To study the sequence requirements for addition of O-linked N-acetylgalactosamine to proteins, amino acid distributions around 174 O-glycosylation sites were compared with distributions around non-glycosylated sites. In comparison with non-glycosylated serine and threonine residues, the most prominent feature in the vicinity of O-glycosylated sites is a significantly increased frequency of proline residues, especially at positions -1 and +3 relative to the glycosylated residues. 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. Such clusters can be predicted from the primary sequence in some cases, but there is no apparent possibility of predicting isolated O-glycosylation sites from primary sequence data.
Research Article|April 15 1991
Amino acid distributions around O-linked glycosylation sites
I B Wilson;
†Research Group for Theoretical Biophysics, Department of Theoretical Physics, Royal Institute of Technology, S-100 44 Stockholm, Sweden
‡IDepartment of Molecular Biology, Karolinska Institute, Center for Biotechnology, NOVUM, S-141 52 Huddinge, Sweden
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Biochem J (1991) 275 (2): 529-534.
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I B Wilson, Y Gavel, G von Heijne; Amino acid distributions around O-linked glycosylation sites. Biochem J 15 April 1991; 275 (2): 529–534. doi: https://doi.org/10.1042/bj2750529
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