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TIMM10
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2BSK
Identifiers
Aliases	TIMM10, TIM10, TIM10A, translocase of inner mitochondrial membrane 10 homolog (yeast), translocase of inner mitochondrial membrane 10, TIMM10A
External IDs	OMIM: 602251; MGI: 1353429; HomoloGene: 40845; GeneCards: TIMM10; OMA:TIMM10 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q12.1 Start 57,528,464 bp End 57,530,803 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 D Start 84,657,341 bp End 84,660,557 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gingival epithelium prefrontal cortex muscle of thigh islet of Langerhans gastrocnemius muscle anterior cingulate cortex apex of heart tendon of biceps brachii right lobe of liver biceps brachii Top expressed in facial motor nucleus myocardium of ventricle right ventricle morula endocardial cushion atrioventricular valve digastric muscle embryo soleus muscle cardiac muscles More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding chaperone binding protein binding protein homodimerization activity metal ion binding transporter activity Cellular component mitochondrial inner membrane mitochondrial intermembrane space TIM23 mitochondrial import inner membrane translocase complex mitochondrial intermembrane space protein transporter complex membrane mitochondrion TIM22 mitochondrial import inner membrane insertion complex Biological process protein transport protein insertion into mitochondrial inner membrane protein targeting to mitochondrion hearing Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 26519 30059 Ensembl ENSG00000134809 ENSMUSG00000027076 UniProt P62072 P62073 RefSeq (mRNA) NM_012456 NM_013899 RefSeq (protein) NP_036588 NP_038927 Location (UCSC) Chr 11: 57.53 – 57.53 Mb Chr 2: 84.66 – 84.66 Mb PubMed search
Wikidata
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Mitochondrial import inner membrane translocase subunit Tim10 is an enzyme that in humans is encoded by the TIMM10 gene.

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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000134809 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000027076 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. ^ "Entrez Gene: TIMM10 translocase of inner mitochondrial membrane 10 homolog (yeast)".

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. doi:10.1126/science.279.5349.369. PMID 9430585.
• 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. S2CID 27484018.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. PMC 528928. 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. S2CID 29365940.

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