ID OGT1_RAT Reviewed; 1036 AA. AC P56558; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 1. DT 02-SEP-2026, entry version 182. DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; DE EC=2.4.1.255 {ECO:0000269|PubMed:10542233, ECO:0000269|PubMed:24995978}; 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, RP PHOSPHORYLATION AT TYR-979, GLYCOSYLATION, SUBCELLULAR LOCATION, AND RP PROBABLE PROCESSING. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX PubMed=9083067; DOI=10.1074/jbc.272.14.9308; RA Kreppel L.K., Blomberg M.A., Hart G.W.; RT "Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and RT characterization of a unique O-GlcNAc transferase with multiple RT tetratricopeptide repeats."; RL J. Biol. Chem. 272:9308-9315(1997). RN [2] RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBCELLULAR LOCATION. RC TISSUE=Liver; RX PubMed=1533623; DOI=10.1016/s0021-9258(19)50380-5; RA Haltiwanger R.S., Blomberg M.A., Hart G.W.; RT "Glycosylation of nuclear and cytoplasmic proteins. Purification and RT characterization of a uridine diphospho-N-acetylglucosamine:polypeptide RT beta-N-acetylglucosaminyltransferase."; RL J. Biol. Chem. 267:9005-9013(1992). RN [3] RP TISSUE SPECIFICITY. RX PubMed=10580430; DOI=10.2337/diabetes.48.12.2407; RA Akimoto Y., Kreppel L.K., Hirano H., Hart G.W.; RT "Localization of the O-linked N-acetylglucosamine transferase in rat RT pancreas."; RL Diabetes 48:2407-2413(1999). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF 2-MET--ARG-274 RP AND 2-MET--ALA-173. RX PubMed=10542233; DOI=10.1074/jbc.274.45.32015; RA Kreppel L.K., Hart G.W.; RT "Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the RT tetratricopeptide repeats."; RL J. Biol. Chem. 274:32015-32022(1999). RN [5] RP SUBCELLULAR LOCATION, INTERACTION WITH ATXN10, SUBUNIT, TISSUE SPECIFICITY, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16714295; DOI=10.1074/jbc.m601563200; RA Maerz P., Stetefeld J., Bendfeldt K., Nitsch C., Reinstein J., RA Shoeman R.L., Dimitriades-Schmutz B., Schwager M., Leiser D., Ozcan S., RA Otten U., Ozbek S.; RT "Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in RT the brain."; RL J. Biol. Chem. 281:20263-20270(2006). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL-BINDING, AND RP MUTAGENESIS OF 981-LYS-LYS-982; ARG-984; LYS-986; LYS-989; ARG-991 AND RP LYS-1000. RX PubMed=18288188; DOI=10.1038/nature06668; RA Yang X., Ongusaha P.P., Miles P.D., Havstad J.C., Zhang F., So W.V., RA Kudlow J.E., Michell R.H., Olefsky J.M., Field S.J., Evans R.M.; RT "Phosphoinositide signalling links O-GlcNAc transferase to insulin RT resistance."; RL Nature 451:964-969(2008). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, PATHWAY, INTERACTION WITH KIF5B; RP RHOT1; RHOT2 AND TRAK1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 2-MET--MET-129; 2-MET--HIS-248 AND HIS-498. 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). 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:10542233, PubMed:24995978). CC Glycosylates a large and diverse number of proteins including histone CC H2B, AKT1, AMPK, ATG4B, CAPRIN1, EZH2, FNIP1, GSDMD, KRT7, LMNA, LMNB1, CC LMNB2, RPTOR, HOXA1, PFKL, KMT2E/MLL5, MAPT/TAU, TET2, RBL2, RET, NOD2 CC and HCFC1 (PubMed:10542233). Can regulate their cellular processes via CC cross-talk between glycosylation and phosphorylation or by affecting CC proteolytic processing (By similarity). Involved in insulin resistance CC in muscle and adipocyte cells via glycosylating insulin signaling CC components and inhibiting the 'Thr-308' phosphorylation of AKT1, CC enhancing IRS1 phosphorylation and attenuating insulin signaling CC (PubMed:18288188). Involved in glycolysis regulation by mediating CC glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity CC (By similarity). 