This article is about the term in molecular biology. For the plant and food, see
Zanthoxylum piperitum.
In
molecular biology,
biochemistry and
cell signaling the kinome of an organism is the complete set of
protein kinases encoded in its
genome. Kinases are usually
enzymes that catalyze
phosphorylation reactions (of amino acids) and fall into several groups and families, e.g., those that phosphorylate the
amino acidsserine 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 refers to both protein kinases and protein
pseudokinases[1] and their evolution of protein kinases throughout the eukaryotes.[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.[9]
In animals, the kinome includes kinases that phosphorylate only tyrosine (tyrosine kinases), those that act on serine or threonine, and a few classes, such as
GSK3 and
MAP2K that can act on both.[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.[citation needed]
^Reiterer V, Eyers PA, Farhan H (2014). "Day of the dead: pseudokinases and pseudophosphatases in physiology and disease". Trends in Cell Biology. 24 (9): 489–505.
doi:
10.1016/j.tcb.2014.03.008.
PMID24818526.