Ogt
entrez
108155
canonical
uniprot
Q8CGY8
canonical
ensembl
ENSMUSG00000034160
resolver
ensp
ENSMUSP00000045409
resolver
ensp
ENSMUSP00000113454
resolver
ensp
ENSMUSP00000298707
resolver
genesymbol
Ogt
resolver
uniprot
A2ALY1
resolver
uniprot
Q6PG10
resolver
uniprot
Q8BXH6
resolver
uniprot
Q91Y38
resolver
uniprot_entry
OGT1_MOUSE
resolver
uniprot_sec
A2ALY1
resolver
uniprot_sec
Q6PG10
resolver
uniprot_sec
Q8BXH6
resolver
uniprot_sec
Q91Y38
resolver
activity_regulation
ACTIVITY REGULATION: Subject to product inhibition by UDP. {ECO:0000250|UniProtKB:O15294}.
uniprot
proteins
amino_acid_sequence
MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVAEQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNPDSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKSRQEYEDIAVKLGTDLEYLKKIRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA
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:29465778). 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 (By similarity). 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 (By similarity). 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 (PubMed:23337503, PubMed:23395176). Stabilizes clock proteins BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation (PubMed:23337503, PubMed:23395176). Promotes the CLOCK-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). 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 (By similarity). 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:P56558, ECO:0000269|PubMed:23337503, ECO:0000269|PubMed:23395176, ECO:0000269|PubMed:29465778}.
uniprot
proteins
mass_dalton
116952
uniprot
proteins
mutagenesis
MUTAGEN 2..473; /note="Missing: Loss of interaction with HOXA1. Loss of glycosylation of HOXA1."; /evidence="ECO:0000269|PubMed:29465778"; MUTAGEN 474..1046; /note="Missing: Interacts with HOXA1. Interaction is localized to the nucleus."; /evidence="ECO:0000269|PubMed:29465778"; MUTAGEN 504..1046; /note="Missing: Interacts with HOXA1. Interaction is localized to the nucleus."; /evidence="ECO:0000269|PubMed:29465778"; MUTAGEN 991..1046; /note="Missing: Impaired interaction with HOXA1. Loss of glycosylation of HOXA1."; /evidence="ECO:0000269|PubMed:29465778
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:29465778}.
uniprot
proteins
post_translational_modification
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 (PubMed:23395175). Phosphorylation at Thr-454 by AMPK promotes nuclear localization (By similarity). {ECO:0000250|UniProtKB:O15294, ECO:0000269|PubMed:23395175}.; PTM: Glycosylated via autocatalysis; O-GlcNAcylation at Ser-399 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
12504895
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16182253
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19483677
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23337503
uniprot
proteins
pubmed
23352454
uniprot
proteins
pubmed
23395175
uniprot
proteins
pubmed
23395176
uniprot
proteins
pubmed
24563466
uniprot
proteins
pubmed
28554894
uniprot
proteins
pubmed
29465778
uniprot
proteins
sequence_length
1046
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24563466}. Nucleus {ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:29465778}. Cell membrane {ECO:0000250|UniProtKB:O15294}. Mitochondrion membrane {ECO:0000250|UniProtKB:P56558}. Cell projection {ECO:0000250|UniProtKB:P56558}. Note=Predominantly localizes to the nucleus. Translocates into the nucleus via association with importin KPNA1. {ECO:0000250|UniProtKB:O15294}.
uniprot
proteins