Diseases associated with O-glycosylation of proteins

Stable Identifier
R-HSA-3906995
Type
Pathway
Species
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
Participants
Participant Of
Disease
Name Identifier Synonyms
congenital disorder of glycosylation 5212 carbohydrate-deficient glycoprotein syndrome
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