TIMM10

From Wikipedia, the free encyclopedia

Translocase of inner mitochondrial membrane 10 homolog (yeast)

PDB rendering based on 2bsk.

Available structures: 2bsk

Identifiers

Symbol(s)

TIMM10; TIM10; TIM10A

External IDs

OMIM: 602251 MGI: 1353429 HomoloGene: 40845

Gene ontology
Molecular Function:	• zinc ion binding • metal ion binding
Cellular Component:	• mitochondrion • mitochondrial inner membrane presequence translocase complex • membrane • mitochondrial intermembrane space protein transporter complex
Biological Process:	• protein folding • sensory perception of sound • protein transport • protein import into mitochondrial inner membrane

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012456 (mRNA)
NP_036588 (protein)

NM_013899 (mRNA)
NP_038927 (protein)

Location

Chr 11: 57.05 - 57.05 Mb

Chr 2: 84.63 - 84.63 Mb

Pubmed search

[1]

[2]

Translocase of inner mitochondrial membrane 10 homolog (yeast), also known as TIMM10, is a human gene.^[1]

TIMM10 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

^ ^a ^b Entrez Gene: TIMM10 translocase of inner mitochondrial membrane 10 homolog (yeast).

[edit] Further reading

Koehler CM, Jarosch E, Tokatlidis K, et al. (1998). "Import of mitochondrial carriers mediated by essential proteins of the intermembrane space.". Science 279 (5349): 369–73. PMID 9430585.
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:10.1006/geno.1999.5966. PMID 10552927.
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.
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.
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.
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. PMID 12477932.
Allen S, Lu H, Thornton D, Tokatlidis K (2003). "Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10.". J. Biol. Chem. 278 (40): 38505–13. doi:10.1074/jbc.M306027200. PMID 12882976.
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:10.1074/jbc.M312485200. PMID 14726512.
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. PMID 15489334.
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.
Carey KA, Segal D, Klein R, et al. (2006). "Identification of novel genes expressed during rhabdomyosarcoma differentiation using cDNA microarrays.". Pathol. Int. 56 (5): 246–55. doi:10.1111/j.1440-1827.2006.01958.x. PMID 16669873.