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PMID: 8948436 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase.

The Biochemical journal ·Vol. 308 ( Pt 3) ·1995-06-15 ·Pages 801-13

Hansen JE, Lund O, Engelbrecht J, Bohr H, Nielsen JO, Hansen JE

Abstract

The specificity of the enzyme(s) catalysing the covalent link between the hydroxyl side chains of serine or threonine and the sugar moiety N-acetylgalactosamine (GalNAc) is unknown. Pattern recognition by artificial neural networks and weight matrix algorithms was performed to determine the exact position of in vivo O-linked GalNAc-glycosylated serine and threonine residues from the primary sequence exclusively. The acceptor sequence context for O-glycosylation of serine was found to differ from that of threonine and the two types were therefore treated separately. The context of the sites showed a high abundance of proline, serine and threonine extending far beyond the previously reported region covering positions -4 through +4 relative to the glycosylated residue. The O-glycosylation sites were found to cluster and to have a high abundance in the N-terminal part of the protein. The sites were also found to have an increased preference for three different classes of beta-turns. No simple consensus-like rule could be deduced for the complex glycosylation sequence acceptor patterns. The neural networks were trained on the hitherto largest data material consisting of 48 carefully examined mammalian glycoproteins comprising 264 O-glycosylation sites. For detection neural network algorithms were much more reliable than weight matrices. The networks correctly found 60-95% of the O-glycosylated serine/threonine residues and 88-97% of the non-glycosylated residues in two independent test sets of known glycoproteins. A computer server using E-mail for prediction of O-glycosylation sites has been implemented and made publicly available. The Internet address is NetOglyc@cbs.dtu.dk.

MeSH Terms
Algorithms Animals Computer Communication Networks Glycoproteins/chemistry Glycosylation Information Systems Mammals/metabolism Molecular Sequence Data N-Acetylgalactosaminyltransferases/chemistry,metabolism Neural Networks, Computer Protein Structure, Secondary Serine/chemistry,metabolism Threonine/chemistry,metabolism
Chemicals
Glycoproteins Threonine Serine N-Acetylgalactosaminyltransferases polypeptide N-acetylgalactosaminyltransferase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hansen J E
Laboratory for Infectious Diseases, Hvidovre Hospital, University of Copenhagen, Denmark.
Lund O
Engelbrecht J
Bohr H
Nielsen J O
Hansen J E
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1995-06-15
Pages
801-13
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1136796
Subset
IM
Analysis Services
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