Reversible protein phosphorylation is a ubiquitous posttranslational modification in all eukaryotes. It is critically involved in the regulation of nearly all cellular processes and signaling pathways. Protein kinases, the enzymes that catalyze the phosphotransfer reaction, constitute one of the largest protein families, accounting for approximately 2 % of the genes in any given eukaryotic genome (122). Few of these kinases are constitutively active; unregulated activity would be deleterious or lethal to cells in the cases of most protein kinases. Cells have thus developed a variety of finely tuned mechanisms to precisely control the activities of these enzymes. We aim here to characterize the regulatory mechanisms governing the activities of protein kinases in Saccharomyces cerevisiae on a genome-wide scale. We do not attempt to review comprehensively the substrates, target sequences, o
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