Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1

Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in... Mammalian Genome 13, 62–64 (2002). DOI: 10.1007/s00335-001-2108-9 Incorporating Mouse Genome © Springer-Verlag New York Inc. 2002 Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1 Dagmar Nolte, Ulrich Mu ¨ ller Institut fu ¨ r Humangenetik, Justus-Liebig-Universita ¨t, Schlangenzahl 14, 35392 Giessen, Germany Received: 9 July 2001 / Accepted: 22 August 2001 O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) quenced (AL590763), and 18 exons corresponding to the reported catalyzes polypeptide glycosylation by the addition of N- full-length hOGT cDNA (Lubas et al. 1997) were identified in acetylglucosamine to serine and threonine residues. This process is silico (exons 6–23 of Fig. 1). We screened a human fetal brain 5 referred to as O-GlcNAcylation and has been observed to occur on stretch plus cDNA library (Clontech, Cat. HL5015b) with a 490-bp many nuclear and cytosolic proteins. These include RNA- probe corresponding to exons 8–11 (Fig. 1). Three different clones polymerase II, nuclear pore proteins, neurofilaments, microtubule- with inserts of 1.6 kb, 2.0 kb, and 2.3 kb were obtained. The 2.0-kb associated proteins such as tau, synapsin I, and both onco- and insert revealed an additional 700-bp 5 sequence, but did not con- tumor suppressor proteins. O-GlcNAcylation is a http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Mammalian Genome Springer Journals

Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1

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Publisher
Springer-Verlag
Copyright
Copyright © 2002 by Springer-Verlag New York Inc.
Subject
Life Sciences; Cell Biology; Anatomy; Zoology
ISSN
0938-8990
eISSN
1432-1777
D.O.I.
10.1007/s00335-001-2108-9
Publisher site
See Article on Publisher Site

Abstract

Mammalian Genome 13, 62–64 (2002). DOI: 10.1007/s00335-001-2108-9 Incorporating Mouse Genome © Springer-Verlag New York Inc. 2002 Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1 Dagmar Nolte, Ulrich Mu ¨ ller Institut fu ¨ r Humangenetik, Justus-Liebig-Universita ¨t, Schlangenzahl 14, 35392 Giessen, Germany Received: 9 July 2001 / Accepted: 22 August 2001 O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) quenced (AL590763), and 18 exons corresponding to the reported catalyzes polypeptide glycosylation by the addition of N- full-length hOGT cDNA (Lubas et al. 1997) were identified in acetylglucosamine to serine and threonine residues. This process is silico (exons 6–23 of Fig. 1). We screened a human fetal brain 5 referred to as O-GlcNAcylation and has been observed to occur on stretch plus cDNA library (Clontech, Cat. HL5015b) with a 490-bp many nuclear and cytosolic proteins. These include RNA- probe corresponding to exons 8–11 (Fig. 1). Three different clones polymerase II, nuclear pore proteins, neurofilaments, microtubule- with inserts of 1.6 kb, 2.0 kb, and 2.3 kb were obtained. The 2.0-kb associated proteins such as tau, synapsin I, and both onco- and insert revealed an additional 700-bp 5 sequence, but did not con- tumor suppressor proteins. O-GlcNAcylation is a

Journal

Mammalian GenomeSpringer Journals

Published: Feb 19, 2014

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