Unknown

Dataset Information

0

DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites.


ABSTRACT: Protein dephosphorylation, which is an inverse process of phosphorylation, plays a crucial role in a myriad of cellular processes, including mitotic cycle, proliferation, differentiation, and cell growth. Compared with tyrosine kinase substrate and phosphorylation site prediction, there is a paucity of studies focusing on computational methods of predicting protein tyrosine phosphatase substrates and dephosphorylation sites. In this work, we developed two elegant models for predicting the substrate dephosphorylation sites of three specific phosphatases, namely, PTP1B, SHP-1, and SHP-2. The first predictor is called MGPS-DEPHOS, which is modified from the GPS (Group-based Prediction System) algorithm with an interpretable capability. The second predictor is called CKSAAP-DEPHOS, which is built through the combination of support vector machine (SVM) and the composition of k-spaced amino acid pairs (CKSAAP) encoding scheme. Benchmarking experiments using jackknife cross validation and 30 repeats of 5-fold cross validation tests show that MGPS-DEPHOS and CKSAAP-DEPHOS achieved AUC values of 0.921, 0.914 and 0.912, for predicting dephosphorylation sites of the three phosphatases PTP1B, SHP-1, and SHP-2, respectively. Both methods outperformed the previously developed kNN-DEPHOS algorithm. In addition, a web server implementing our algorithms is publicly available at http://genomics.fzu.edu.cn/dephossite/ for the research community.

SUBMITTER: Wang X 

PROVIDER: S-EPMC4802303 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites.

Wang Xiaofeng X   Yan Renxiang R   Song Jiangning J  

Scientific reports 20160322


Protein dephosphorylation, which is an inverse process of phosphorylation, plays a crucial role in a myriad of cellular processes, including mitotic cycle, proliferation, differentiation, and cell growth. Compared with tyrosine kinase substrate and phosphorylation site prediction, there is a paucity of studies focusing on computational methods of predicting protein tyrosine phosphatase substrates and dephosphorylation sites. In this work, we developed two elegant models for predicting the substr  ...[more]

Similar Datasets

| S-EPMC8264445 | biostudies-literature
| S-EPMC9219956 | biostudies-literature
| S-EPMC9675776 | biostudies-literature
| S-EPMC2887807 | biostudies-literature
| S-EPMC9887078 | biostudies-literature
| S-EPMC7439510 | biostudies-literature
| S-EPMC6286390 | biostudies-literature
| S-EPMC5905914 | biostudies-other
| S-EPMC7657920 | biostudies-literature
| S-EPMC10839993 | biostudies-literature