O-GLYCBASE: a revised database of O-glycosylated proteins
Open Access
- 1 January 1996
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 24 (1) , 248-252
- https://doi.org/10.1093/nar/24.1.248
Abstract
O-GLYCBASE is a comprehensive database of information on glycoproteins and their O -linked glycosylationsites. Entries are compiled and revised from the SWISS-PROT and PIR databases as well as directly from recently published reports. Nineteen percent of the entries extracted from the databases needed revision with respect to O -linked glycosylation. Entries include information about species, sequence, glycosylation site and glycan type, and are fully referenced. Sequence logos displaying the acceptor specificity for the GalNAc transferase is shown. A neural network method for prediction of mucin type O -glycosylation sites in mammalian glycoproteins exclusively from the primary sequence is made available by E-mail or WWW. The O-GLYCBASE database is also available electronically through our WWW server or by anonymous FTP.Keywords
This publication has 39 references indexed in Scilit:
- Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferaseBiochemical Journal, 1995
- Neural network detects errors in the assignment of mRNA splice sitesNucleic Acids Research, 1990
- Cleaning up gene databasesNature, 1990
- Identification of a Disaccharide (Xyl-Glc) and a Trisaccharide (Xyl2-Glc) O-Glycosidically Linked to a Serine Residue in the First Epidermal Growth Factor-like Domain of Human Factors VII and IX and Protein Z and Bovine Protein ZJournal of Biological Chemistry, 1989
- Predicting the secondary structure of globular proteins using neural network modelsJournal of Molecular Biology, 1988
- Isolation and sequence analysis of the glycosaminoglycan attachment site of type IX collagen.Journal of Biological Chemistry, 1988
- Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins.Proceedings of the National Academy of Sciences, 1987
- Influence of quaternary structure on glycosylation. Differential subunit association affects the site-specific glycosylation of the common beta-chain from Mac-1 and LFA-1.Journal of Biological Chemistry, 1986
- A Revision of the N-Terminal Structure of Sialoglycoprotein D (Glycophorin C) from Human Erythrocyte MembranesBiological Chemistry Hoppe-Seyler, 1985
- Properties of potato lectin and the nature of its glycoprotein linkagesBiochemical Journal, 1978