TIMM9
From Wikipedia, the free encyclopedia
Translocase of inner mitochondrial membrane 9 homolog (yeast)
|
||||||||||||||
PDB rendering based on 2bsk. | ||||||||||||||
Available structures: 2bsk | ||||||||||||||
Identifiers | ||||||||||||||
Symbol(s) | TIMM9; TIM9; TIM9A | |||||||||||||
External IDs | OMIM: 607384 MGI: 1353436 HomoloGene: 40847 | |||||||||||||
|
||||||||||||||
RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 26520 | 30056 | ||||||||||||
Ensembl | ENSG00000100575 | ENSMUSG00000021079 | ||||||||||||
Uniprot | Q9Y5J7 | Q9WV98 | ||||||||||||
Refseq | NM_012460 (mRNA) NP_036592 (protein) |
NM_001024853 (mRNA) NP_001020024 (protein) |
||||||||||||
Location | Chr 14: 57.95 - 57.96 Mb | Chr 12: 72.04 - 72.06 Mb | ||||||||||||
Pubmed search | [1] | [2] |
Translocase of inner mitochondrial membrane 9 homolog (yeast), also known as TIMM9, is a human gene.[1]
TIMM9 belongs to a family of evolutionarily conserved proteins that are organized in heterooligomeric complexes in the mitochondrial intermembrane space. These proteins mediate the import and insertion of hydrophobic membrane proteins into the mitochondrial inner membrane.[supplied by OMIM][1]
[edit] References
[edit] Further reading
- Webb CT, Gorman MA, Lazarou M, et al. (2006). "Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller.". Mol. Cell 21 (1): 123-33. doi: . PMID 16387659.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi: . PMID 15489334.
- Mühlenbein N, Hofmann S, Rothbauer U, Bauer MF (2004). "Organization and function of the small Tim complexes acting along the import pathway of metabolite carriers into mammalian mitochondria.". J. Biol. Chem. 279 (14): 13540-6. doi: . PMID 14726512.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi: . PMID 12477932.
- Vial S, Lu H, Allen S, et al. (2002). "Assembly of Tim9 and Tim10 into a functional chaperone.". J. Biol. Chem. 277 (39): 36100-8. doi: . PMID 12138093.
- Rothbauer U, Hofmann S, Mühlenbein N, et al. (2001). "Role of the deafness dystonia peptide 1 (DDP1) in import of human Tim23 into the inner membrane of mitochondria.". J. Biol. Chem. 276 (40): 37327-34. doi: . PMID 11489896.
- Bauer MF, Rothbauer U, Mühlenbein N, et al. (2000). "The mitochondrial TIM22 preprotein translocase is highly conserved throughout the eukaryotic kingdom.". FEBS Lett. 464 (1-2): 41-7. PMID 10611480.
- Jin H, Kendall E, Freeman TC, et al. (2000). "The human family of Deafness/Dystonia peptide (DDP) related mitochondrial import proteins.". Genomics 61 (3): 259-67. doi: . PMID 10552927.