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||P.1240 left column 2nd paragraph: "Protein phosphorylation is the most abundant post-translational modification that may alter the structure, function, localization, molecular interactions, or degradation of a protein (Nishi et al. 2014), and may therefore function as a molecular switch or rheostat of enzyme activity (Chen and Nielsen 2016). The importance of this level of regulation is highlighted by the fact that up to 23% of intracellular ATP may be utilized by protein kinases for phosphorylating their numerous targets (primary sources). Furthermore, this type of regulation is expected to be tightly controlled, otherwise the ATP supply would be rapidly depleted (Krebs and Stull 1975). The identification of crucial p-sites in key proteins offers synthetic biologists the prospect of manipulating molecular pathways or organismal phenotypes with greater precision than can be achieved by either the deletion or under/overexpression of complete genes (Oliveira et al. 2012 Oliveira and Sauer 2012)."