|PROSITE documentation PDOC51455 [for PROSITE entry PS51455]|
Phosphoinositides (PIs) are central to signal transduction and membrane trafficking in all eukaryotes. They are derived from phosphatidylinositol (PtdIns) as the result of phosphorylation of hydroxyl groups at positions 3, 4 or 5 of the PtdIns head group. Phosphatidylinositol phosphate kinases (PIPKs) phosphorylate phosphatidylinositol phosphate (PtdInsP) to phosphatidylinositol bisphosphate (PtdInsP2). Three types of PIPKs are present throughout the eukaryotic kingdoms. Type I (PtdIns4P 5-kinase) and type II (PtdIns5P 4-kinase) generate PtdIns(4,5)P2 from PtdIns4P and PtdIns5P, respectively. Type III PIPK (PtdIns3P 5-kinases) are distinct from the type I and II PIPKs and synthesize PtdIns(3,5)P2 [1,2,3].
The basic structure of PIPKs shared by animals, yeast and plant PIPks consists of a highly conserved central kinase domain and a dimerization domain. PIPK domains have high sequence identity, well-defined motifs and conserved residues. They consist of two α+β subdomains (see <PDB:1BO1>]. The larger N-terminal subdomain contains a seven-stranded antiparallel β sheet and four helices. The C-terminal subdomain contains a five-stranded antiparallel β sheet and four helices .
The profile we developed covers the entire PIPK domain.Last update:
June 2009 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Bakthavatsalam D., Meijer H.J.G., Noegel A.A., Govers F.|
|Title||Novel phosphatidylinositol phosphate kinases with a G-protein coupled receptor signature are shared by Dictyostelium and Phytophthora.|
|Source||Trends Microbiol. 14:378-382(2006).|
|2||Authors||Heck J.N., Mellman D.L., Ling K., Sun Y., Wagoner M.P., Schill N.J., Anderson R.A.|
|Title||A conspicuous connection: structure defines function for the phosphatidylinositol-phosphate kinase family.|
|Source||Crit. Rev. Biochem. Mol. Biol. 42:15-39(2007).|
|3||Authors||Saavedra L., Balbi V., Dove S.K., Hiwatashi Y., Mikami K., Sommarin M.|
|Title||Characterization of phosphatidylinositol phosphate kinases from the moss Physcomitrella patens: PpPIPK1 and PpPIPK2.|
|Source||Plant Cell Physiol. 50:595-609(2009).|
|4||Authors||Rao V.D., Misra S., Boronenkov I.V., Anderson R.A., Hurley J.H.|
|Title||Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation.|