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PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates
Protein phosphorylation catalysed by kinases plays crucial regulatory roles in intracellular signal transduction. With the increasing number of kinase-specific phosphorylation sites and disease-related phosphorylation substrates that have been identified, the desire to explore the regulatory relatio...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3970127/ https://www.ncbi.nlm.nih.gov/pubmed/24681538 http://dx.doi.org/10.1038/srep04524 |
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author | Suo, Sheng-Bao Qiu, Jian-Ding Shi, Shao-Ping Chen, Xiang Liang, Ru-Ping |
author_facet | Suo, Sheng-Bao Qiu, Jian-Ding Shi, Shao-Ping Chen, Xiang Liang, Ru-Ping |
author_sort | Suo, Sheng-Bao |
collection | PubMed |
description | Protein phosphorylation catalysed by kinases plays crucial regulatory roles in intracellular signal transduction. With the increasing number of kinase-specific phosphorylation sites and disease-related phosphorylation substrates that have been identified, the desire to explore the regulatory relationship between protein kinases and disease-related phosphorylation substrates is motivated. In this work, we analysed the kinases' characteristic of all disease-related phosphorylation substrates by using our developed Phosphorylation Set Enrichment Analysis (PSEA) method. We evaluated the efficiency of our method with independent test and concluded that our approach is reliable for identifying kinases responsible for phosphorylated substrates. In addition, we found that Mitogen-activated protein kinase (MAPK) and Glycogen synthase kinase (GSK) families are more associated with abnormal phosphorylation. It can be anticipated that our method might be helpful to identify the mechanism of phosphorylation and the relationship between kinase and phosphorylation related diseases. A user-friendly web interface is now freely available at http://bioinfo.ncu.edu.cn/PKPred_Home.aspx. |
format | Online Article Text |
id | pubmed-3970127 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-39701272014-04-01 PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates Suo, Sheng-Bao Qiu, Jian-Ding Shi, Shao-Ping Chen, Xiang Liang, Ru-Ping Sci Rep Article Protein phosphorylation catalysed by kinases plays crucial regulatory roles in intracellular signal transduction. With the increasing number of kinase-specific phosphorylation sites and disease-related phosphorylation substrates that have been identified, the desire to explore the regulatory relationship between protein kinases and disease-related phosphorylation substrates is motivated. In this work, we analysed the kinases' characteristic of all disease-related phosphorylation substrates by using our developed Phosphorylation Set Enrichment Analysis (PSEA) method. We evaluated the efficiency of our method with independent test and concluded that our approach is reliable for identifying kinases responsible for phosphorylated substrates. In addition, we found that Mitogen-activated protein kinase (MAPK) and Glycogen synthase kinase (GSK) families are more associated with abnormal phosphorylation. It can be anticipated that our method might be helpful to identify the mechanism of phosphorylation and the relationship between kinase and phosphorylation related diseases. A user-friendly web interface is now freely available at http://bioinfo.ncu.edu.cn/PKPred_Home.aspx. Nature Publishing Group 2014-03-31 /pmc/articles/PMC3970127/ /pubmed/24681538 http://dx.doi.org/10.1038/srep04524 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-nd/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported license. The images in this article are included in the article's Creative Commons license, unless indicated otherwise in the image credit; if the image is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the image. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/ |
spellingShingle | Article Suo, Sheng-Bao Qiu, Jian-Ding Shi, Shao-Ping Chen, Xiang Liang, Ru-Ping PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates |
title | PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates |
title_full | PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates |
title_fullStr | PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates |
title_full_unstemmed | PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates |
title_short | PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates |
title_sort | psea: kinase-specific prediction and analysis of human phosphorylation substrates |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3970127/ https://www.ncbi.nlm.nih.gov/pubmed/24681538 http://dx.doi.org/10.1038/srep04524 |
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