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TIM13 Tim13p

Tim13, Tim13p, TIMM13
This gene encodes a translocase with similarity to yeast mitochondrial proteins that are involved in the import of metabolite transporters from the cytoplasm and into the mitochondrial inner membrane. The encoded protein and the TIMM8a protein form a 70 kDa complex in the intermembrane space. This gene is in a head-to-tail orientation with the gene for lamin B2. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: DDP1, V1a, CAN, 70-kDa, HAD
Papers on Tim13
Early targets of miR-34a in neuroblastoma.
Zollo et al., Napoli, Italy. In Mol Cell Proteomics, 2014
By combining the proteomics data with Kaplan Meier gene-expression studies, we identified seven new gene products (ALG13, TIMM13, TGM2, ABCF2, CTCF, Ki67, and LYAR) that were correlated with worse clinical outcomes.
Reconstitution of the mia40-erv1 oxidative folding pathway for the small tim proteins.
Koehler et al., Los Angeles, United States. In Mol Biol Cell, 2009
Sudies demonstrate that Mia40, Erv1, and oxygen are the minimal machinery for Tim13 oxidation.
Neurological phenotype and reduced lifespan in heterozygous Tim23 knockout mice, the first mouse model of defective mitochondrial import.
Klopstock et al., München, Germany. In Biochim Biophys Acta, 2009
It locates to the inner mitochondrial membrane and its own import is dependent on the DDP1/TIM13 complex.
The Tim8-Tim13 complex has multiple substrate binding sites and binds cooperatively to Tim23.
Koehler et al., Los Angeles, United States. In J Mol Biol, 2008
The central region of Tim23, which enters the intermembrane space first, may serve to nucleate the binding of the Tim8-Tim13 complex, thereby initiating the chaperoned translocation of Tim23 to the mitochondrial inner membrane.
The Tim9p/10p and Tim8p/13p complexes bind to specific sites on Tim23p during mitochondrial protein import.
Johnson et al., College Station, United States. In Mol Biol Cell, 2007
The import of polytopic membrane proteins into the mitochondrial inner membrane (IM) is facilitated by Tim9p/Tim10p and Tim8p/Tim13p protein complexes in the intermembrane space (IMS).
Molecular genetics of a patient with Mohr-Tranebjaerg Syndrome due to a new mutation in the DDP1 gene.
Coria et al., Valencia, Spain. In Neuromolecular Med, 2006
Screening of mutations were performed in TIMM8A, TIMM13, and other mitochondrial protein transport genes by conformation sensitive gel electrophoresis (CSGE), followed by direct DNA sequencing of tissue samples from the patient.
The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are new substrates for the DDP1/TIMM8a-TIMM13 complex.
Koehler et al., Los Angeles, United States. In Hum Mol Genet, 2004
TIMM8a partners with TIMM13 in the mitochondrial intermembrane space to form a 70 kDa complex and facilitates the import of the inner membrane substrate TIMM23.
The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes.
Nargang et al., Edmonton, Canada. In J Biol Chem, 2004
The Tim8 and Tim13 proteins in yeast are known to exist in the mitochondrial intermembrane space and to form a hetero-oligomeric complex involved in the import of the mitochondrial inner membrane protein Tim23, the central component of the TIM23 translocase.
A transcriptomic and proteomic characterization of the Arabidopsis mitochondrial protein import apparatus and its response to mitochondrial dysfunction.
Whelan et al., Australia. In Plant Physiol, 2004
Mass spectrometric analysis of purified mitochondria identified 17 import components, their mitochondrial sub-compartment, and verified the presence of TIM8, TIM13, TIM17, TIM23, TIM44, TIM50, and METAXIN proteins for the first time, to our knowledge.
Transcription of TIM9, a new factor required for the petite-positive phenotype of Saccharomyces cerevisiae, is defective in spt7 mutants.
Clark-Walker et al., Canberra, Australia. In Curr Genet, 2003
Examination of genes encoding other Tim components indicated that the temperature-conditional alleles of essential genes for the viability of S. cerevisiae, TIM9, TIM10 and TIM12, are required for petite survival, while deletion of TIM8 and TIM13 has no notable effect on petite cell viability.
The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins.
Koehler et al., Los Angeles, United States. In J Cell Biol, 2002
The Tim8p-Tim13p complex facilitates translocation across the intermembrane space by binding to the membrane spanning domains as shown by Tim23p peptide scans with the purified Tim8p-Tim13p complex and crosslinking studies with Tim23p fusion constructs.
The C66W mutation in the deafness dystonia peptide 1 (DDP1) affects the formation of functional DDP1.TIM13 complexes in the mitochondrial intermembrane space.
Bauer et al., München, Germany. In J Biol Chem, 2002
As a consequence, the mutated DDP1 is incorrectly folded and loses its ability to assemble into a hetero-hexameric 70-kDa complex with its cognate partner protein human Tim13.
Human deafness dystonia syndrome is caused by a defect in assembly of the DDP1/TIMM8a-TIMM13 complex.
Koehler et al., Los Angeles, United States. In Hum Mol Genet, 2002
DDP1/TIMM8a, when expressed with TIMM13 in yeast mitochondria lacking the Tim8p-Tim13p complex, restores Tim23p import, and TIMM8a and TIMM13 can be cross-linked to the hTim23 import intermediate in rat and yeast mitochondria.
The essential function of the small Tim proteins in the TIM22 import pathway does not depend on formation of the soluble 70-kilodalton complex.
Koehler et al., Cambridge, United Kingdom. In Mol Cell Biol, 2001
Characterization of this strain revealed that Tim9(S67C)p and Tim10p were tightly associated with the inner membrane, the soluble 70-kDa Tim8p-Tim13p and Tim9p-Tim10p complexes were not detectable, and the rate of protein import into isolated mitochondria proceeded at a slower rate.
Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria.
Jensen et al., Baltimore, United States. In J Cell Biol, 2000
At this intermediate stage, we find that Tim23p forms cross-linked products with two distinct protein complexes of the intermembrane space, Tim8p-Tim13p and Tim9p-Tim10p.
The human family of Deafness/Dystonia peptide (DDP) related mitochondrial import proteins.
Vetrie et al., London, United Kingdom. In Genomics, 1999
It bears a strong resemblance to a recently characterized set of zinc-binding yeast proteins (Tim8p, Tim9p, Tim10p, Tim12p, and Tim13p) that are implicated in the import of a class of transmembrane carrier proteins from the cytoplasm to the mitochondrial inner membrane.
Different import pathways through the mitochondrial intermembrane space for inner membrane proteins.
Koehler et al., Basel, Switzerland. In Embo J, 1999
The other complex contains the non-essential proteins Tim8p and Tim13p as well as loosely associated Tim9p; its function was unclear, but it interacted structurally or functionally with the Tim9p-Tim10p complex.
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