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PROSITE documentation PDOC51545 [for PROSITE entry PS51545]
Phosphatidylinositol kinase (PIK) helical domain profile


Description

Phosphatidylinositol kinases are found in all eukaryotes and serve important functions in phosphatidylinositol (PI) signaling pathways. All PI3Ks and PI4Ks contain a conserved PI-kinase domain (see <PDOC00710>), and most have various additional domains that are involved in protein-protein or phospholipid-protein interactions [1,2]. The phosphoinositide kinase (PIK) domain is a region conserved among all PI3 and PI4-kinases and although its role is presently unclear, it is likely to be involved in substrate presentation [3].

The PIK domain folds as an all α-helical structure (see <PDB:2RD0>) [4].

The profile we developed covers the entire PIK helical domain.

Last update:

August 2011 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

PIK_HELICAL, PS51545; PIK helical domain profile  (MATRIX)


References

1AuthorsBosotti R. Isacchi A. Sonnhammer E.L.
TitleFAT: a novel domain in PIK-related kinases.
SourceTrends Biochem. Sci. 25:225-227(2000).
PubMed ID10782091

2AuthorsMeijer H.J.G. Govers F.
TitleGenomewide analysis of phospholipid signaling genes in Phytophthora spp.: novelties and a missing link.
SourceMol. Plant Microbe Interact. 19:1337-1347(2006).
PubMed ID17153918
DOI10.1094/MPMI-19-1337

3AuthorsDomin J. Waterfield M.D.
TitleUsing structure to define the function of phosphoinositide 3-kinase family members.
SourceFEBS Lett. 410:91-95(1997).
PubMed ID9247130

4AuthorsHuang C.-H. Mandelker D. Schmidt-Kittler O. Samuels Y. Velculescu V.E. Kinzler K.W. Vogelstein B. Gabelli S.B. Amzel L.M.
TitleThe structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations.
SourceScience 318:1744-1748(2007).
PubMed ID18079394
DOI10.1126/science.1150799



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