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PhosContext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction
Phosphorylation is the most important type of protein post-translational modification. Accordingly, reliable identification of kinase-mediated phosphorylation has important implications for functional annotation of phosphorylated substrates and characterization of cellular signalling pathways. The l...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5974293/ https://www.ncbi.nlm.nih.gov/pubmed/29844483 http://dx.doi.org/10.1038/s41598-018-26392-7 |
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author | Xu, Ying Song, Jiangning Wilson, Campbell Whisstock, James C. |
author_facet | Xu, Ying Song, Jiangning Wilson, Campbell Whisstock, James C. |
author_sort | Xu, Ying |
collection | PubMed |
description | Phosphorylation is the most important type of protein post-translational modification. Accordingly, reliable identification of kinase-mediated phosphorylation has important implications for functional annotation of phosphorylated substrates and characterization of cellular signalling pathways. The local sequence context surrounding potential phosphorylation sites is considered to harbour the most relevant information for phosphorylation site prediction models. However, currently there is a lack of condensed vector representation for this important contextual information, despite the presence of varying residue-level features that can be constructed from sequence homology profiles, structural information, and physicochemical properties. To address this issue, we present PhosContext2vec which is a distributed representation of residue-level sequence contexts for potential phosphorylation sites and demonstrate its application in both general and kinase-specific phosphorylation site predictions. Benchmarking experiments indicate that PhosContext2vec could achieve promising predictive performance compared with several other existing methods for phosphorylation site prediction. We envisage that PhosContext2vec, as a new sequence context representation, can be used in combination with other informative residue-level features to improve the classification performance in a number of related bioinformatics tasks that require appropriate residue-level feature vector representation and extraction. The web server of PhosContext2vec is publicly available at http://phoscontext2vec.erc.monash.edu/. |
format | Online Article Text |
id | pubmed-5974293 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-59742932018-05-31 PhosContext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction Xu, Ying Song, Jiangning Wilson, Campbell Whisstock, James C. Sci Rep Article Phosphorylation is the most important type of protein post-translational modification. Accordingly, reliable identification of kinase-mediated phosphorylation has important implications for functional annotation of phosphorylated substrates and characterization of cellular signalling pathways. The local sequence context surrounding potential phosphorylation sites is considered to harbour the most relevant information for phosphorylation site prediction models. However, currently there is a lack of condensed vector representation for this important contextual information, despite the presence of varying residue-level features that can be constructed from sequence homology profiles, structural information, and physicochemical properties. To address this issue, we present PhosContext2vec which is a distributed representation of residue-level sequence contexts for potential phosphorylation sites and demonstrate its application in both general and kinase-specific phosphorylation site predictions. Benchmarking experiments indicate that PhosContext2vec could achieve promising predictive performance compared with several other existing methods for phosphorylation site prediction. We envisage that PhosContext2vec, as a new sequence context representation, can be used in combination with other informative residue-level features to improve the classification performance in a number of related bioinformatics tasks that require appropriate residue-level feature vector representation and extraction. The web server of PhosContext2vec is publicly available at http://phoscontext2vec.erc.monash.edu/. Nature Publishing Group UK 2018-05-29 /pmc/articles/PMC5974293/ /pubmed/29844483 http://dx.doi.org/10.1038/s41598-018-26392-7 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Xu, Ying Song, Jiangning Wilson, Campbell Whisstock, James C. PhosContext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction |
title | PhosContext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction |
title_full | PhosContext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction |
title_fullStr | PhosContext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction |
title_full_unstemmed | PhosContext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction |
title_short | PhosContext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction |
title_sort | phoscontext2vec: a distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5974293/ https://www.ncbi.nlm.nih.gov/pubmed/29844483 http://dx.doi.org/10.1038/s41598-018-26392-7 |
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