Version 5.4
Mus musculus Protein: Timm8a2
Summary
InnateDB Protein IDBP-188525.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Timm8a2
Protein Name translocase of inner mitochondrial membrane 8 homolog a2 (yeast)
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000047497
InnateDB Gene IDBG-188523 (Timm8a2)
Protein Structure
UniProt Annotation
Function Putative mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). {ECO:0000250}.
Subcellular Localization Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0046872 metal ion binding
Biological Process
GO:0015031 protein transport
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
Protein Structure and Domains
PDB ID MGI:3615492
InterPro IPR004217 Tim10/DDP family zinc finger
PFAM PF02953
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q4FZG7
PhosphoSite PhosphoSite-Q4FZG7
TrEMBL
UniProt Splice Variant
Entrez Gene 223262
UniGene Mm.297637
RefSeq NP_001032833
MGI ID
MGI Symbol Timm8a2
OMIM
CCDS CCDS37020
HPRD
IMGT
EMBL BC099499
GenPept AAH99499

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca