Recombinant Human OGT / O-Linked N-Acetylglucosamine Transferase protein (GST tag N-Terminus)
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(1 Publication)
Recombinant Human OGT / O-Linked N-Acetylglucosamine Transferase protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 1046 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, O-GlcNAc transferase subunit p110, O-linked N-acetylglucosamine transferase 110 kDa subunit, OGT
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human OGT / O-Linked N-Acetylglucosamine Transferase protein (GST tag N-Terminus) (AB131881)
12.5% SDS-PAGE stained with Coomassie Blue showing ab131881 at approximately 143.3 kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Through its transferase activity OGT regulates a wide array of cellular functions including signal transduction transcription and metabolism. It is a component of a complex involving several other proteins that facilitate its regulatory actions. OGT manages protein function and stability by influencing interactions between proteins and other cellular components.
Pathways
OGT is critical in the insulin signaling pathway and the regulation of glucose metabolism. It interacts with multiple proteins such as IRS-1 and Akt to modulate their activity and stability. The modification by OGT impacts protein phosphorylation states affecting the downstream processing of cellular signals.
Specifications
Form
Liquid
General info
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 : 12150998, PubMed : 15361863, PubMed : 19451179, PubMed : 20018868, PubMed : 21240259, PubMed : 21285374, PubMed : 23103939, PubMed : 26237509, PubMed : 26369908, PubMed : 26678539, PubMed : 27713473, PubMed : 37541260, PubMed : 37962578). 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 : 19451179, PubMed : 20200153, PubMed : 21285374, PubMed : 22923583, PubMed : 23353889, PubMed : 24474760, PubMed : 26237509, PubMed : 26369908, PubMed : 26678539, PubMed : 27527864, PubMed : 30699359, PubMed : 34074792, PubMed : 34667079, PubMed : 37541260, PubMed : 37962578). Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing (PubMed : 21285374). 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 (PubMed : 22923583). 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) (PubMed : 22121020, PubMed : 23353889). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed : 20018852). O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (PubMed : 24474760). Stabilizes KMT2E/MLL5 by mediating its glycosylation, thereby preventing KMT2E/MLL5 ubiquitination (PubMed : 26678539). 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 (PubMed : 21285374, PubMed : 28302723, PubMed : 28584052). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (PubMed : 20200153). Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity). Promotes autophagy by mediating O-glycosylation of ATG4B (PubMed : 27527864). 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 (PubMed : 30699359, PubMed : 37541260).. Isoform 2. The mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.. Isoform 4. Has N-acetylglucosaminyltransferase activity : glycosylates proteins, such as HNRNPU, NEUROD1, NUP62 and PDCD6IP (PubMed : 31527085). Displays specific substrate selectivity compared to other isoforms (PubMed : 31527085).
Sequence similarities
Belongs to the glycosyltransferase 41 family. O-GlcNAc transferase subfamily.
Post-translational modifications
Ubiquitinated by the SCF(FBXO31) complex, leading to its proteasomal degradation.. Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity (By similarity). Phosphorylation at Thr-454 by AMPK promotes nuclear localization (PubMed:24563466).. Glycosylated via autocatalysis; O-GlcNAcylation at Ser-399 promotes nuclear localization.. Isoform 4. Glycosylated via autocatalysis; does not affect the enzyme activity but regulates substrate selectivity.
Subcellular localisation
Nucleus
Target data
Publications (1)
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Experimental cell research 382:111464 PubMed31202709
2019
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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