PROSITE documentation PDOC51545Phosphatidylinositol kinase (PIK) helical domain profile
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Bosotti R. Isacchi A. Sonnhammer E.L. |
| Title | FAT: a novel domain in PIK-related kinases. | |
| Source | Trends Biochem. Sci. 25:225-227(2000). | |
| PubMed ID | 10782091 |
| 2 | Authors | Meijer H.J.G. Govers F. |
| Title | Genomewide analysis of phospholipid signaling genes in Phytophthora spp.: novelties and a missing link. | |
| Source | Mol. Plant Microbe Interact. 19:1337-1347(2006). | |
| PubMed ID | 17153918 | |
| DOI | 10.1094/MPMI-19-1337 |
| 3 | Authors | Domin J. Waterfield M.D. |
| Title | Using structure to define the function of phosphoinositide 3-kinase family members. | |
| Source | FEBS Lett. 410:91-95(1997). | |
| PubMed ID | 9247130 |
| 4 | Authors | Huang C.-H. Mandelker D. Schmidt-Kittler O. Samuels Y. Velculescu V.E. Kinzler K.W. Vogelstein B. Gabelli S.B. Amzel L.M. |
| Title | The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations. | |
| Source | Science 318:1744-1748(2007). | |
| PubMed ID | 18079394 | |
| DOI | 10.1126/science.1150799 |
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