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Protein Page:
OGT (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
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, MLL5, MAPT/TAU 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. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Heterotrimer; consists of one 78 kDa subunit and two 110 kDa subunits dimerized via TPR repeats 6 and 7. Interacts (via TPR repeats 6 and 7) with ATXN10. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, HCFC1, PPP1CC and ACTB. Component of a THAP1/THAP3-HCFC1-OGT complex. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts directly with HCFC1; the interaction O- glycosylates HCFC1, regulates its proteolytic processing and transcriptional activity and, in turn, stabilizes OGT in the nucleus. Interacts (via TPRs 1-6) with SIN3A; the interaction mediates transcriptional repression in parallel with histone deacetylase. Induction of the nucleocytoplasmic OGT (ncOGT) isoform in the liver on glucose deprivation is mediated by the decreased hexosamine biosynthesis pathway (HBP) flux. Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver. Subject to product inhibition by UDP. Belongs to the O-GlcNAc transferase family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 2.4.1.-; Glycan Metabolism - O-glycan biosynthesis; EC 2.4.1.255; Transferase
Cellular Component: nucleoplasm; mitochondrion; cytoplasm; nucleolus; plasma membrane; microtubule organizing center; nucleus; cytosol; histone acetyltransferase complex
Molecular Function: acetylglucosaminyltransferase activity; protein binding; phosphatidylinositol-3,4,5-triphosphate binding; protein N-acetylglucosaminyltransferase activity; enzyme activator activity; histone acetyltransferase activity (H4-K16 specific)
Biological Process: positive regulation of catalytic activity; protein amino acid O-linked glycosylation; establishment and/or maintenance of chromatin architecture; phosphoinositide-mediated signaling; regulation of insulin receptor signaling pathway; positive regulation of proteolysis; apoptosis; positive regulation of granulocyte differentiation; positive regulation of histone H3-K4 methylation; signal transduction; response to insulin stimulus; regulation of Rac protein signal transduction; regulation of glycolysis; negative regulation of protein ubiquitination; positive regulation of transcription from RNA polymerase II promoter; circadian regulation of gene expression; response to nutrient
Reference #:  O15294 (UniProtKB)
Alt. Names/Synonyms: FLJ23071; HRNT1; MGC22921; O-GLCNAC; O-GlcNAc transferase p110 subunit; O-GlcNAc transferase subunit p110; O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase); O-linked N-acetylglucosamine transferase 110 kDa subunit; OGT; OGT1; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit; uridinediphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyl transferase
Gene Symbols: OGT
Molecular weight: 116,925 Da
Basal Isoelectric point: 6.22  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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OGT

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 S3-p _____MAssVGNVAD
1 0 S4-p ____MAssVGNVADS
0 1 K16-ub ADSTEPTkRMLsFQG
1 15 S20-p EPTkRMLsFQGLAEL
0 11 K83-ub HFSTLAIkQNPLLAE
0 33 K100-ub SNLGNVYkERGQLQE
0 44 K168-ub SDLGNLLkALGRLEE
0 10 K236-ub INLGNVLkEARIFDR
0 1 T325-p TALRLCPtHADSLNN
0 1 S365-p PEFAAAHsNLAsVLQ
0 1 S369-p AAHsNLAsVLQQQGK
0 1 Y384-p LQEALMHyKEAIRIS
1 0 T454-p EAIASYRtALKLKPD
0 1 K488 DYDERMKKLVsIVAD
0 1 S491-p ERMKKLVsIVADQLE
0 1 K550 YEHPKDLKLSDGRLR
0 12 K716-ub ANMFPHLkkKAVIDF
0 19 K717-ub NMFPHLkkKAVIDFK
0 1 K742 VLNGIDLKAFLDSLP
0 22 K742-ub VLNGIDLkAFLDSLP
0 2 K752-ub LDSLPDVkIVKMKCP
0 1 Y844 LPEDAIVYCNFNQLY
0 1 T857 LYKIDPSTLQMWANI
0 3 Y976-p IAKNRQEyEDIAVKL
1 0 Y989 KLGTDLEYLKKVRGK
0 5 K1010-ub SSPLFNTkQYTMELE
  mouse

 
S3 _____MASSVGNVAD
S4 ____MASSVGNVADS
K16 ADSTEPTKRMLsFQG
S20-p EPTKRMLsFQGLAEL
K83 HFSTLAIKQNPLLAE
K100-ub SNLGNVYkERGQLQE
K168-ub SDLGNLLkALGRLEE
K236-ub INLGNVLkEARIFDR
T325 TALRLCPTHADSLNN
S365 PEFAAAHSNLASVLQ
S369 AAHSNLASVLQQQGK
Y384 LQEALMHYKEAIRIS
T454 EAIASYRTALKLKPD
K488-ub DYDERMKkLVSIVAE
S491 ERMKkLVSIVAEQLE
K550-ub YEHPKDLkLSDGRLR
K716-ub ANMFPHLkkKAVIDF
K717-ub NMFPHLkkKAVIDFK
K742-ac VLNGIDLkAFLDSLP
K742-ub VLNGIDLkAFLDSLP
K752-ub LDSLPDVkIVKMKCP
Y844 LPEDAIVYCNFNQLY
T857-p LYKIDPStLQMWANI
Y976 IAKSRQEYEDIAVKL
Y989 KLGTDLEYLKKIRGK
K1010-ub SSPLFNTkQYTMELE
  rat

 
S3 _____MASSVGNVAD
S4 ____MASSVGNVADS
- gap
- gap
K73 HFSTLAIKQNPLLAE
K90 SNLGNVYKERGQLQE
K158 SDLGNLLKALGRLEE
K226 INLGNVLKEARIFDR
T315 TALRLCPTHADSLNN
S355 PEFAAAHSNLASVLQ
S359 AAHSNLASVLQQQGK
Y374 LQEALMHYKEAIRIS
T444-p EAIASYRtALKLKPD
K478 DYDERMKKLVSIVAE
S481 ERMKKLVSIVAEQLE
K540 YEHPKDLKLSDGRLR
K706-ub ANMFPHLkkKAVIDF
K707-ub NMFPHLkkKAVIDFK
K732 VLNGIDLKAFLDSLP
K732-ub VLNGIDLkAFLDSLP
K742 LDSLPDVKIVKMKCP
Y834-p LPEDAIVyCNFNQLY
T847 LYKIDPSTLQMGANI
Y966-p IAKSRQEyEDIAVKL
Y979-p KLGTDLEyLKKIRGK
K1000 SSPLFNTKQYTMELE
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