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• W2896876179 abstract "Abstract Protein kinases catalyse the phosphorylation of target proteins, controlling most cellular processes. The specificity of serine/threonine kinases is partly determined by interactions with a few residues near the phospho-acceptor residue, forming the so-called kinase substrate motif. Kinases have been extensively duplicated throughout evolution but little is known about when in time new target motifs have arisen. Here we show that sequence variation occurring early in the evolution of kinases is dominated by changes in specificity determining residues. We then analysed kinase specificity models, based on known target sites, observing that specificity has remained mostly unchanged for recent kinase duplications. Finally, analysis of phosphorylation data from a taxonomically broad set of 48 eukaryotic species indicates that most phosphorylation motifs are broadly distributed in eukaryotes but not present in prokaryotes. Overall, our results suggest that the set of eukaryotes kinase motifs present today was acquired soon after the eukaryotic last common ancestor and that early expansions of the protein kinase fold rapidly explored the space of possible target motifs." @default.
• W2896876179 created "2018-10-26" @default.
• W2896876179 creator A5031240113 @default.
• W2896876179 creator A5050058340 @default.
• W2896876179 date "2018-10-16" @default.
• W2896876179 modified "2023-09-26" @default.
• W2896876179 title "Evolution of protein kinase substrate recognition at the active site" @default.
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• W2896876179 doi "https://doi.org/10.1101/443945" @default.
• W2896876179 hasPublicationYear "2018" @default.
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