ISOGlyP

ISOGlyP predicts isoform-specific mucin-type O-glycosylation sites by assigning polypeptide GalNAc-transferase (GalNAc-T) isoforms that may transfer N-acetylgalactosamine (GalNAc) to serine or threonine residues.

Key Features:

• Isoform-Specific Prediction: Predicts O-glycosylation sites with assignment to specific GalNAc-T isoforms among the 20 different human GalNAc-Ts.
• Position-Specific Enhancement Values: Uses position-specific enhancement values derived from isoform-specific amino acid preferences to score the likelihood of glycosylation at candidate sites.
• Prediction Accuracy: Demonstrates approximately 70% overall prediction accuracy against in vivo data, comparable to NetOGlyc4.0.
• Consideration of Glycosylation Effects: Accounts for the known effects of both long- and short-range prior glycosylation events when evaluating site likelihoods.
• Generation of Selective Peptide Sequences: Generates candidate peptide sequences predicted to be selectively glycosylated by specific GalNAc-T isoforms.

Scientific Applications:

• Disease and Cancer Research: Enables analysis of GalNAc-T isoform–dependent O-glycosylation changes implicated in diseases, including various cancers.
• Biomarker and Therapeutic Target Discovery: Supports identification of glycosylation-based biomarkers and potential therapeutic targets by detailing isoform-specific modification patterns.

Methodology:

Integrates position-specific enhancement values based on isoform-specific amino acid preferences and models the influence of long- and short-range prior glycosylation events to predict GalNAc-T–specific O-glycosylation on serine and threonine residues.