Over half of all cellular proteins are modified by phosphorylation which typically controls their functions.
[1] Protein phosphatomes have been cataloged for human and 8 other key eukaryotes,[1] for Plasmodium and Trypanosomes [2] [3] [4] and phosphatomes have been used for functional analysis, by experimentally investing all known protein phosphatases, in the yeast Fusarium,[5] in Plasmodium [6] and in human cancer [7][8] Large scale databases exist for human and animal phosphatomes Phosphatome.net, parasitic protozoans ProtozPhosDB and for the substrates of human phosphatases DEPOD.
Non-protein phosphorylation has three general forms The human non-protein phosphatome has been cataloged,[1] but most phosphatome analyses are restricted to protein and lipid phosphatases that have regulatory functions.
The phosphatome includes proteins that are structurally closely related to phosphatases but lack catalytic activity.
These retain biological function, and may regulate pathways that involve active phosphatases, or bind to phosphorylated substrates without cleaving them.