SCUBA

OGT — O-linked N-acetylglucosamine (GlcNAc) transferase

OGT belongs to a gene co-expression module in 6 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

OGT's module in each cell type

Cell typeModuleShares the module with
CD19⁺ B cellsLymphoid signaling regulators
BCR/AP1/NFKb pathway
CCDC88B, FGD2, IKZF1, LENG8, MACF1, PCSK7, PHYKPL, PNISR +4 moreView in SCUBA
CD4⁺ T cellsJAK-STAT Signaling
Immune regulation
ARHGAP30, CELF2, DDX17, DNAJC1, GSDMD, HCLS1, JAK3, MBNL1 +7 moreView in SCUBA
Gamma-delta T cellsmTOR-Exocyst Signaling
TCR Signaling
ANKRD36C, ARFGEF1, CGGBP1, CTC1, DOCK11, EXOC1, EXOC4, FRYL +12 more
MacrophagesChromatin Epigenetic Regulation
Housekeeping
ABHD17B, ANKH, ARHGAP21, CCNH, CTTNBP2NL, DMXL1, EEIG2, ELF2 +21 moreView in SCUBA
Mucosal-associated invariant T cellChromatin Remodeling
DNA/chromatin regulation
ANP32E, ARHGAP30, CANX, DCTN1, EPRS1, FLII, HK1, JAK3 +9 more
NeutrophilsmRNA Splicing Processing
Housekeeping
ABCA13, ATP2A3, EMB, FBXO9, LUC7L3, NKTR, PAXBP1, PNN +8 more

About the gene

SynonymsFLJ23071, HRNT1, MGC22921, O-GLCNAC, OGT1
ChromosomeX: 71533087-71575892
Predicted locationIntracellular
Essential geneYes
Protein classDisease related genes, Enzymes, Essential proteins, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins
Molecular functionChromatin regulator, Glycosyltransferase, Transferase
Biological processApoptosis, Biological rhythms, Host-virus interaction, Ubl conjugation pathway

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). 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. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. 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. 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. Stabilizes KMT2E/MLL5 by mediating its glycosylation, thereby preventing KMT2E/MLL5 ubiquitination. 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. O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity). Promotes autophagy by mediating O-glycosylation of ATG4B. 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. The mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line. Has N-acetylglucosaminyltransferase activity: glycosylates proteins, such as HNRNPU, NEUROD1, NUP62 and PDCD6IP. Displays specific substrate selectivity compared to other isoforms

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.