Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Different import pathways through the mitochondrial intermembrane space for inner membrane proteins.
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Tim9p-Tim10p and Tim8p-Tim13p complexes each mediate import of different subsets of inner membrane proteins, transferring them to TIM22, TIM23, or other sites.
Tim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane.
Functional reconstitution of the import of the yeast ADP/ATP carrier mediated by the TIM10 complex.
The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier.
Assembly of Tim9 and Tim10 into a functional chaperone.
Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.
Structural and functional requirements for activity of the Tim9-Tim10 complex in mitochondrial protein import.
The Dutch multicenter experience of the endo-sponge treatment for anastomotic leakage after colorectal surgery.
Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae.
The cellular economy of the Saccharomyces cerevisiae zinc proteome.
Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5.
Tim9p, an essential partner subunit of Tim10p for the import of mitochondrial carrier proteins.
Tim9, a new component of the TIM22.54 translocase in mitochondria.
TIM9:TIM10 binds hydrophobic proteins
MIA40:ERV1 oxidizes cysteine residues to cystine disulfide bonds
UniProtKB entry for TIM9_YEAST
Falcon deep research on TIM9 (Edison Scientific Literature)
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Tim9 is a small TIM family soluble IMS chaperone (holdase) whose primary role is chaperone-like binding and transfer of hydrophobic precursors, not catalysis or transport.
"Tim9 is best viewed as a **specialized, soluble IMS holdase chaperone**"
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Tim9 is located in the mitochondrial intermembrane space, between TOM-mediated entry and TIM22-mediated inner-membrane insertion.
"Tim9 is located in the **mitochondrial IMS**"
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Tim9 forms the canonical Tim9-Tim10 heterohexamer (3:3 stoichiometry, ~70 kDa soluble complex) and a Tim9-Tim10-Tim12 (3:2:1) docking complex linked to TIM22.
"Tim9:Tim10 complex stoichiometry is **3:3**; the TIM22-associated complex is **Tim9–Tim10–Tim12 = 3:2:1**; the soluble Tim9/Tim10 complex is about **~70 kDa**"
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Tim9 acts as a chaperone/escort factor that prevents aggregation of hydrophobic precursors in the aqueous IMS and transfers them from TOM to TIM22.
"Tim9 acts as a **chaperone/escort factor** that prevents aggregation of hydrophobic precursors in the aqueous IMS and transfers them from **TOM** to **TIM22**."
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Within the complex, Tim10 provides the key substrate-binding elements; Tim9 alone does not bind the AAC carrier (consistent with UniProt noting Tim9 has a strong structural role relative to Tim10).
"Biochemical substrate-binding evidence indicates that **Tim10** (alone) can bind the **ATP/ADP carrier (AAC)** similarly to the Tim9–Tim10 complex, whereas **Tim9 alone does not bind AAC**, supporting a model where Tim10 provides key substrate-binding elements within the complex"
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The Tim9-Tim10 complex recognizes hydrophobic clients through a hydrophobic cleft formed by chaperone helices.
"TIM9·10 recognizes hydrophobic clients primarily through a **hydrophobic cleft** formed by chaperone helices"
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Small TIMs including Tim9 can also assist trafficking of some outer-membrane beta-barrel proteins toward the SAM complex.
"Small TIMs can also assist trafficking of some outer-membrane β-barrel proteins toward the SAM complex"
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Tim9 is itself imported via TOM and oxidatively folded in the IMS by the MIA pathway, which introduces the two intramolecular disulfides in its conserved CX3C motifs (rather than stable metal coordination in the mature form).
"Small TIM proteins (including Tim9) are imported through TOM and undergo oxidative folding in the IMS via the **MIA (mitochondrial import and assembly) pathway**, which introduces disulfides in the conserved CX3C motifs"
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Tim9 and Tim10 assemble into an essential heterohexameric Tim9/10 complex; unassembled small TIMs can be degraded by Yme1, with assembly being protective.
"Tim9 and Tim10 assemble into an essential heterohexameric Tim9/10 complex** that chaperones hydrophobic preproteins from TOM to TIM22"
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Conserved-residue mutants tim9-19 (E52G) and tim9-3 (V40A + S60P) abolish a detectable Tim9-Tim10 heterohexamer, linking these residues to complex integrity and import function.
"tim9-19 (E52G)** and **tim9-3 (V40A + S60P)** show **no detectable Tim9–Tim10 heterohexamer** in detergent-solubilized mitochondria"
Current PANTHER PTHR13172 PAINT annotation snapshot
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Current PAINT retains PTN004407763 for the Tim9/TIMM9/TIMM10B clade and now places both mitochondrial IMS chaperone-complex membership and unfolded protein holdase activity at that node.
"PTHR13172 PTN004407763 GO:0042719 C IBD false MGI:MGI:1353436|SGD:S000007256|UniProtKB:Q9Y5J6|UniProtKB:Q9Y5J7 taxon:2759 20260128
PTHR13172 PTN004407763 GO:0140309 F IBD false SGD:S000007256|UniProtKB:Q9Y5J7 taxon:2759 20260603"
Intermembrane space proteome of yeast mitochondria.
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This comprehensive yeast IMS proteome used Tim9 as a known IMS marker and identified more than 90% of known soluble IMS proteins in Bax-releasable mitochondrial fractions.
"From the known 31 soluble IMS proteins, 29 proteins were reproducibly identified, corresponding to a coverage of >90%."
Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.
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Reconstituted yeast TIM9-TIM10 binds unfolded alpha-helical carrier precursors and a VDAC/Por1 beta-hairpin peptide through the same hydrophobic cleft, and Tim9/Tim10 binding-cleft mutations impair carrier and beta-barrel biogenesis in vivo.
"Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis."