Peptide Modifications advanced
O-Glycosylation of Peptides
Explore O-glycosylation on serine and threonine residues and its impact on peptide function.
By Encyclopeptide Editorial | 1 min read
glycosylation post-translational modification
Overview
O-glycosylation attaches sugar moieties to serine or threonine hydroxyl groups, primarily in the Golgi apparatus.
Types
- Mucin-type (GalNAc): Most common O-glycan
- O-Fucose: Notch signaling regulation
- O-GlcNAc: Cytoplasmic/nuclear modification
- O-Mannose: Muscular dystrophy-related
Biological Significance
O-glycosylation is critical for mucin function, cell adhesion, and immune recognition. Aberrant O-glycosylation is a cancer hallmark.
References
- Source: ENCP Peptide Database
- Category: Peptide Modifications
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