EGF domain specific O-linked N-acetylglucosamine transferase
Last updated 18 Aug 2020
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The EOGT gene provides instructions for making a protein that modifies certain other proteins by transferring a molecule called N-acetylglucosamine to them. This change, called an O-GlcNAc modification, can affect protein stability and regulate several cellular processes, such as signaling in cells and the first step in the production of proteins from genes (transcription). Little is known about the proteins altered by the EOGT protein or what effect the O-GlcNAc modification has on them. Studies suggest that Notch proteins may be modified by EOGT. Notch proteins stimulate signaling pathways important during the development of several tissues throughout the body, including the bones, heart, liver, muscles, and blood cells, among others.
Normal function
The EOGT gene provides instructions for making a protein that modifies certain other proteins by transferring a molecule called N-acetylglucosamine to them. This change, called an O-GlcNAc modification, can affect protein stability and regulate several cellular processes, such as signaling in cells and the first step in the production of proteins from genes (transcription). Little is known about the proteins altered by the EOGT protein or what effect the O-GlcNAc modification has on them. Studies suggest that Notch proteins may be modified by EOGT. Notch proteins stimulate signaling pathways important during the development of several tissues throughout the body, including the bones, heart, liver, muscles, and blood cells, among others.
Conditions referring to this gene or chromosome
Other names
AER61
AER61 glycosyltransferase
AOS4
C3orf64
EGF domain-specific O-linked N-acetylglucosamine (GlcNAc) transferase
EGF domain-specific O-linked N-acetylglucosamine transferase
EGF-O-GlcNAc transferase
EOGT1
EOGT_HUMAN
extracellular O-linked N-acetylglucosamine transferase
FLJ33770
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Further reading and references
- EGF domain specific O-linked N-acetylglucosamine transferase; MedlinePlus, National Library of Medicine.
- Cohen I, Silberstein E, Perez Y, Landau D, Elbedour K, Langer Y, Kadir R, Volodarsky M, Sivan S, Narkis G, Birk OS. Autosomal recessive Adams-Oliver syndrome caused by homozygous mutation in EOGT, encoding an EGF domain-specific O-GlcNAc transferase. Eur J Hum Genet. 2014 Mar;22(3):374-8. doi: 10.1038/ejhg.2013.159. Epub 2013 Jul 17.
- Ogawa M, Sawaguchi S, Kawai T, Nadano D, Matsuda T, Yagi H, Kato K, Furukawa K, Okajima T. Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in Adams-Oliver syndrome. J Biol Chem. 2015 Jan 23;290(4):2137-49. doi: 10.1074/jbc.M114.598821. Epub 2014 Dec 8.
- Sakaidani Y, Ichiyanagi N, Saito C, Nomura T, Ito M, Nishio Y, Nadano D, Matsuda T, Furukawa K, Okajima T. O-linked-N-acetylglucosamine modification of mammalian Notch receptors by an atypical O-GlcNAc transferase Eogt1. Biochem Biophys Res Commun. 2012 Mar 2;419(1):14-9. doi: 10.1016/j.bbrc.2012.01.098. Epub 2012 Jan 28.
- Sakaidani Y, Nomura T, Matsuura A, Ito M, Suzuki E, Murakami K, Nadano D, Matsuda T, Furukawa K, Okajima T. O-linked-N-acetylglucosamine on extracellular protein domains mediates epithelial cell-matrix interactions. Nat Commun. 2011 Dec 13;2:583. doi: 10.1038/ncomms1591.
- Shaheen R, Aglan M, Keppler-Noreuil K, Faqeih E, Ansari S, Horton K, Ashour A, Zaki MS, Al-Zahrani F, Cueto-Gonzalez AM, Abdel-Salam G, Temtamy S, Alkuraya FS. Mutations in EOGT confirm the genetic heterogeneity of autosomal-recessive Adams-Oliver syndrome. Am J Hum Genet. 2013 Apr 4;92(4):598-604. doi: 10.1016/j.ajhg.2013.02.012. Epub 2013 Mar 21.
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