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Prediction of Protein Phosphorylation Sites by Using the Composition of k-Spaced Amino Acid Pairs
As one of the most widespread protein post-translational modifications, phosphorylation is involved in many biological processes such as cell cycle, apoptosis. Identification of phosphorylated substrates and their corresponding sites will facilitate the understanding of the molecular mechanism of ph...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3478286/ https://www.ncbi.nlm.nih.gov/pubmed/23110047 http://dx.doi.org/10.1371/journal.pone.0046302 |
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author | Zhao, Xiaowei Zhang, Wenyi Xu, Xin Ma, Zhiqiang Yin, Minghao |
author_facet | Zhao, Xiaowei Zhang, Wenyi Xu, Xin Ma, Zhiqiang Yin, Minghao |
author_sort | Zhao, Xiaowei |
collection | PubMed |
description | As one of the most widespread protein post-translational modifications, phosphorylation is involved in many biological processes such as cell cycle, apoptosis. Identification of phosphorylated substrates and their corresponding sites will facilitate the understanding of the molecular mechanism of phosphorylation. Comparing with the labor-intensive and time-consuming experiment approaches, computational prediction of phosphorylation sites is much desirable due to their convenience and fast speed. In this paper, a new bioinformatics tool named CKSAAP_PhSite was developed that ignored the kinase information and only used the primary sequence information to predict protein phosphorylation sites. The highlight of CKSAAP_PhSite was to utilize the composition of k-spaced amino acid pairs as the encoding scheme, and then the support vector machine was used as the predictor. The performance of CKSAAP_PhSite was measured with a sensitivity of 84.81%, a specificity of 86.07% and an accuracy of 85.43% for serine, a sensitivity of 78.59%, a specificity of 82.26% and an accuracy of 80.31% for threonine as well as a sensitivity of 74.44%, a specificity of 78.03% and an accuracy of 76.21% for tyrosine. Experimental results obtained from cross validation and independent benchmark suggested that our method was very promising to predict phosphorylation sites and can be served as a useful supplement tool to the community. For public access, CKSAAP_PhSite is available at http://59.73.198.144/cksaap_phsite/. |
format | Online Article Text |
id | pubmed-3478286 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34782862012-10-29 Prediction of Protein Phosphorylation Sites by Using the Composition of k-Spaced Amino Acid Pairs Zhao, Xiaowei Zhang, Wenyi Xu, Xin Ma, Zhiqiang Yin, Minghao PLoS One Research Article As one of the most widespread protein post-translational modifications, phosphorylation is involved in many biological processes such as cell cycle, apoptosis. Identification of phosphorylated substrates and their corresponding sites will facilitate the understanding of the molecular mechanism of phosphorylation. Comparing with the labor-intensive and time-consuming experiment approaches, computational prediction of phosphorylation sites is much desirable due to their convenience and fast speed. In this paper, a new bioinformatics tool named CKSAAP_PhSite was developed that ignored the kinase information and only used the primary sequence information to predict protein phosphorylation sites. The highlight of CKSAAP_PhSite was to utilize the composition of k-spaced amino acid pairs as the encoding scheme, and then the support vector machine was used as the predictor. The performance of CKSAAP_PhSite was measured with a sensitivity of 84.81%, a specificity of 86.07% and an accuracy of 85.43% for serine, a sensitivity of 78.59%, a specificity of 82.26% and an accuracy of 80.31% for threonine as well as a sensitivity of 74.44%, a specificity of 78.03% and an accuracy of 76.21% for tyrosine. Experimental results obtained from cross validation and independent benchmark suggested that our method was very promising to predict phosphorylation sites and can be served as a useful supplement tool to the community. For public access, CKSAAP_PhSite is available at http://59.73.198.144/cksaap_phsite/. Public Library of Science 2012-10-22 /pmc/articles/PMC3478286/ /pubmed/23110047 http://dx.doi.org/10.1371/journal.pone.0046302 Text en © 2012 Zhao et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Zhao, Xiaowei Zhang, Wenyi Xu, Xin Ma, Zhiqiang Yin, Minghao Prediction of Protein Phosphorylation Sites by Using the Composition of k-Spaced Amino Acid Pairs |
title | Prediction of Protein Phosphorylation Sites by Using the Composition of k-Spaced Amino Acid Pairs |
title_full | Prediction of Protein Phosphorylation Sites by Using the Composition of k-Spaced Amino Acid Pairs |
title_fullStr | Prediction of Protein Phosphorylation Sites by Using the Composition of k-Spaced Amino Acid Pairs |
title_full_unstemmed | Prediction of Protein Phosphorylation Sites by Using the Composition of k-Spaced Amino Acid Pairs |
title_short | Prediction of Protein Phosphorylation Sites by Using the Composition of k-Spaced Amino Acid Pairs |
title_sort | prediction of protein phosphorylation sites by using the composition of k-spaced amino acid pairs |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3478286/ https://www.ncbi.nlm.nih.gov/pubmed/23110047 http://dx.doi.org/10.1371/journal.pone.0046302 |
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