OGT1_RAT
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 03-AUG-2022, entry version 164.
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, PATHWAY, INTERACTION WITH KIF5B; RHOT1; RHOT2
RP AND TRAK1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 2-MET--MET-129;
RP 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:24995978, PubMed:10542233). Has 3
CC distinct KM values for UDP-GlcNAc; GlcNAc concentration modulates its
CC affinity for different substrates (PubMed:10542233). Glycosylates a
CC large and diverse number of proteins including histone H2B, AKT1,
CC ATG4B, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their
CC cellular processes via cross-talk between glycosylation and
CC phosphorylation or by affecting proteolytic processing. Probably by
CC glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its
CC ubiquitination (By similarity). Involved in insulin resistance in
CC 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 Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the
CC regulation of the transcriptional activity of RRM1. Plays a key role in
CC chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of
CC histone H2B: recruited to CpG-rich transcription start sites of active
CC genes via its interaction with TET proteins (TET1, TET2 or TET3). As
CC part of the NSL complex indirectly involved in acetylation of
CC nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of
CC 'Ser-75' of EZH2 increases its stability, and facilitating the
CC formation of H3K27me3 by the PRC2/EED-EZH2 complex. Regulates circadian
CC oscillation of the clock genes and glucose homeostasis in the liver.
CC Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-
CC glycosylation, which prevents their ubiquitination and subsequent
CC degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of
CC genes in the negative loop of the circadian clock such as PER1/2 and
CC CRY1/2. O-glycosylates HCFC1 and regulates its proteolytic processing
CC and transcriptional activity (By similarity). Regulates mitochondrial
CC motility in neurons by mediating glycosylation of TRAK1
CC (PubMed:24995978). Glycosylates HOXA1 (By similarity). O-glycosylates
CC FNIP1 (By similarity). Promotes autophagy by mediating O-glycosylation
CC of ATG4B (By similarity). {ECO:0000250|UniProtKB:O15294,
CC ECO:0000250|UniProtKB:Q8CGY8, ECO:0000269|PubMed:10542233,
CC ECO:0000269|PubMed:1533623, ECO:0000269|PubMed:18288188,
CC 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] + H(+) + UDP;
CC Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.255;
CC Evidence={ECO:0000269|PubMed: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] + H(+) + UDP;
CC Xref=Rhea:RHEA:48908, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90840; EC=2.4.1.255;
CC Evidence={ECO:0000269|PubMed: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: 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 (PubMed:10542233). A heterotrimer
CC consisting of two 110 kDa subunits and one highly related 78 kDa
CC subunit is isolated from liver (PubMed:1533623). 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.
CC Interacts (via TPR 5-6) with TET1, TET2 and TET3 (By similarity).
CC Interacts (via TPR repeats 6 and 7) with ATXN10 (PubMed:16714295).
CC Interacts with histone H2B (By similarity). Interacts with ARNTL/BMAL1.
CC Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30,
CC RBBP4, OGT and TET1. Interacts with SINHCAF (By similarity). 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 (via N-terminus). Interacts with USP7 (By similarity). Interacts
CC with TRAK1; this interaction is not required for glycosylation of TRAK1
CC by this protein. Found in a complex with KIF5B, RHOT1, RHOT2 and TRAK1
CC (PubMed:24995978). Interacts (via TPR repeats domain) with HOXA1; the
CC interaction takes place mainly in the nucleus (By similarity).
CC Interacts with NSD2 (By 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 (Probable).
CC Retained in the nucleus via interaction with HCFC1 (By similarity).
CC After insulin induction, translocated from the nucleus to the cell
CC membrane via phosphatidylinositide binding. Colocalizes with AKT1 at
CC the plasma membrane (PubMed:18288188). TRAK1 recruits this protein to
CC mitochondria. In the absence of TRAK1, localizes in cytosol and nucleus
CC (PubMed:24995978). {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, 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:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000305}.
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DR EMBL; U76557; AAC53121.1; -; mRNA.
DR PIR; T31673; T31673.
DR RefSeq; NP_058803.2; NM_017107.2.
DR AlphaFoldDB; P56558; -.
DR SMR; P56558; -.
DR BioGRID; 247798; 6.
DR IntAct; P56558; 5.
DR MINT; P56558; -.
DR STRING; 10116.ENSRNOP00000004692; -.
DR CAZy; GT41; Glycosyltransferase Family 41.
DR GlyGen; P56558; 2 sites.
DR iPTMnet; P56558; -.
DR PhosphoSitePlus; P56558; -.
DR jPOST; P56558; -.
DR PaxDb; P56558; -.
DR PRIDE; P56558; -.
DR GeneID; 26295; -.
DR KEGG; rno:26295; -.
DR UCSC; RGD:62060; rat.
DR CTD; 8473; -.
DR RGD; 62060; Ogt.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG4626; Eukaryota.
DR InParanoid; P56558; -.
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 UniPathway; UPA00378; -.
DR PRO; PR:P56558; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0000791; C:euchromatin; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0044545; C:NSL complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0017122; C:protein N-acetylglucosaminyltransferase complex; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; 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:0048029; F:monosaccharide binding; IDA: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:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:RGD.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; ISS:UniProtKB.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0006041; P:glucosamine metabolic process; IDA:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
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; IMP:RGD.
DR GO; GO:0000423; P:mitophagy; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IMP:RGD.
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:0048015; P:phosphatidylinositol-mediated signaling; 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:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO: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:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:RGD.
DR GO; GO:0016485; P:protein processing; ISS:UniProtKB.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; ISO:RGD.
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:0035020; P:regulation of Rac protein signal transduction; 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 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; 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 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 979
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:9083067"
FT CARBOHYD 3
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 4
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT 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
