| Description | Glycans are vital components of glycoproteins, glycolipids, and proteoglycans in all domains of life. Glycoproteins are grouped by the type of carbohydrate and amino acid linkage site. N-linked glycosylation is a modification of asparagine, whereas O-linked glycosylation occurs through the hydroxyl group of serine and threonine residues. Glycosylation occurs co- or post-translationally on >50% of eukaryotic proteins resulting in membrane-associated, intracellular, or secreted glycoproteins that are crucial in cellular processes, protein bioactivity and metabolic turnover. Attachment of O-linked mucin-type glycans is a common post-translational modification initiated by the addition of N-acetyl-galactosamine (GalNAc) to a Ser or Thr residue |
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