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PROSITE documentation PDOC51545

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.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

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



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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