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      Using multitask classification methods to investigate the kinase-specific phosphorylation sites

      research-article
      1 , 2 , 1 , 1 ,
      Proteome Science
      BioMed Central
      IEEE International Conference on Bioinformatics and Biomedicine 2011
      12-15 November 2011

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          Abstract

          Background

          Identification of phosphorylation sites by computational methods is becoming increasingly important because it reduces labor-intensive and costly experiments and can improve our understanding of the common properties and underlying mechanisms of protein phosphorylation.

          Methods

          A multitask learning framework for learning four kinase families simultaneously, instead of studying each kinase family of phosphorylation sites separately, is presented in the study. The framework includes two multitask classification methods: the Multi-Task Least Squares Support Vector Machines (MTLS-SVMs) and the Multi-Task Feature Selection (MT-Feat3).

          Results

          Using the multitask learning framework, we successfully identify 18 common features shared by four kinase families of phosphorylation sites. The reliability of selected features is demonstrated by the consistent performance in two multi-task learning methods.

          Conclusions

          The selected features can be used to build efficient multitask classifiers with good performance, suggesting they are important to protein phosphorylation across 4 kinase families.

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          Most cited references13

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          The protein kinase complement of the human genome.

          G. Manning (2002)
          We have catalogued the protein kinase complement of the human genome (the "kinome") using public and proprietary genomic, complementary DNA, and expressed sequence tag (EST) sequences. This provides a starting point for comprehensive analysis of protein phosphorylation in normal and disease states, as well as a detailed view of the current state of human genome analysis through a focus on one large gene family. We identify 518 putative protein kinase genes, of which 71 have not previously been reported or described as kinases, and we extend or correct the protein sequences of 56 more kinases. New genes include members of well-studied families as well as previously unidentified families, some of which are conserved in model organisms. Classification and comparison with model organism kinomes identified orthologous groups and highlighted expansions specific to human and other lineages. We also identified 106 protein kinase pseudogenes. Chromosomal mapping revealed several small clusters of kinase genes and revealed that 244 kinases map to disease loci or cancer amplicons.
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            Two-component signal transduction.

            Most prokaryotic signal-transduction systems and a few eukaryotic pathways use phosphotransfer schemes involving two conserved components, a histidine protein kinase and a response regulator protein. The histidine protein kinase, which is regulated by environmental stimuli, autophosphorylates at a histidine residue, creating a high-energy phosphoryl group that is subsequently transferred to an aspartate residue in the response regulator protein. Phosphorylation induces a conformational change in the regulatory domain that results in activation of an associated domain that effects the response. The basic scheme is highly adaptable, and numerous variations have provided optimization within specific signaling systems. The domains of two-component proteins are modular and can be integrated into proteins and pathways in a variety of ways, but the core structures and activities are maintained. Thus detailed analyses of a relatively small number of representative proteins provide a foundation for understanding this large family of signaling proteins.
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              • Record: found
              • Abstract: found
              • Article: found
              Is Open Access

              AAindex: amino acid index database, progress report 2008

              AAindex is a database of numerical indices representing various physicochemical and biochemical properties of amino acids and pairs of amino acids. We have added a collection of protein contact potentials to the AAindex as a new section. Accordingly AAindex consists of three sections now: AAindex1 for the amino acid index of 20 numerical values, AAindex2 for the amino acid substitution matrix and AAindex3 for the statistical protein contact potentials. All data are derived from published literature. The database can be accessed through the DBGET/LinkDB system at GenomeNet (http://www.genome.jp/dbget-bin/www_bfind?aaindex) or downloaded by anonymous FTP (ftp://ftp.genome.jp/pub/db/community/aaindex/).
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                Author and article information

                Conference
                Proteome Sci
                Proteome Sci
                Proteome Science
                BioMed Central
                1477-5956
                2012
                21 June 2012
                : 10
                : Suppl 1
                : S7
                Affiliations
                [1 ]Applied Bioinformatics Laboratory, Kansas University, 2034 Becker Dr., Lawrence, KS 66047, USA
                [2 ]Institute of Scientific and Technical Information of China, No. 15 Fuxing Road, Haidian District, Beijing 100038, P.R. China
                Article
                1477-5956-10-S1-S7
                10.1186/1477-5956-10-S1-S7
                3380725
                22759584
                6ac49ce4-89f0-4390-87b1-2a12ff7e2997
                Copyright ©2012 Gao et al; licensee BioMed Central Ltd.

                This is an open access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                IEEE International Conference on Bioinformatics and Biomedicine 2011
                Atlanta, GA, USA
                12-15 November 2011
                History
                Categories
                Proceedings

                Molecular biology
                Molecular biology

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