Diseases associated with O-glycosylation of proteins

Stable Identifier
Homo sapiens
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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).

Literature References
PubMed ID Title Journal Year
24051442 Congenital disorders of glycosylation. Part II. Defects of protein O-glycosylation

Cylwik, B, Lipartowska, K, Chrostek, L, Gruszewska, E

Acta Biochim. Pol. 2013
24507773 Solving glycosylation disorders: fundamental approaches reveal complicated pathways

Freeze, HH, Chong, JX, Bamshad, MJ, Ng, BG

Am. J. Hum. Genet. 2014
Participant Of
Name Identifier Synonyms
congenital disorder of glycosylation 5212 carbohydrate-deficient glycoprotein syndrome
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