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HandWiki. OGT (Gene). Encyclopedia. Available online: https://encyclopedia.pub/entry/34857 (accessed on 27 September 2026).
HandWiki. OGT (Gene). Encyclopedia. Available at: https://encyclopedia.pub/entry/34857. Accessed September 27, 2026.
HandWiki. "OGT (Gene)" Encyclopedia, https://encyclopedia.pub/entry/34857 (accessed September 27, 2026).
HandWiki. (2022, November 16). OGT (Gene). In Encyclopedia. https://encyclopedia.pub/entry/34857
HandWiki. "OGT (Gene)." Encyclopedia. Web. 16 November, 2022.
OGT (Gene)
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UDP-N-acetylglucosamine—peptide N-acetylglucosaminyltransferase (EC 2.4.1.255), also known as O-linked β-N-acetylglucosamine transferase and O-GlcNAc transferase, OGT is an enzyme that in humans is encoded by the OGT gene.

β-n-acetylglucosamine n-acetylglucosaminyltransferase udp-n-acetylglucosamine—peptide

References

  1. "Cysteine S-linked N-acetylglucosamine (S-GlcNAcylation), A New Post-translational Modification in Mammals". Molecular & Cellular Proteomics 15 (11): 3405–3411. November 2016. doi:10.1074/mcp.M116.061549. PMID 27558639.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=5098038
  2. "Genetic recoding to dissect the roles of site-specific protein O-GlcNAcylation". Nature Structural & Molecular Biology 26 (11): 1071–1077. November 2019. doi:10.1038/s41594-019-0325-8. PMID 31695185.  https://dx.doi.org/10.1038%2Fs41594-019-0325-8
  3. "Entrez Gene: OGT O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8473. 
  4. "GlcNAcylation of histone H2B facilitates its monoubiquitination". Nature 480 (7378): 557–60. November 2011. doi:10.1038/nature10656. PMID 22121020.  https://dx.doi.org/10.1038%2Fnature10656
  5. "Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes". The Journal of Biological Chemistry 285 (8): 5204–11. February 2010. doi:10.1074/jbc.M109.077818. PMID 20018868.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2820748
  6. "O15294 (OGT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot". UniProt. https://www.uniprot.org/uniprot/O15294#ref11. 
  7. "Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease". Brain 132 (Pt 7): 1820–32. July 2009. doi:10.1093/brain/awp099. PMID 19451179.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2702834
  8. "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes & Development 17 (7): 896–911. April 2003. doi:10.1101/gad.252103. PMID 12670868.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=196026
  9. "Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression". Cell 110 (1): 69–80. July 2002. doi:10.1016/S0092-8674(02)00810-3. PMID 12150998.  https://dx.doi.org/10.1016%2FS0092-8674%2802%2900810-3
  10. "Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance". Nature 451 (7181): 964–9. February 2008. doi:10.1038/nature06668. PMID 18288188.  https://dx.doi.org/10.1038%2Fnature06668
  11. "The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny". Proceedings of the National Academy of Sciences of the United States of America 97 (11): 5735–9. May 2000. doi:10.1073/pnas.100471497. PMID 10801981.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18502
  12. "TET2 promotes histone O-GlcNAcylation during gene transcription". Nature 493 (7433): 561–4. January 2013. doi:10.1038/nature11742. PMID 23222540.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3684361
  13. "Structure of human O-GlcNAc transferase and its complex with a peptide substrate". Nature 469 (7331): 564–7. January 2011. doi:10.1038/nature09638. PMID 21240259.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3064491
  14. "Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway". Proceedings of the National Academy of Sciences of the United States of America 108 (7): 2747–52. February 2011. doi:10.1073/pnas.1013822108. PMID 21285374.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3041071
  15. "Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase". The Journal of Biological Chemistry 267 (13): 9005–13. May 1992. PMID 1533623.  http://www.ncbi.nlm.nih.gov/pubmed/1533623
  16. "O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats". The Journal of Biological Chemistry 272 (14): 9316–24. April 1997. doi:10.1074/jbc.272.14.9316. PMID 9083068.  https://dx.doi.org/10.1074%2Fjbc.272.14.9316
  17. "Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins". Nature 446 (7139): 1017–22. April 2007. doi:10.1038/nature05815. PMID 17460662.  https://dx.doi.org/10.1038%2Fnature05815
  18. "O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability". Proceedings of the National Academy of Sciences of the United States of America 98 (12): 6611–6. June 2001. doi:10.1073/pnas.111099998. PMID 11371615.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=34401
  19. "The hexosamine signaling pathway: deciphering the "O-GlcNAc code"". Science's STKE 2005 (312): re13. November 2005. doi:10.1126/stke.3122005re13. PMID 16317114.  https://dx.doi.org/10.1126%2Fstke.3122005re13
  20. "Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1". Science 324 (5929): 930–5. May 2009. doi:10.1126/science.1170116. PMID 19372391.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2715015
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