Human Gene TIMM10 (ENST00000257245.9_7) from GENCODE V47lift37
  Description: translocase of inner mitochondrial membrane 10 (from RefSeq NM_012456.3)
Gencode Transcript: ENST00000257245.9_7
Gencode Gene: ENSG00000134809.9_9
Transcript (Including UTRs)
   Position: hg19 chr11:57,295,937-57,298,227 Size: 2,291 Total Exon Count: 3 Strand: -
Coding Region
   Position: hg19 chr11:57,296,190-57,297,662 Size: 1,473 Coding Exon Count: 2 

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Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr11:57,295,937-57,298,227)mRNA (may differ from genome)Protein (90 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
AlphaFoldBioGPSEnsemblEntrez GeneExonPrimerGeneCards
HGNCMalacardsMGIOMIMPubMedReactome
UniProtKBWikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: TIM10_HUMAN
DESCRIPTION: RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10;
FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be 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.
SUBUNIT: Heterohexamer; composed of 3 copies of TIMM9 and 3 copies of TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-bladed alpha-propeller structure and associates with the TIMM22 component of the TIM22 complex. Interacts with multi-pass transmembrane proteins in transit. Also forms a complex composed of TIMM9, TIMM10/TIM10A and FXC1/TIM10B.
INTERACTION: Q9Y5J7:TIMM9; NbExp=5; IntAct=EBI-1200391, EBI-1200370;
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle.
DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM10 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (Probable).
SIMILARITY: Belongs to the small Tim family.

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: TIMM10
Diseases sorted by gene-association score: mitochondrial metabolism disease (1)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 37.16 RPKM in Cells - EBV-transformed lymphocytes
Total median expression: 881.63 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
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-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -51.20142-0.361 Picture PostScript Text
3' UTR -86.60253-0.342 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR004217 - Tim8/9/10/13_Znf-like

Pfam Domains:
PF02953 - Tim10/DDP family zinc finger

SCOP Domains:
144122 - Tim10-like

Protein Data Bank (PDB) 3-D Structure
MuPIT help
2BSK - X-ray


ModBase Predicted Comparative 3D Structure on P62072
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The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologNo orthologNo ortholog
Gene DetailsGene Details    
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-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0005215 transporter activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0008565 protein transporter activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0051087 chaperone binding

Biological Process:
GO:0006626 protein targeting to mitochondrion
GO:0007605 sensory perception of sound
GO:0015031 protein transport
GO:0045039 protein import into mitochondrial inner membrane
GO:0072321 chaperone-mediated protein transport

Cellular Component:
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005744 mitochondrial inner membrane presequence translocase complex
GO:0005758 mitochondrial intermembrane space
GO:0016020 membrane
GO:0042719 mitochondrial intermembrane space protein transporter complex
GO:0042721 mitochondrial inner membrane protein insertion complex


-  Descriptions from all associated GenBank mRNAs
  BC032133 - Homo sapiens translocase of inner mitochondrial membrane 10 homolog (yeast), mRNA (cDNA clone MGC:29523 IMAGE:4761702), complete cds.
AF150089 - Homo sapiens small zinc finger-like protein (TIM10) mRNA, complete cds.
JD172081 - Sequence 153105 from Patent EP1572962.
AK289751 - Homo sapiens cDNA FLJ76375 complete cds, highly similar to Homo sapiens translocase of inner mitochondrial membrane 10 homolog (yeast) (TIMM10), mRNA.
JD347259 - Sequence 328283 from Patent EP1572962.
AF152354 - Homo sapiens TIMM10 mRNA, complete cds.
KJ893569 - Synthetic construct Homo sapiens clone ccsbBroadEn_02963 TIMM10 gene, encodes complete protein.
DQ578189 - Homo sapiens piRNA piR-46301, complete sequence.
DQ579709 - Homo sapiens piRNA piR-47821, complete sequence.
JD409627 - Sequence 390651 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein P62072 (Reactome details) participates in the following event(s):

R-HSA-1299481 TIMM9:TIMM10 binds hydrophobic proteins
R-HSA-1955380 TIMM9:TIMM10 transfers proteins to TIMM22
R-HSA-1268020 Mitochondrial protein import
R-HSA-392499 Metabolism of proteins

-  Other Names for This Gene
  Alternate Gene Symbols: A8K136, ENST00000257245.1, ENST00000257245.2, ENST00000257245.3, ENST00000257245.4, ENST00000257245.5, ENST00000257245.6, ENST00000257245.7, ENST00000257245.8, NM_012456, P62072, Q9WV99, Q9WVA0, Q9Y5J8, TIM10, TIM10_HUMAN, uc317fxo.1, uc317fxo.2
UCSC ID: ENST00000257245.9_7
RefSeq Accession: NM_012456.3
Protein: P62072 (aka TIM10_HUMAN)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.