ISOGlyP: de novo prediction of isoform-specific mucin-type O-glycosylation.

Glycobiology
Jonathon E MohlMing-Ying Leung

Abstract

Mucin-type O-glycosylation is one of the most common posttranslational modifications of proteins. The abnormal expression of various polypeptide GalNAc-transferases (GalNAc-Ts) which initiate and define sites of O-glycosylation are linked to many cancers and other diseases. Current O-glycosyation prediction programs utilize O-glycoproteomics data obtained without regard to the transferase isoform (s) responsible for the glycosylation. With 20 different GalNAc-Ts in humans, having an ability to predict and interpret O-glycosylation sites in terms of specific GalNAc-T isoforms is invaluable. To fill this gap, ISOGlyP (Isoform-Specific O-Glycosylation Prediction) has been developed. Using position-specific enhancement values generated based on GalNAc-T isoform-specific amino acid preferences, ISOGlyP predicts the propensity that a site would be glycosylated by a specific transferase. ISOGlyP gave an overall prediction accuracy of 70% against in vivo data, which is comparable to that of the NetOGlyc4.0 predictor. Additionally, ISOGlyP can identify the known effects of long- and short-range prior glycosylation and can generate potential peptide sequences selectively glycosylated by specific isoforms. ISOGlyP is freely available for ...Continue Reading

References

Apr 16, 2013·The EMBO Journal·Catharina SteentoftHenrik Clausen
Jun 21, 2016·Oncotarget·Muhammad Ramzan Manwar HussainMin Fang
Dec 4, 2016·Glycobiology·María Florencia FestariEduardo Osinaga
Nov 20, 2020·Journal of Theoretical & Computational Chemistry·Jonathon E MohlMing-Ying Leung

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Citations

Jul 29, 2021·ACS Chemical Biology·Valentina Rangel-Angarita, Stacy A Malaker
Jun 13, 2021·Genomics, Proteomics & Bioinformatics·José Alexandre FerreiraLúcio Lara Santos

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