In molecular biology, biochemistry and cell signaling the kinome of an organism is the complete set of protein kinases encoded in its genome.
[2] Other kinomes have been determined for rice,[3] several fungi, nematodes, and insects, sea urchins,[4] Dictyostelium discoideum,[5] and the process of infection by Mycobacterium tuberculosis.
[6] Although the primary sequence of protein kinases shows substantial divergence between unrelated eukaryotes, and amino acid differences in catalytic motifs have permitted their separation of kinomes into canonical and pseudokinase subtypes,[7] the variation found in the amino acid motifs adjacent to the site of actual phosphorylation of substrates by eukaryotic kinases is much smaller.
[8] As kinases are a major drug target and a major control point in cell behavior, the kinome has also been the target of large scale functional genomics with RNAi screens and of drug discovery efforts, especially in cancer therapeutics.
[citation needed] Research has shown that there are specialized protein domains that bind to phosphorylated serine and threonine residues, such as BRCA and FHA domains.