Amino acid found i at o linked glycosylation point
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N-linked glycosylation, is the attachment of the sugar molecule oligosaccharide known asglycan to a nitrogen atom (amide nitrogen ofasparagine (Asn) residue of a protein), in a process called N-glycosylation, studied inbiochemistry. This type of linkage is important for both the structure and function of some eukaryotic proteins. The N-linked glycosylation process occurs ineukaryotes and widely in archaea, but very rarely in bacteria. The nature of N-linked glycans attached to a glycoprotein is determined by the protein and the cell in which it is expressed. It also varies acrossspecies. Different species synthesize different types of N-linked glycan.
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Alanine, serine and threonine are also significantly increased. The high serine and threonine content of O-glycosylated regions is due to the presence of clusters of several closely spaced glycosylated hydroxy amino acids in many O-glycosylated proteins.
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