TIMM9

Translocase of inner mitochondrial membrane 9 homolog (yeast)

PDB rendering based on 2bsk.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2BSK

Identifiers

Symbols

TIMM9 ; TIM9; TIM9A

External IDs

OMIM: 607384 MGI: 1353436 HomoloGene: 40847 GeneCards: TIMM9 Gene

Gene ontology
Molecular function	• transporter activity • protein binding • zinc ion binding • protein homodimerization activity • chaperone binding
Cellular component	• mitochondrion • mitochondrial inner membrane • mitochondrial intermembrane space • mitochondrial intermembrane space protein transporter complex
Biological process	• protein targeting to mitochondrion • sensory perception of sound • cellular protein metabolic process • protein import into mitochondrial inner membrane • chaperone-mediated protein transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
58.41 – 58.43 Mb

Chr 12:
71.12 – 71.14 Mb

PubMed search

Mitochondrial import inner membrane translocase subunit Tim9 is an enzyme that in humans is encoded by the TIMM9 gene.^[1]^[2]^[3]

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]^[3]

References

↑ Jin H, Kendall E, Freeman TC, Roberts RG, Vetrie DL (Feb 2000). "The human family of Deafness/Dystonia peptide (DDP) related mitochondrial import proteins". Genomics 61 (3): 259–67. doi:10.1006/geno.1999.5966. PMID 10552927.
↑ Muhlenbein N, Hofmann S, Rothbauer U, Bauer MF (Mar 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:10.1074/jbc.M312485200. PMID 14726512.
1 2 "Entrez Gene: TIMM9 translocase of inner mitochondrial membrane 9 homolog (yeast)".

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:10.1016/j.molcel.2005.11.010. 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:10.1101/gr.2596504. PMC 528928. PMID 15489334.
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:10.1073/pnas.242603899. PMC 139241. 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:10.1074/jbc.M202310200. 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:10.1074/jbc.M105313200. 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. doi:10.1016/S0014-5793(99)01665-8. PMID 10611480.

PDB gallery

2bsk: CRYSTAL STRUCTURE OF THE TIM9 TIM10 HEXAMERIC COMPLEX

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TIMM9

References

Further reading