O-GlyThr
O-GlyThr predicts human O-linked threonine glycosylation sites using a feature-fusion approach and a random forest classifier to enable accurate identification of O-glycosites.
Key Features:
- Target residue and organism: Predicts O-linked glycosylation sites on threonine residues in Homo sapiens proteins.
- Feature encoding: Integrates seven distinct feature coding methods to represent sample sequences comprehensively.
- Classifier: Uses a random forest classifier selected after evaluation of various algorithms.
- Training data: Built from collected and curated high-quality human protein data with known O-linked threonine glycosylation sites.
- Validation and evaluation: Validated by rigorous 5-fold cross-validation and assessment on an independent validation dataset.
- Performance metrics: Achieved AUC 0.9308 on the training set and AUC 0.9323 on an independent validation dataset, and ACC 0.8475 on an independent test dataset.
- Comparative benchmarking: Compared against previously published predictors, achieving the highest reported ACC of 0.8475 on an independent test dataset.
Scientific Applications:
- Glycosite identification: Enables identification of O-glycosites on threonine residues in human proteins for glycobiology research.
- Glycosylation structure–function studies: Supports studies of glycosylation structure and function in cellular metabolic and signaling pathways.
Methodology:
Collected and curated human protein data with known O-linked threonine glycosylation sites; encoded sequences with seven feature coding methods; trained a random forest classifier after algorithm evaluation; validated using 5-fold cross-validation and an independent validation dataset.
Topics
Details
- Cost:
- Free of charge
- Tool Type:
- desktop application
- Operating Systems:
- Mac, Windows, Linux
- Added:
- 1/22/2024
- Last Updated:
- 1/22/2024
Operations
Data Inputs & Outputs
PTM localisation
Inputs
Outputs
Publications
Tang H, Tang Q, Zhang Q, Feng P. O-GlyThr: Prediction of human O-linked threonine glycosites using multi-feature fusion. International Journal of Biological Macromolecules. 2023;242:124761. doi:10.1016/j.ijbiomac.2023.124761. PMID:37156312.