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An ensemble method approach to investigate kinase-specific phosphorylation sites

Authors Datta S, Mukhopadhyay S

Received 13 November 2013

Accepted for publication 29 January 2014

Published 10 May 2014 Volume 2014:9(1) Pages 2225—2239


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Sutapa Datta, Subhasis Mukhopadhyay

Department of Biophysics, Molecular Biology and Bioinformatics and Distributed Information Centre for Bioinformatics, University of Calcutta, West Bengal, India

Abstract: Protein phosphorylation is one of the most significant and well-studied post-translational modifications, and it plays an important role in various cellular processes. It has made a considerable impact in understanding the protein functions which are involved in revealing signal transductions and various diseases. The identification of kinase-specific phosphorylation sites has an important role in elucidating the mechanism of phosphorylation; however, experimental techniques for identifying phosphorylation sites are labor intensive and expensive. An exponentially increasing number of protein sequences generated by various laboratories across the globe require computer-aided procedures for reliably and quickly identifying the phosphorylation sites, opening a new horizon for in silico analysis. In this regard, we have introduced a novel ensemble method where we have selected three classifiers (least square support vector machine, multilayer perceptron, and k-Nearest Neighbor) and three different feature encoding parameters (dipeptide composition, physicochemical properties of amino acids, and protein–protein similarity score). Each of these classifiers is trained on each of the three different parameter systems. The final results of the ensemble method are obtained by fusing the results of all the classifiers by a weighted voting algorithm. Extensive experiments reveal that our proposed method can successfully predict phosphorylation sites in a kinase-specific manner and performs significantly better when compared with other existing phosphorylation site prediction methods.

Keywords: post-translational modification, cell signaling, phosphate

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