Journal article
Prediction of kinase-specific phosphorylation sites through an integrative model of protein context and sequence
R Patrick, C Horin, B Kobe, KAL Cao, M Bodén
Biochimica Et Biophysica Acta Proteins and Proteomics | ELSEVIER | Published : 2016
Abstract
Identifying kinase substrates and the specific phosphorylation sites they regulate is an important factor in understanding protein function regulation and signalling pathways. Computational prediction of kinase targets – assigning kinases to putative substrates, and selecting from protein sequence the sites that kinases can phosphorylate – requires the consideration of both the cellular context that kinases operate in, as well as their binding affinity. This consideration enables investigation of how phosphorylation influences a range of biological processes. We report here a novel probabilistic model for classifying kinase-specific phosphorylation sites from sequence across three model orga..
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Awarded by National Health and Medical Research Council
Funding Acknowledgements
KALC was supported by the National Health and Medical Research Council (NHMRC) Career Development fellowship (APP1087415). BK is a NHMRC Senior Research Fellow (1003326 and 1110971).