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) (By similarity). As part of the NSL CC complex indirectly involved in acetylation of nucleosomal histone H4 on CC several lysine residues (By similarity). O-GlcNAcylation of 'Ser-75' of CC EZH2 increases its stability, and facilitating the formation of CC H3K27me3 by the PRC2/EED-EZH2 complex (By similarity). Stabilizes CC KMT2E/MLL5 by mediating its glycosylation, thereby preventing CC KMT2E/MLL5 ubiquitination (By similarity). Regulates circadian CC oscillation of the clock genes and glucose homeostasis in the liver (By CC similarity). Stabilizes clock proteins BMAL1 and CLOCK through O- CC glycosylation, which prevents their ubiquitination and subsequent CC degradation (By similarity). Promotes the CLOCK-BMAL1-mediated CC transcription of genes in the negative loop of the circadian clock such CC as PER1/2 and CRY1/2 (By similarity). O-glycosylates HCFC1 and CC regulates its proteolytic processing and transcriptional activity (By CC similarity). Component of a THAP1/THAP3-HCFC1-OGT complex that is CC required for the regulation of the transcriptional activity of RRM1 (By CC similarity). Regulates mitochondrial motility in neurons by mediating CC glycosylation of TRAK1 (PubMed:24995978). Promotes autophagy by CC mediating O-glycosylation of ATG4B (By similarity). Acts as a regulator CC of mTORC1 signaling by mediating O-glycosylation of RPTOR and FNIP1: O- CC GlcNAcylation of RPTOR in response to glucose sufficiency promotes CC activation of the mTORC1 complex (By similarity). CC {ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:Q8CGY8, CC ECO:0000269|PubMed:10542233, ECO:0000269|PubMed:1533623, CC ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:24995978}. 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] + UDP + H(+); 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:10542233, ECO:0000269|PubMed:24995978}; 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] + UDP + H(+); 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:10542233, ECO:0000269|PubMed:24995978}; CC -!- ACTIVITY REGULATION: Inhibited by UDP, UTP and UDP-GlcNAc; 50 mM NaCl CC or KCl inhibit activity about 70%. {ECO:0000269|PubMed:1533623}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.0. {ECO:0000269|PubMed:1533623}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:24995978}. CC -!- SUBUNIT: Monomer; may exist in different oligomerization states in CC cells (By similarity). Homotrimer, oligomerizes via TPR repeats 6 and 7 CC (By similarity). Trimerization is not necessary for activity in vitro, CC however it increases affinity for UDP-GlcNAc (PubMed:10542233). A CC heterotrimer consisting of two 110 kDa subunits and one highly related CC 78 kDa subunit is isolated from liver (PubMed:1533623). Component of a CC THAP1/THAP3-HCFC1-OGT complex (By similarity). Component of the NSL CC complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, CC PHF20, OGT1/OGT, WDR5 and HCFC1 (By similarity). Found in a complex CC with KIF5B, RHOT1, RHOT2 and TRAK1 (PubMed:24995978). Found in a CC complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT CC and TET1 (By similarity). Component of a complex composed of CC KMT2E/MLL5, OGT and USP7; the complex stabilizes KMT2E/MLL5, preventing CC KMT2E/MLL5 ubiquitination and proteasomal-mediated degradation (By CC similarity). Interacts (via TPRs 1-6) with SIN3A; the interaction CC mediates transcriptional repression in parallel with histone CC deacetylase (By similarity). Interacts (via TPR 5-6) with TET1, TET2 CC and TET3 (By similarity). Interacts (via TPR repeats 6 and 7) with CC ATXN10 (PubMed:16714295). Interacts with NSD2 (By similarity). CC Interacts with PROSER1; this interaction mediates TET2 O-GlcNAcylation CC and stability by promoting the interaction between OGT and TET2 (By CC similarity). {ECO:0000250|UniProtKB:O15294, CC ECO:0000250|UniProtKB:Q8CGY8, ECO:0000269|PubMed:10542233, CC ECO:0000269|PubMed:1533623, ECO:0000269|PubMed:16714295, CC ECO:0000269|PubMed:24995978}. CC -!