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

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.

PMID: 37156312
Funding: - Natural Science Foundation of Sichuan Province: 2022NSFSC1770 - Sichuan Province Science and Technology Support Program: 2022YFS0614 - National Natural Science Foundation of China: 62172343