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DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites
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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802303/ https://www.ncbi.nlm.nih.gov/pubmed/27002216 http://dx.doi.org/10.1038/srep23510 |
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author | Wang, Xiaofeng Yan, Renxiang Song, Jiangning |
author_facet | Wang, Xiaofeng Yan, Renxiang Song, Jiangning |
author_sort | Wang, Xiaofeng |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4802303 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-48023032016-03-23 DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites Wang, Xiaofeng Yan, Renxiang Song, Jiangning Sci Rep Article 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. Nature Publishing Group 2016-03-22 /pmc/articles/PMC4802303/ /pubmed/27002216 http://dx.doi.org/10.1038/srep23510 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Wang, Xiaofeng Yan, Renxiang Song, Jiangning DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites |
title | DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites |
title_full | DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites |
title_fullStr | DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites |
title_full_unstemmed | DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites |
title_short | DephosSite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites |
title_sort | dephossite: a machine learning approach for discovering phosphotase-specific dephosphorylation sites |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802303/ https://www.ncbi.nlm.nih.gov/pubmed/27002216 http://dx.doi.org/10.1038/srep23510 |
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