OGT 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). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination. 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. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. 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). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex. Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2. O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity. Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1. Glycosylates HOXA1. Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line. Belongs to the glycosyltransferase 41 family. O-GlcNAc transferase subfamily. Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver. 4 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: EC 2.4.1.255; Glycan Metabolism - O-glycan biosynthesis; Transferase
Chromosomal Location of Human Ortholog: X|X D
Cellular Component:  cell projection; cytoplasm; cytosol; euchromatin; histone acetyltransferase complex; membrane; mitochondrion; neuron projection; neuronal cell body; nucleoplasm; nucleus; plasma membrane; protein N-acetylglucosaminyltransferase complex; protein-containing complex; zymogen granule
Molecular Function:  catalytic activity; lipid binding; monosaccharide binding; N-acetyltransferase activity; peptide binding; phosphatidylinositol-3,4,5-trisphosphate binding; protein binding; protein domain specific binding; protein N-acetylglucosaminyltransferase activity; protein O-GlcNAc transferase activity; transcription factor binding; transferase activity; transferase activity, transferring glycosyl groups
Biological Process:  apoptotic process; cellular response to glucose stimulus; cellular response to lipopolysaccharide; chromatin organization; circadian regulation of gene expression; glucosamine metabolic process; histone H3-K4 trimethylation; histone H4-K16 acetylation; histone H4-K5 acetylation; histone H4-K8 acetylation; intracellular distribution of mitochondria; negative regulation of cell death; negative regulation of cellular response to hypoxia; negative regulation of peptidyl-serine phosphorylation; negative regulation of peptidyl-threonine phosphorylation; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; negative regulation of protein phosphorylation; negative regulation of protein targeting to membrane; negative regulation of protein ubiquitination; phosphatidylinositol-mediated signaling; positive regulation of cell size; positive regulation of cold-induced thermogenesis; positive regulation of gene expression; positive regulation of histone H3-K27 methylation; positive regulation of protein localization to nucleus; positive regulation of protein phosphorylation; positive regulation of proteolysis; positive regulation of reactive oxygen species biosynthetic process; positive regulation of transcription by RNA polymerase II; protein heterotrimerization; protein homotrimerization; protein O-linked glycosylation; protein processing; regulation of gluconeogenesis; regulation of glycolytic process; regulation of insulin receptor signaling pathway; regulation of Rac protein signal transduction; regulation of transcription by RNA polymerase II; response to insulin; rhythmic process
Reference #:  Q8CGY8 (UniProtKB)
Alt. Names/Synonyms: 1110038P24Rik; 4831420N21Rik; AI115525; O linked N-acetylglucosamine transferase like; O-GlcNAc transferase subunit p110; O-linked GlcNAc transferase; O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase); O-linked N-acetylglucosamine transferase 110 kDa subunit; Ogt; OGT1; Ogtl; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; UDP-N-acetylglucosaminyltransferase
Gene Symbols: Ogt
Molecular weight: 116,952 Da
Basal Isoelectric point: 6.22  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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OGT

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein