EOGT gene
EGF domain specific O-linked N-acetylglucosamine transferase
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.
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At least three mutations in the EOGT gene have been found in individuals with Adams-Oliver syndrome. This condition is characterized by areas of missing skin (aplasia cutis congenita), usually on the scalp, and malformations of the hands and feet. The most common EOGT gene mutation involved in this condition, which is found in the Arab population, leads to an abnormally short protein. The other mutations change single protein building blocks (amino acids) in the EOGT protein. Research suggests that the EOGT gene mutations reduce or eliminate the protein's ability to transfer N-acetylglucosamine. It is unknown what effect this impairment has on cells or how it leads to the features of Adams-Oliver syndrome.
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Cytogenetic Location: 3p14.1, which is the short (p) arm of chromosome 3 at position 14.1
Molecular Location: base pairs 68,975,212 to 69,013,961 on chromosome 3 (Homo sapiens Updated Annotation Release 109.20190607, GRCh38.p13) (NCBI)
Related Information
- 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
Related Information
- 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.
- OMIM: EGF DOMAIN-SPECIFIC O-LINKED N-ACETYLGLUCOSAMINE TRANSFERASE
- 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-González 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.