- INTERACTION: CC P56558; Q9WVH3: Foxo4; Xeno; NbExp=2; IntAct=EBI-7614183, EBI-4567305; CC P56558; Q9WU00: Nrf1; Xeno; NbExp=2; IntAct=EBI-7614183, EBI-11291138; CC P56558; Q9UPV9: TRAK1; Xeno; NbExp=6; IntAct=EBI-7614183, EBI-1105048; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1533623, CC ECO:0000269|PubMed:16714295, ECO:0000269|PubMed:24995978, CC ECO:0000269|PubMed:9083067}. Nucleus {ECO:0000269|PubMed:18288188, CC ECO:0000269|PubMed:24995978, ECO:0000269|PubMed:9083067}. Cell membrane CC {ECO:0000269|PubMed:18288188}. Mitochondrion membrane CC {ECO:0000269|PubMed:24995978}. Cell projection CC {ECO:0000269|PubMed:24995978}. Note=Mostly in the nucleus CC (PubMed:9083067). After insulin induction, translocated from the CC nucleus to the cell membrane via phosphatidylinositide binding. CC Colocalizes with AKT1 at the plasma membrane (PubMed:18288188). TRAK1 CC recruits this protein to mitochondria (PubMed:24995978). In the absence CC of TRAK1, localizes in cytosol and nucleus (PubMed:24995978). CC Translocates into the nucleus via association with importin KPNA1 (By CC similarity). {ECO:0000250|UniProtKB:O15294, CC ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:24995978, CC ECO:0000305|PubMed:9083067}. CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, thymus, muscle, CC lung, spleen, uterus and ovary; in the kidney only an immunologically- CC related 78 kDa band is present, which is also present in liver and CC muscle (PubMed:9083067). In the pancreas, expressed in both exocrine CC acinar cells and in endocrine cells of the islets of Langerhans. CC {ECO:0000269|PubMed:10580430, ECO:0000269|PubMed:16714295, CC ECO:0000269|PubMed:9083067}. CC -!- DOMAIN: The TPR repeat domain is required for substrate binding and CC oligomerization. {ECO:0000250|UniProtKB:O15294, CC ECO:0000269|PubMed:24995978}. CC -!- PTM: Several different immunologically-related forms of this protein CC are found in different tissues (with apparent molecular weights of 110, CC 80 and 78 kDa); they are probably the result of alternative splicing CC and/or proteolysis. {ECO:0000269|PubMed:9083067}. CC -!- PTM: O-glycosylated; contains O-GlcNAc. Both p110 and p78 forms are O- CC glycosylated. {ECO:0000269|PubMed:9083067}. CC -!- PTM: Ubiquitinated by the SCF(FBXO31) complex, leading to its CC proteasomal degradation. {ECO:0000250|UniProtKB:O15294}. CC -!- PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively CC regulates its activity (By similarity). Phosphorylation at Thr-444 by CC AMPK promotes nuclear localization (By similarity). CC {ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:Q8CGY8}. CC -!- PTM: Glycosylated via autocatalysis; O-GlcNAcylation at Ser-389 CC promotes nuclear localization. {ECO:0000250|UniProtKB:O15294}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc CC transferase subfamily. {ECO:0000305}. 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; U76557; AAC53121.1; -; mRNA. DR PIR; T31673; T31673. DR RefSeq; NP_058803.2; NM_017107.3. DR AlphaFoldDB; P56558; -. DR SMR; P56558; -. DR BioGRID; 247798; 6. DR CORUM; P56558; -. DR FunCoup; P56558; 3480. DR IntAct; P56558; 5. DR MINT; P56558; -. DR STRING; 10116.ENSRNOP00000072791; -. DR CAZy; GT41; Glycosyltransferase Family 41. DR GlyCosmos; P56558; 2 sites, No reported glycans. DR GlyGen; P56558; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; P56558; -. DR PhosphoSitePlus; P56558; -. DR jPOST; P56558; -. DR PaxDb; 10116-ENSRNOP00000072791; -. DR GeneID; 26295; -. DR KEGG; rno:26295; -. DR UCSC; RGD:62060; rat. DR AGR; RGD:62060; -. DR CTD; 8473; -. DR RGD; 62060; Ogt. DR eggNOG; KOG1124; Eukaryota. DR eggNOG; KOG4626; Eukaryota. DR InParanoid; P56558; -. DR OrthoDB; 9991317at2759; -. DR PhylomeDB; P56558; -. DR BRENDA; 2.4.1.255; 5301. DR Reactome; R-RNO-3214847; HATs acetylate histones. DR Reactome; R-RNO-5675482; Regulation of necroptotic cell death. DR Reactome; R-RNO-5689603; UCH proteinases. DR Reactome; R-RNO-9772755; Formation of WDR5-containing histone-modifying complexes. DR UniPathway; UPA00378; -. DR PRO; PR:P56558; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0150048; C:cerebellar granule cell to Purkinje cell synapse; IDA:SynGO. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0000791; C:euchromatin; IDA:RGD. DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0031966; C:mitochondrial membrane; EXP:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0005654; C:nucleoplasm; ISO:RGD. