Difference between revisions of "Phosphatase Subfamily TIMM50"
From PhosphataseWiki
(→Evolution) |
(→Catalytic activity) |
||
| Line 9: | Line 9: | ||
===Domain Structure=== | ===Domain Structure=== | ||
| − | == Catalytic activity == | + | ===Catalytic activity=== |
None | None | ||
Revision as of 05:32, 29 December 2014
Phosphatase Classification: FCP: TIMM50
TIMM50 (or TIM50) is named after translocase of inner mitochondrial membrane 50 homolog (S. cerevisiae) [1] [2]. It is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes. It lacks the DxDx[T|V] motif at catalytic site.
Evolution
TIMM50 is conserved from yeast to human.
Domain Structure
Catalytic activity
None
Related Kinases
1) Raf. High throughput yeast two-hybrid assay show Raf kinase can interact with TIMM50, as well as FCP1. The paper also guessed Raf is the substrate of TIMM50 [3], but actually TIMM50 lacks the catalytic motif. (Note: Raf also interacts with FCP1 in the paper).
Curation notes
References
- Yamamoto H, Esaki M, Kanamori T, Tamura Y, Nishikawa Si, and Endo T. Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes. Cell. 2002 Nov 15;111(4):519-28. DOI:10.1016/s0092-8674(02)01053-x |
- Meinecke M, Wagner R, Kovermann P, Guiard B, Mick DU, Hutu DP, Voos W, Truscott KN, Chacinska A, Pfanner N, and Rehling P. Tim50 maintains the permeability barrier of the mitochondrial inner membrane. Science. 2006 Jun 9;312(5779):1523-6. DOI:10.1126/science.1127628 |
- Yuryev A and Wennogle LP. Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis. Genomics. 2003 Feb;81(2):112-25. DOI:10.1016/s0888-7543(02)00008-3 |
Links
Human TIMM50 from NCBI Gene
