Ogt
entrez
26295
canonical
uniprot
P56558
canonical
ensembl
ENSRNOG00000003359
resolver
ensp
ENSRNOP00000004692
resolver
ensp
ENSRNOP00000086509
resolver
enst
ENSRNOT00000004692
resolver
genesymbol
Ogt
resolver
uniprot
G3V6F4
resolver
uniprot_entry
G3V6F4_RAT
resolver
uniprot_entry
OGT1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by UDP, UTP and UDP-GlcNAc; 50 mM NaCl or KCl inhibit activity about 70%. {ECO:0000269|PubMed:1533623}.
uniprot
proteins
amino_acid_sequence
MASSVGNVADSTGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVAEQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADTTNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMGANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKSRQEYEDIAVKLGTDLEYLKKIRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA
uniprot
proteins
ec_number
2.4.1.255
uniprot
proteins
function
FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc) (PubMed:10542233, PubMed:24995978). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, AMPK, ATG4B, CAPRIN1, EZH2, FNIP1, GSDMD, KRT7, LMNA, LMNB1, LMNB2, RPTOR, HOXA1, PFKL, KMT2E/MLL5, MAPT/TAU, TET2, RBL2, RET, NOD2 and HCFC1 (PubMed:10542233). Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing (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 (PubMed:18288188). Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity (By similarity). 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) (By similarity). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues (By similarity). O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (By similarity). Stabilizes KMT2E/MLL5 by mediating its glycosylation, thereby preventing KMT2E/MLL5 ubiquitination (By similarity). Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver (By similarity). Stabilizes clock proteins BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation (By similarity). Promotes the CLOCK-BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2 (By similarity). O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity (By similarity). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (By similarity). Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (PubMed:24995978). Promotes autophagy by mediating O-glycosylation of ATG4B (By similarity). Acts as a regulator of mTORC1 signaling by mediating O-glycosylation of RPTOR and FNIP1: O-GlcNAcylation of RPTOR in response to glucose sufficiency promotes activation of the mTORC1 complex (By similarity). {ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:Q8CGY8, ECO:0000269|PubMed:10542233, ECO:0000269|PubMed:1533623, ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:24995978}.
uniprot
proteins
mass_dalton
115606
uniprot
proteins
mutagenesis
MUTAGEN 2..274; /note="Missing: Wild-type O-GlcNAc transferase activity, does not form trimers."; /evidence="ECO:0000269|PubMed:10542233"; MUTAGEN 2..248; /note="Missing: Decreased TRAK1 O-glycosylation by this protein."; /evidence="ECO:0000269|PubMed:24995978"; MUTAGEN 2..173; /note="Missing: Wild-type O-GlcNAc transferase activity, forms trimers."; /evidence="ECO:0000269|PubMed:10542233"; MUTAGEN 2..129; /note="Missing: Decreased ability to reduce neuronal mitochondrial motility in both anterograde and retrograde directions."; /evidence="ECO:0000269|PubMed:24995978"; MUTAGEN 498; /note="H->N: Loss of glycosylation activity. Loss of ability to reduce mitochondrial motility."; /evidence="ECO:0000269|PubMed:24995978"; MUTAGEN 981..982; /note="KK->AA: Abolishes phosphatidylinisitol binding, no translocation to the cell membrane, and no effect on phosphorylation of AKT1 nor IRS1."; /evidence="ECO:0000269|PubMed:18288188"; MUTAGEN 984; /note="R->A: No effect on phosphatidylinisitol binding."; /evidence="ECO:0000269|PubMed:18288188"; MUTAGEN 986; /note="K->A: Reduced phosphatidylinisitol binding."; /evidence="ECO:0000269|PubMed:18288188"; MUTAGEN 989; /note="K->A: Reduced phosphatidylinisitol binding."; /evidence="ECO:0000269|PubMed:18288188"; MUTAGEN 991; /note="R->A: No effect on phosphatidylinisitol binding."; /evidence="ECO:0000269|PubMed:18288188"; MUTAGEN 1000; /note="K->A: No effect on phosphatidylinisitol binding."; /evidence="ECO:0000269|PubMed:18288188
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:24995978}.
uniprot
proteins
post_translational_modification
PTM: Several different immunologically-related forms of this protein are found in different tissues (with apparent molecular weights of 110, 80 and 78 kDa); they are probably the result of alternative splicing and/or proteolysis. {ECO:0000269|PubMed:9083067}.; PTM: O-glycosylated; contains O-GlcNAc. Both p110 and p78 forms are O-glycosylated. {ECO:0000269|PubMed:9083067}.; PTM: Ubiquitinated by the SCF(FBXO31) complex, leading to its proteasomal degradation. {ECO:0000250|UniProtKB:O15294}.; PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity (By similarity). Phosphorylation at Thr-444 by AMPK promotes nuclear localization (By similarity). {ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:Q8CGY8}.; PTM: Glycosylated via autocatalysis; O-GlcNAcylation at Ser-389 promotes nuclear localization. {ECO:0000250|UniProtKB:O15294}.
uniprot
proteins
protein_family
Glycosyltransferase 41 family
uniprot
proteins
protein_family
O-GlcNAc transferase subfamily
uniprot
proteins
pubmed
10542233
uniprot
proteins
pubmed
10580430
uniprot
proteins
pubmed
1533623
uniprot
proteins
pubmed
16714295
uniprot
proteins
pubmed
18288188
uniprot
proteins
pubmed
24995978
uniprot
proteins
pubmed
9083067
uniprot
proteins
sequence_length
1036
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1533623, ECO:0000269|PubMed:16714295, ECO:0000269|PubMed:24995978, ECO:0000269|PubMed:9083067}. Nucleus {ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:24995978, ECO:0000269|PubMed:9083067}. Cell membrane {ECO:0000269|PubMed:18288188}. Mitochondrion membrane {ECO:0000269|PubMed:24995978}. Cell projection {ECO:0000269|PubMed:24995978}. Note=Mostly in the nucleus (PubMed:9083067). After insulin induction, translocated from the nucleus to the cell membrane via phosphatidylinositide binding. Colocalizes with AKT1 at the plasma membrane (PubMed:18288188). TRAK1 recruits this protein to mitochondria (PubMed:24995978). In the absence of TRAK1, localizes in cytosol and nucleus (PubMed:24995978). Translocates into the nucleus via association with importin KPNA1 (By similarity). {ECO:0000250|UniProtKB:O15294, ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:24995978, ECO:0000305|PubMed:9083067}.
uniprot
proteins