ArticleInternational journal of molecular sciences2010
Computational prediction of O-linked glycosylation sites that preferentially map on intrinsically disordered regions of extracellular proteins.
Article in International journal of molecular sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Deciphering How Clustered O‑Glycosylation Shapes Substrate-Binding Preferences in an Intrinsically Disordered Protein Region.JACS Au · 2026Article
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- The non-catalytic domains of O-GlcNAc cycling enzymes present new opportunities for function-specific control.Current opinion in chemical biology · 2024Review
- Many Roles of Carbohydrates: A Computational Spotlight on the Coronavirus S Protein Binding.ACS applied bio materials · 2024Review
- Structural analysis and functional evaluation of the disordered ß-hexosyltransferase region fromFrontiers in bioengineering and biotechnology · 2023Article
- Review
- PolarProtPred: predicting apical and basolateral localization of transmembrane proteins using putative short linear motifs and deep learning.Bioinformatics (Oxford, England) · 2021Article
- Suppression of O-Linked Glycosylation of the SARS-CoV-2 Spike by Quaternary Structural Restraints.Analytical chemistry · 2021Article
- Advances in chemical probing of proteinChemical Society reviews · 2021Review
- Review
- Precision Mapping of O-LinkedJournal of the American Chemical Society · 2020Article
- Mutually exclusive locales for N-linked glycans and disorder in human glycoproteins.Scientific reports · 2020Article
- Parallel Determination of Polypeptide and Oligosaccharide Connectivities by Energy-Resolved Collison-Induced Dissociation of Protonated O-Glycopeptides Derived from Nonspecific Proteolysis.Journal of the American Society for Mass Spectrometry · 2020Article
- Review
- Exploitation of glycosylation in enveloped virus pathobiology.Biochimica et biophysica acta. General subjects · 2019Review
- Structure and function of class III pistil-specific extensin-like protein in interspecific reproductive barriers.BMC plant biology · 2019Article
- Cell Metabolism Control Through O-GlcNAcylation of STAT5: A Full or Empty Fuel Tank Makes a Big Difference for Cancer Cell Growth and Survival.International journal of molecular sciences · 2019Review
- Mapping the O-glycoproteome using site-specific extraction of O-linked glycopeptides (EXoO).Molecular systems biology · 2018Article
- Too sweet to resist: Control of immune cell function by O-GlcNAcylation.Cellular immunology · 2018Review
- Investigation of Outbreak-Specific Nonsynonymous Mutations on Ebolavirus GP in the Context of Known Immune Reactivity.Journal of immunology research · 2018Article
Corrections and comments
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
O-glycosylation of mammalian proteins is one of the important posttranslational modifications. We applied a support vector machine (SVM) to predict whether Ser or Thr is glycosylated, in order to elucidate the O-glycosylation mechanism. O-glycosylated sites were often found clustered along the sequence, whereas other sites were located sporadically. Therefore, we developed two types of SVMs for predicting clustered and isolated sites separately. We found that the amino acid composition was effective for predicting the clustered type, whereas the site-specific algorithm was effective for the isolated type. The highest prediction accuracy for the clustered type was 74%, while that for the isolated type was 79%. The existence frequency of amino acids around the O-glycosylation sites was different in the two types: namely, Pro, Val and Ala had high existence probabilities at each specific position relative to a glycosylation site, especially for the isolated type. Independent component analyses for the amino acid sequences around O-glycosylation sites showed the position-specific existences of the identified amino acids as independent components. The O-glycosylation sites were preferentially located within intrinsically disordered regions of extracellular proteins: particularly, more than 90% of the clustered O-GalNAc glycosylation sites were observed in intrinsically disordered regions. This feature could be the key for understanding the non-conservation property of O-glycosylation, and its role in functional diversity and structural stability.
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