PhosContext2vec: A distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction

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Abstract

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/.

Original languageEnglish
Article number8240
Number of pages14
JournalScientific Reports
Volume8
Issue number1
DOIs
Publication statusPublished - 1 Dec 2018

Cite this

@article{87fe0caea576461597bc4a1290ac3f8a,
title = "PhosContext2vec: A distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction",
abstract = "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/.",
author = "Ying Xu and Jiangning Song and Campbell Wilson and Whisstock, {James C.}",
year = "2018",
month = "12",
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doi = "10.1038/s41598-018-26392-7",
language = "English",
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journal = "Scientific Reports",
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T2 - A distributed representation of residue-level sequence contexts and its application to general and kinase-specific phosphorylation site prediction

AU - Xu, Ying

AU - Song, Jiangning

AU - Wilson, Campbell

AU - Whisstock, James C.

PY - 2018/12/1

Y1 - 2018/12/1

N2 - 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/.

AB - 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/.

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