Literature summary for 2.4.1.258 extracted from

Bailey, U.M.; Jamaluddin, M.F.; Schulz, B.L.
Analysis of congenital disorder of glycosylation-Id in a yeast model system shows diverse site-specific under-glycosylation of glycoproteins (2012), J. Proteome Res., 11, 5376-5383.

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Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

General Information

General Information	Comment	Organism
physiological function	an the alg3 knockout strain displays decreased site-specific N-glycosylation occupancy preferentially at Asn-Xaa-Ser sequences located in secondary structural elements. Glycosylation sites are not uniformly affected in DELTAalg3 cells, with the subset of sites with lower affinity for oligosaccharyltransferase most strongly affected. 13 specific glycosylation sites are found which are underglycosylated in the DELTAalg3 strain compared to wild type cells. The features of these glycosylation sites suggest that they are the subset of normally modified sites that are more difficult for oligosaccharyltransferase to glycosylate. Under-glycosylated sites in the DELTAalg3 strain are likely to be present in secondary structural elements such as helices or sheets, whereas efficiently glycosylated sites are more likely present in flexible loops	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)