In
molecular biology, the
kinome of an organism is the set of
protein kinases in its
genome. Kinases are
enzymes that catalyze
phosphorylation reactions (of amino acids) and fall into several groups and families, e.g., those that phosphorylate the
amino acids serine and
threonine, those that phosphorylate
tyrosine and some that can phosphorylate both, such as the MAP2K and GSK families. The term was first used in 2002 by Gerard Manning and colleagues in twin papers analyzing the 518 human protein kinases and the evolution of protein kinases throughout eukaryotes. Other kinomes have been determined for rice, several fungi, nematodes, and insects,
sea urchins,
Dictyostelium discoideum, and the process of infection by
Mycobacterium tuberculosis. Although the primary sequence of kinases shows substantial divergence between unrelated eukaryotes, variation in the motifs that are actually phosphorylated by eukaryotic kinases is much smaller.