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO. DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO. DR GO; GO:0017122; C:protein N-acetylglucosaminyltransferase complex; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:0045202; C:synapse; ISO:RGD. DR GO; GO:0042588; C:zymogen granule; IDA:RGD. DR GO; GO:0031490; F:chromatin DNA binding; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0042277; F:peptide binding; IDA:RGD. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD. DR GO; GO:0097363; F:protein O-acetylglucosaminyltransferase activity; IDA:RGD. DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD. DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB. DR GO; GO:0071333; P:cellular response to glucose stimulus; IMP:RGD. DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:RGD. DR GO; GO:0097237; P:cellular response to toxic substance; IEP:RGD. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0006041; P:D-glucosamine metabolic process; IDA:RGD. DR GO; GO:0030900; P:forebrain development; IEP:RGD. DR GO; GO:0030097; P:hemopoiesis; ISO:RGD. DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:RGD. DR GO; GO:0000423; P:mitophagy; ISO:RGD. DR GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IMP:RGD. DR GO; GO:0160076; P:negative regulation of non-canonical inflammasome complex assembly; ISS:UniProtKB. DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:RGD. DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:RGD. DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD. DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; IMP:RGD. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB. DR GO; GO:0045793; P:positive regulation of cell size; IMP:RGD. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:RGD. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD. DR GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB. DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:RGD. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0000432; P:positive regulation of transcription from RNA polymerase II promoter by glucose; ISO:RGD. DR GO; GO:0045727; P:positive regulation of translation; ISO:RGD. DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:RGD. DR GO; GO:0016485; P:protein processing; ISS:UniProtKB. DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB. DR GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB. DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISO:RGD. DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:RGD. DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISO:RGD. DR GO; GO:0051963; P:regulation of synapse assembly; ISO:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0032868; P:response to insulin; ISO:RGD. DR FunFam; 1.25.40.10:FF:000013; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; 1. DR FunFam; 1.25.40.10:FF:000019; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; 1. DR FunFam; 3.30.720.150:FF:000001; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; 1. DR FunFam; 3.40.50.11380:FF:000001; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; 1. DR FunFam; 3.40.50.2000:FF:000012; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; 1. DR Gene3D; 3.30.720.150; -; 1. DR Gene3D; 3.40.50.11380; -; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2. DR InterPro; IPR037919; OGT. DR InterPro; IPR029489; OGT/SEC/SPY_C. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_rpt. DR PANTHER; PTHR44366; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1. DR PANTHER; PTHR44366:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1. DR Pfam; PF13844; Glyco_transf_41; 1. DR Pfam; PF00515; TPR_1; 2. DR Pfam; PF13414; TPR_11; 3. DR Pfam; PF13424; TPR_12; 1. DR Pfam; PF13181; TPR_8; 2. DR SMART; SM00028; TPR; 12. DR SUPFAM; SSF48452; TPR-like; 3. DR PROSITE; PS50005; TPR; 12. