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PROSITE documentation PDOC00001

N-glycosylation site





Description

It has been known for a long time [1] that potential N-glycosylation sites are specific to the consensus sequence Asn-Xaa-Ser/Thr. It must be noted that the presence of the consensus tripeptide is not sufficient to conclude that an asparagine residue is glycosylated, due to the fact that the folding of the protein plays an important role in the regulation of N-glycosylation [2]. It has been shown [3] that the presence of proline between Asn and Ser/Thr will inhibit N-glycosylation; this has been confirmed by a statistical analysis of glycosylation sites [4], which also shows that about 50% of the sites that have a proline C-terminal to Ser/Thr are not glycosylated.

It must also be noted that there are a few reported cases of glycosylation sites with the pattern Asn-Xaa-Cys; an experimentally demonstrated occurrence of such a non-standard site is found in the plasma protein C [5].

Last update:

May 1991 / Text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

ASN_GLYCOSYLATION, PS00001; N-glycosylation site  (PATTERN with a high probability of occurrence!)


References

1AuthorsMarshall R.D.
TitleGlycoproteins.
SourceAnnu. Rev. Biochem. 41:673-702(1972).
PubMed ID4563441
DOI10.1146/annurev.bi.41.070172.003325

2AuthorsPless D.D. Lennarz W.J.
TitleEnzymatic conversion of proteins to glycoproteins.
SourceProc. Natl. Acad. Sci. U.S.A. 74:134-138(1977).
PubMed ID264667

3AuthorsBause E.
TitleStructural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes.
SourceBiochem. J. 209:331-336(1983).
PubMed ID6847620

4AuthorsGavel Y. von Heijne G.
TitleSequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering.
SourceProtein Eng. 3:433-442(1990).
PubMed ID2349213

5AuthorsMiletich J.P. Broze G.J. Jr.
TitleBeta protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites.
SourceJ. Biol. Chem. 265:11397-11404(1990).
PubMed ID1694179



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