tyc.3; mouse. [Q8CGY8-1]
DR UCSC; uc057ask.1; mouse. [Q8CGY8-2]
DR CTD; 8473; -.
DR MGI; MGI:1339639; Ogt.
DR VEuPathDB; HostDB:ENSMUSG00000034160; -.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG4626; Eukaryota.
DR GeneTree; ENSGT00940000155085; -.
DR HOGENOM; CLU_001721_1_0_1; -.
DR InParanoid; Q8CGY8; -.
DR OMA; HAYSEKL; -.
DR OrthoDB; 142546at2759; -.
DR PhylomeDB; Q8CGY8; -.
DR TreeFam; TF105785; -.
DR BRENDA; 2.4.1.255; 3474.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-5675482; Regulation of necroptotic cell death.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 108155; 28 hits in 78 CRISPR screens.
DR ChiTaRS; Ogt; mouse.
DR PRO; PR:Q8CGY8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8CGY8; protein.
DR Bgee; ENSMUSG00000034160; Expressed in metanephric cortical collecting duct and 270 other tissues.
DR Genevisible; Q8CGY8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0044545; C:NSL complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0017122; C:protein N-acetylglucosaminyltransferase complex; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0042588; C:zymogen granule; ISO:MGI.
DR GO; GO:0003824; F:catalytic activity; ISS:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR GO; GO:0008080; F:N-acetyltransferase activity; TAS:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006041; P:glucosamine metabolic process; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:ARUK-UCL.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:MGI.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
DR GO; GO:0000423; P:mitophagy; IMP:ARUK-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1900038; P:negative regulation of cellular response to hypoxia; ISO:MGI.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA: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; ISS:UniProtKB.
DR GO; GO:0045793; P:positive regulation of cell size; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IDA:ComplexPortal.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
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; 3.
DR PROSITE; PS50005; TPR; 12.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Biological rhythms; Cell membrane;
KW Cell projection; Chromatin regulator; Cytoplasm; Direct protein sequencing;
KW Glycoprotein; Glycosyltransferase; Lipid-binding; Membrane; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT CHAIN 2..1046
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase 110 kDa subunit"
FT /id="PRO_0000285216"
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:0000250|UniProtKB:O15294"
FT BINDING 849
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 852
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 906..908
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 911..914
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 930..932
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT BINDING 935
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O15294"
FT MOD_RES 3
FT /note="Phosphoserine; by GSK3-beta; alternate"
FT /evidence="ECO:0000269|PubMed:23395175"
FT MOD_RES 4
FT /note="Phosphoserine; by GSK3-beta; alternate"
FT /evidence="ECO:0000269|PubMed:23395175"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0000269|PubMed:23395175"
FT CARBOHYD 4
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000269|PubMed:23395175"
FT VAR_SEQ 13..22
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_024844"
FT MUTAGEN 2..473
FT /note="Missing: Loss of interaction with HOXA1. Loss of
FT glycosylation of HOXA1."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 474..1046
FT /note="Missing: Interacts with HOXA1. Interaction is
FT localized to the nucleus."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 504..1046
FT /note="Missing: Interacts with HOXA1. Interaction is
FT localized to the nucleus."
FT /evidence="ECO:0000269|PubMed:29465778"
FT MUTAGEN 991..1046
FT /note="Missing: Impaired interaction with HOXA1. Loss of
FT glycosylation of HOXA1."
FT /evidence="ECO:0000269|PubMed:29465778"
FT CONFLICT 57
FT /note="V -> A (in Ref. 1; AAO17363)"
FT /evidence="ECO:0000305"
FT CONFLICT 992
FT /note="K -> R (in Ref. 2; AAK39123)"
FT /evidence="ECO:0000305"
SQ 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
