Literature DB >> 21062758

GPS 2.1: enhanced prediction of kinase-specific phosphorylation sites with an algorithm of motif length selection.

Yu Xue1, Zexian Liu, Jun Cao, Qian Ma, Xinjiao Gao, Qingqi Wang, Changjiang Jin, Yanhong Zhou, Longping Wen, Jian Ren.   

Abstract

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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Year:  2010        PMID: 21062758     DOI: 10.1093/protein/gzq094

Source DB:  PubMed          Journal:  Protein Eng Des Sel        ISSN: 1741-0126            Impact factor:   1.650


  108 in total

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Authors:  Joanna Boruc; Annika K Weimer; Virginie Stoppin-Mellet; Evelien Mylle; Ken Kosetsu; Cesyen Cedeño; Michel Jaquinod; Maria Njo; Liesbeth De Milde; Peter Tompa; Nathalie Gonzalez; Dirk Inzé; Tom Beeckman; Marylin Vantard; Daniël Van Damme
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9.  Conformational stability and catalytic activity of PTEN variants linked to cancers and autism spectrum disorders.

Authors:  Sean B Johnston; Ronald T Raines
Journal:  Biochemistry       Date:  2015-02-13       Impact factor: 3.162

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