OGT (gene)

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

PDB rendering based on 1w3b.
Identifiers
Symbols OGT; FLJ23071; HRNT1; MGC22921; O-GLCNAC
External IDs OMIM300255 MGI1339639 HomoloGene9675 GeneCards: OGT Gene
RNA expression pattern
PBB GE OGT 207563 s at tn.png
PBB GE OGT 207564 x at tn.png
PBB GE OGT 209240 at tn.png
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. 

Wikimedia Foundation. 2010.

Игры ⚽ Поможем решить контрольную работу

Look at other dictionaries:

  • OGT — Ohio Graduation Test (Community » Educational) * Oxford Gene Technology (Medical » Human Genome) * Orphan Grain Train (Community » Non Profit Organizations) * Operation Game Thief (Community » Sports) * Operation Game Thief (Community » Law) *… …   Abbreviations dictionary

  • Tay-Sachs disease — Infobox Disease Name = Tay Sachs disease Caption = DiseasesDB = 12916 ICD10 = ICD10|E|75|0|e|70 ICD9 = ICD9|330.1 ICDO = OMIM = 272800 OMIM mult = OMIM2|272750 MedlinePlus = 001417 eMedicineSubj = ped eMedicineTopic = 3016 MeshID = D013661 Tay… …   Wikipedia

  • DNA repair — For the journal, see DNA Repair (journal). DNA damage resulting in multiple broken chromosomes DNA repair refers to a collection of processes by which a cell identifies and corrects damage to the DNA molecules that encode its genome. In human… …   Wikipedia

  • MSH2 — MutS homolog 2, colon cancer, nonpolyposis type 1 (E. coli) PDB rendering based on 2o8b …   Wikipedia

  • Саузерн, Эдвин — Сэр Эдвин Мэллор Саузерн (р. 7 июня 1938)  английский молекулярный биолог, член лондонского королевского общества по развитию знаний о природе (также известного как лондонское королевское общество), лауреат премии Ласкера (2005). Премия была …   Википедия

  • Non-homologous end joining — (NHEJ) is a pathway that repairs double strand breaks in DNA. NHEJ is referred to as non homologous because the break ends are directly ligated without the need for a homologous template, in contrast to homologous recombination, which requires a… …   Wikipedia

  • Edwin Southern — Infobox Scientist name = Sir Edwin Southern image width = 200px caption = birth date = 1938 birth place = United Kingdom nationality = British death date = death place = field = Biochemistry work institutions = University of Oxford, University of …   Wikipedia

  • MODY Diabetes — MODY ist die Abkürzung für Maturity Onset Diabetes of the Young, übersetzt „Erwachsenendiabetes, der bei Jugendlichen auftritt“. Diese Bezeichnung wird seit den 1970er Jahren für einige Formen des Diabetes mellitus verwendet. Seit 1998 werden die …   Deutsch Wikipedia

  • Postreplication repair — is the repair of damage to the DNA that takes place after replication. Some example genes in humans include: BRCA2 and BRCA1 BLM NBS1 DNA damage prevents the normal enzymatic synthesis of DNA by the replication fork.[1][2][3][4] …   Wikipedia

  • HCFC1 — Factor celular hospedador C1 HUGO 4839 Símbolo HCFC1 Símbolos alt. CFF; HCF 1; HCF1; HFC1; MGC70925; VCAF …   Wikipedia Español

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”