title: Analysis of O-glycosylation.
abstract: Secreted as well as membrane-associated eukaryotic proteins are most commonly glycosylated. Saccharides are attached to proteins mainly through N-and O-glycosydic bonds or as part of the glycosylphosphatidyinositol-membrane anchor. In contrast to N-glycosylation, which involves the co-translational transfer in the endoplasmic reticulum (ER) of the glycan portion of Glc3Man9GlcNAc2-PP-dolichol to suitable Asn residues on nascent polypeptides, O-glycosylation begins with the addition of a single monosaccharide. Contrary to N-glycosylation, which involves an asparagine residue in the sequon Asn-Xaa-Thr/Ser (Xaa can be any amino acid except Pro, and it is rarely Cys), no particular sequence motif has been described for O-glycosylation. This may reflect the fact that: (1) the specificity of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is presently unknown; and (2) seems to be modulated by sequence context, secondary structure, and surface accessibility (1). An internet server, accessible at http://www.cbs.dtu.dk/netOglyc/cbsnetOglyc.html , produces neural network predictions of mucin-type GalNAc O-glycosylation sites in mammalian proteins based on 299 known and verified mucin-type O-glycosylation sites. The sequence context of glycosylated threonines was found to differ from that of serine, and the sites were found to cluster. Nonclustered sites had a sequence context different from that of clustered sites, and charged residues were disfavored at position -1 and +3.
authors: Instituto de Biomedicina de Valencia, CSIC, Valencia, Spain.
authors: Juan J
authors: JJ
authors: Calvete
authors: Libia
authors: L
authors: Sanz
mesh_terms: D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006031:Glycosylation; D008970:Molecular Weight; D011506:Proteins / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D011506:Proteins