description
Glycosylation is the most abundant modification of proteins, variations of which occur in all living cells. Glycosylation can be further categorized into N-linked (where the oligosaccharide is conjugated to Asparagine residues) and O-linked glycosylation (where the oligosaccharide is conjugated to Serine, Threonine and possibly Tyrosine residues). Within the family of O-linked glycosylation, the oligosaccharides attached can be further categorized according to their reducing end residue: GalNAc (often described as mucin-type, due to the abundance of this type of glycosylation on mucins), Mannose and Fucose. This section reviews currently known congenital disorders of glycosylation associated with defects of protein O-glycosylation (Cylwik et al. 2013, Freeze et al. 2014)

external resources
NCBI:1383049
REACTOME:R-HSA-3906995
PUBMED:24051442
PUBMED:24507773

genes
DAG1 , MUC1 , MUC2 , MUC4 , MUC6 , MUC7 , NOTCH1 , NOTCH2 , NOTCH3 , NOTCH4 , CFP , THBS1 , THBS2 , SEMA5A , ADAMTS4 , ADAMTS3 , ADAMTS2 , ADAMTS1 , ADAMTSL2 , MUC12 , SPON2 , SPON1 , ADAMTS13 , ADAMTS8 , ADAMTS5 , ADAMTS7 , ADAMTS6 , SSPO , SEMA5B , ADAMTSL4 , THSD1 , MUC13 , ADAMTS9 , ADAMTSL3 , THSD4 , ADAMTS20 , THSD7B , ADAMTS12 , ADAMTS10 , ADAMTSL1 , MUC16 , MUCL1 , MUC17 , ADAMTS14 , MUC15 , SBSPON , ADAMTS15 , ADAMTS16 , ADAMTS17 , ADAMTS18 , ADAMTS19 , MUC20 , THSD7A , ADAMTSL5 , MUC21 , MUC5B ,