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Updated: Jun 4, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
Distribution of N-glycosylation sequons in proteins: how apart are they?
R Shyama Prasad Rao1, Ole Thomsen Buus, Bernd Wollenweber
1Aarhus University, Department of Genetics and Biotechnology, Slagelse, Denmark. drrsprao@yahoo.co.in
Abstract:
N-glycosylation is a common protein modification process, which affects a number of properties of proteins. Little is known about the distribution of N-glycosylation sequons, for example, the distance between glycosylated sites and their position in the protein primary sequence. Using a large set of experimentally confirmed eukaryotic N-glycoproteins we analyzed the relative position and distribution of sequons. N-Glycosylation probability was found to be lower in the termini of protein sequences compared to the mid region. N-glycosylated sequons were found much farther from C terminus compared to the N-terminus of the protein sequence and this effect was more pronounced for NXS sequons. The distribution of sequons, modeled based on balls-in-boxes classical occupancy, showed a near-maximum probability. Considerable proportion of sequons was found within a distance of ten amino acids, indicating that the steric hindrance was not a key factor in protein N-glycosylation. Interestingly, the distribution of all sequons present in N-glycoproteins showed a pattern very similar to that of glycosylated sequons. The results indicate that protein N-glycosylation chiefly follows a random design.
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Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

