Phox homology
Short name | PX_dom |
Overlapping homologous superfamilies | |
domain relationships |
Description
References
1.The PX domain: a new phosphoinositide-binding module. Ellson CD, Andrews S, Stephens LR, Hawkins PT. J. Cell. Sci. 115, 1099-105, (2002). View articlePMID: 11884510
2.A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate. Lock P, Abram CL, Gibson T, Courtneidge SA. EMBO J. 17, 4346-57, (1998). View articlePMID: 9687503
3.Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction. Karathanassis D, Stahelin RV, Bravo J, Perisic O, Pacold CM, Cho W, Williams RL. EMBO J. 21, 5057-68, (2002). View articlePMID: 12356722
4.The Phox homology (PX) domain, a new player in phosphoinositide signalling. Xu Y, Seet LF, Hanson B, Hong W. Biochem. J. 360, 513-30, (2001). View articlePMID: 11736640
5.Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains? Ponting CP. Protein Sci. 5, 2353-7, (1996). View articlePMID: 8931154
6.The phox homology (PX) domain protein interaction network in yeast. Vollert CS, Uetz P. Mol. Cell Proteomics 3, 1053-64, (2004). View articlePMID: 15263065
7.Sorting out the cellular functions of sorting nexins. Worby CA, Dixon JE. Nat. Rev. Mol. Cell Biol. 3, 919-31, (2002). View articlePMID: 12461558
8.Solution structure of the PX domain, a target of the SH3 domain. Hiroaki H, Ago T, Ito T, Sumimoto H, Kohda D. Nat. Struct. Biol. 8, 526-30, (2001). View articlePMID: 11373621
9.The Phox (PX) domain proteins and membrane traffic. Seet LF, Hong W. Biochim. Biophys. Acta 1761, 878-96, (2006). View articlePMID: 16782399
10.Phosphoinositide signaling and the regulation of membrane trafficking in yeast. Odorizzi G, Babst M, Emr SD. Trends Biochem. Sci. 25, 229-35, (2000). View articlePMID: 10782093
GO terms
biological process
- None
molecular function
cellular component
- None