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW Acetylation; Biological rhythms; Cell membrane; Cell projection; KW Chromatin regulator; Cytoplasm; Direct protein sequencing; Glycoprotein; KW Glycosyltransferase; Lipid-binding; Membrane; Mitochondrion; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transferase; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:O15294" FT CHAIN 2..1036 FT /note="UDP-N-acetylglucosamine--peptide N- FT acetylglucosaminyltransferase 110 kDa subunit" FT /id="PRO_0000191774" FT REPEAT 11..44 FT /note="TPR 1" FT REPEAT 79..112 FT /note="TPR 2" FT REPEAT 113..146 FT /note="TPR 3" FT REPEAT 147..180 FT /note="TPR 4" FT REPEAT 181..214 FT /note="TPR 5" FT REPEAT 215..248 FT /note="TPR 6" FT REPEAT 249..282 FT /note="TPR 7" FT REPEAT 283..316 FT /note="TPR 8" FT REPEAT 317..350 FT /note="TPR 9" FT REPEAT 351..384 FT /note="TPR 10" FT REPEAT 385..418 FT /note="TPR 11" FT REPEAT 419..452 FT /note="TPR 12" FT REPEAT 453..463 FT /note="TPR 13; truncated" FT REGION 981..1000 FT /note="Required for phosphatidylinositol 3,4,5-triphosphate FT binding" FT /evidence="ECO:0000269|PubMed:18288188" FT MOTIF 454..456 FT /note="DFP motif" FT /evidence="ECO:0000250|UniProtKB:O15294" FT MOTIF 478..493 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT ACT_SITE 498 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:24995978" FT BINDING 839 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:O15294" FT BINDING 842 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:O15294" FT BINDING 896..898 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:O15294" FT BINDING 901..904 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:O15294" FT BINDING 920..922 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:O15294" FT BINDING 925 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:0000250|UniProtKB:Q8CGY8" FT MOD_RES 4 FT /note="Phosphoserine; by GSK3-beta; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8CGY8" FT MOD_RES 444 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O15294" FT MOD_RES 979 FT /note="Phosphotyrosine" FT /evidence="ECO:0000305|PubMed:9083067" FT CARBOHYD 3 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8CGY8" FT CARBOHYD 4 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8CGY8" FT CARBOHYD 389 FT /note="O-linked (GlcNAc) serine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:O15294" FT MUTAGEN 2..274 FT /note="Missing: Wild-type O-GlcNAc transferase activity, FT does not form trimers." FT /evidence="ECO:0000269|PubMed:10542233" FT MUTAGEN 2..248 FT /note="Missing: Decreased TRAK1 O-glycosylation by this FT protein." FT /evidence="ECO:0000269|PubMed:24995978" FT MUTAGEN 2..173 FT /note="Missing: Wild-type O-GlcNAc transferase activity, FT forms trimers." FT /evidence="ECO:0000269|PubMed:10542233" FT MUTAGEN 2..129 FT /note="Missing: Decreased ability to reduce neuronal FT mitochondrial motility in both anterograde and retrograde FT directions." FT /evidence="ECO:0000269|PubMed:24995978" FT MUTAGEN 498 FT /note="H->N: Loss of glycosylation activity. Loss of FT ability to reduce mitochondrial motility." FT /evidence="ECO:0000269|PubMed:24995978" FT MUTAGEN 981..982 FT /note="KK->AA: Abolishes phosphatidylinisitol binding, no FT translocation to the cell membrane, and no effect on FT phosphorylation of AKT1 nor IRS1." FT /evidence="ECO:0000269|PubMed:18288188" FT MUTAGEN 984 FT /note="R->A: No effect on phosphatidylinisitol binding." FT /evidence="ECO:0000269|PubMed:18288188" FT MUTAGEN 986 FT /note="K->A: Reduced phosphatidylinisitol binding." FT /evidence="ECO:0000269|PubMed:18288188" FT MUTAGEN 989 FT /note="K->A: Reduced phosphatidylinisitol binding." FT /evidence="ECO:0000269|PubMed:18288188" FT MUTAGEN 991 FT /note="R->A: No effect on phosphatidylinisitol binding." FT /evidence="ECO:0000269|PubMed:18288188" FT MUTAGEN 1000 FT /note="K->A: No effect on phosphatidylinisitol binding." FT /evidence="ECO:0000269|PubMed:18288188" SQ SEQUENCE 1036 AA; 115606 MW; 3F057CABDD019BD6 CRC64; MASSVGNVAD STGLAELAHR 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 GGDNADTTNT ALNMPVIPMN TIAEAVIEMI NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL YKIDPSTLQM GANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL TCLGCLELIA KSRQEYEDIA VKLGTDLEYL KKIRGKVWKQ RISSPLFNTK QYTMELERLY LQMWEHYAAG NKPDHMIKPV EVTESA //