OGT (gene)

O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)
PDB rendering based on 1w3b.
Available structures PDB 1w3b
Identifiers
Symbols	OGT; FLJ23071; HRNT1; MGC22921; O-GLCNAC
External IDs	OMIM: 300255 MGI: 1339639 HomoloGene: 9675 GeneCards: OGT Gene
Gene Ontology Molecular function • protein binding • enzyme activator activity • acetylglucosaminyltransferase activity • protein N-acetylglucosaminyltransferase activity • transferase activity, transferring glycosyl groups • peptide binding • monosaccharide binding Cellular component • nucleus • cytoplasm • cytosol • MLL5-L complex Biological process • protein O-linked glycosylation • signal transduction • response to nutrient • positive regulation of granulocyte differentiation • positive regulation of catalytic activity • positive regulation of proteolysis • positive regulation of histone H3-K4 methylation • protein homotrimerization • cellular response to retinoic acid Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8473	108155
Ensembl	ENSG00000147162	ENSMUSG00000034160
UniProt	O15294	n/a
RefSeq (mRNA)	NM_181672.2	NM_139144.3
RefSeq (protein)	NP_858058.1	NP_631883.2
Location (UCSC)	Chr X: 70.75 – 70.8 Mb	Chr X: 98.84 – 98.88 Mb
PubMed search	[1]	[2]

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit is an enzyme that in humans is encoded by the OGT gene.^[1][2]

O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues of intracellular proteins. Since both phosphorylation and O-GlcNAcylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. The protein contains nine or 14 tetratricopeptide repeats, depending on the splice variant, and a putative bipartite nuclear localization signal. Two alternatively spliced transcript variants encoding distinct isoforms (nucleocytoplasmic and mitochondrial) have been found for this gene.^[2]

Interactions

OGT (gene) has been shown to interact with Host cell factor C1^[3] and SIN3A.^[4]

References

1. ^ Lubas WA, Frank DW, Krause M, Hanover JA (May 1997). "O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats". J Biol Chem 272 (14): 9316–24. doi:10.1074/jbc.272.14.9316. PMID 9083068. 
2. ^ ^{a b} "Entrez Gene: OGT O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8473. 
3. ^ Wysocka, Joanna; Myers Michael P, Laherty Carol D, Eisenman Robert N, Herr Winship (Apr. 2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. (United States) 17 (7): 896–911. doi:10.1101/gad.252103. ISSN 0890-9369. PMC 196026. PMID 12670868. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=196026. 
4. ^ Yang, Xiaoyong; Zhang Fengxue, Kudlow Jeffrey E (Jul. 2002). "Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression". Cell (United States) 110 (1): 69–80. doi:10.1016/S0092-8674(02)00810-3. ISSN 0092-8674. PMID 12150998. 

Further reading

• Konrad RJ, Kudlow JE (2002). "The role of O-linked protein glycosylation in beta-cell dysfunction". Int. J. Mol. Med. 10 (5): 535–9. PMID 12373287. 
• Reason AJ, Morris HR, Panico M et al. (1992). "Localization of O-GlcNAc modification on the serum response transcription factor". J. Biol. Chem. 267 (24): 16911–21. PMID 1512232. 
• Haltiwanger RS, Blomberg MA, Hart GW (1992). "Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase". J. Biol. Chem. 267 (13): 9005–13. PMID 1533623. 
• Roquemore EP, Dell A, Morris HR et al. (1992). "Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine". J. Biol. Chem. 267 (1): 555–63. PMID 1730617. 
• Chou TY, Hart GW, Dang CV (1995). "c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas". J. Biol. Chem. 270 (32): 18961–5. doi:10.1074/jbc.270.32.18961. PMID 7642555. 
• Murphy JE, Hanover JA, Froehlich M et al. (1994). "Clathrin assembly protein AP-3 is phosphorylated and glycosylated on the 50-kDa structural domain". J. Biol. Chem. 269 (33): 21346–52. PMID 8063760. 
• Matoba R, Okubo K, Hori N et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID 8076819. 
• Dong DL, Xu ZS, Chevrier MR et al. (1993). "Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M". J. Biol. Chem. 268 (22): 16679–87. PMID 8344946. 
• Andersson B, Wentland MA, Ricafrente JY et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474. 
• Roquemore EP, Chevrier MR, Cotter RJ, Hart GW (1996). "Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin". Biochemistry 35 (11): 3578–86. doi:10.1021/bi951918j. PMID 8639509. 
• Dong DL, Xu ZS, Hart GW, Cleveland DW (1996). "Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H". J. Biol. Chem. 271 (34): 20845–52. doi:10.1074/jbc.271.34.20845. PMID 8702840. 
• Arnold CS, Johnson GV, Cole RN et al. (1997). "The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine". J. Biol. Chem. 271 (46): 28741–4. doi:10.1074/jbc.271.46.28741. PMID 8910513. 
• Kreppel LK, Blomberg MA, Hart GW (1997). "Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats". J. Biol. Chem. 272 (14): 9308–15. doi:10.1074/jbc.272.14.9308. PMID 9083067. 
• Yu W, Andersson B, Worley KC et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146. 
• Roos MD, Su K, Baker JR, Kudlow JE (1997). "O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions". Mol. Cell. Biol. 17 (11): 6472–80. PMC 232500. PMID 9343410. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=232500. 
• Medina L, Grove K, Haltiwanger RS (1998). "SV40 large T antigen is modified with O-linked N-acetylglucosamine but not with other forms of glycosylation". Glycobiology 8 (4): 383–91. doi:10.1093/glycob/8.4.383. PMID 9499386. 
• Cole RN, Hart GW (1999). "Glycosylation sites flank phosphorylation sites on synapsin I: O-linked N-acetylglucosamine residues are localized within domains mediating synapsin I interactions". J. Neurochem. 73 (1): 418–28. doi:10.1046/j.1471-4159.1999.0730418.x. PMID 10386995. 
• Akimoto Y, Kreppel LK, Hirano H, Hart GW (1999). "Localization of the O-linked N-acetylglucosamine transferase in rat pancreas". Diabetes 48 (12): 2407–13. doi:10.2337/diabetes.48.12.2407. PMID 10580430. 
• Lubas WA, Hanover JA (2000). "Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity". J. Biol. Chem. 275 (15): 10983–8. doi:10.1074/jbc.275.15.10983. PMID 10753899.