OGT (gene)

From Wikipedia, the free encyclopedia

O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)

PDB rendering based on 1w3b.

Available structures: 1w3b

Identifiers

Symbol(s)

OGT; FLJ23071; HRNT1; MGC22921; O-GLCNAC

External IDs

OMIM: 300255 MGI: 1339639 HomoloGene: 9675

Gene ontology
Molecular Function:	• protein binding • acetylglucosaminyltransferase activity • transferase activity, transferring glycosyl groups
Cellular Component:	• nucleus • cytosol
Biological Process:	• protein amino acid O-linked glycosylation • signal transduction • response to nutrient

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_181672 (mRNA)
NP_858058 (protein)

NM_139144 (mRNA)
NP_631883 (protein)

Location

Chr X: 70.67 - 70.71 Mb

Chr X: 97.84 - 97.89 Mb

Pubmed search

[1]

[2]

O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase), also known as OGT, is a human gene.^[1]

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. Since both phosphorylation and glycosylation 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 tetratricopeptide repeats and a putative bipartite nuclear localization signal. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: OGT O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase).

[edit] 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. 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. 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. 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. 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. PMID 9083067.
Lubas WA, Frank DW, Krause M, Hanover JA (1997). "O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats.". J. Biol. Chem. 272 (14): 9316–24. PMID 9083068.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
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. PMID 9343410.
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. 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. 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. 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. PMID 10753899.