Publication | Closed Access
GPS 2.1: enhanced prediction of kinase-specific phosphorylation sites with an algorithm of motif length selection
262
Citations
11
References
2010
Year
Biomolecular Structure PredictionGps 2.1Molecular BiologyReceptor Tyrosine KinaseMotif Length SelectionComputational PredictionProteomicsCell SignalingBiochemistryKinase-specific Phosphorylation SitesProtein ModelingProtein Structure PredictionPathway AnalysisFunctional GenomicsBioinformaticsProtein BioinformaticsStructural BiologyProtein PhosphorylationSignal TransductionNatural SciencesComputational BiologyCellular BiochemistrySystems BiologyMedicine
As the most important post-translational modification of proteins, phosphorylation plays essential roles in all aspects of biological processes. Besides experimental approaches, computational prediction of phosphorylated proteins with their kinase-specific phosphorylation sites has also emerged as a popular strategy, for its low-cost, fast-speed and convenience. In this work, we developed a kinase-specific phosphorylation sites predictor of GPS 2.1 (Group-based Prediction System), with a novel but simple approach of motif length selection (MLS). By this approach, the robustness of the prediction system was greatly improved. All algorithms in GPS old versions were also reserved and integrated in GPS 2.1. The online service and local packages of GPS 2.1 were implemented in JAVA 1.5 (J2SE 5.0) and freely available for academic researches at: http://gps.biocuckoo.org.
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