Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Genetic and structural characterization of the human mitochondrial inner membrane translocase.
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Two human TIM17 genes (TIM17a/TIM17b) were cloned and shown to encode proteins essentially identical except for their C termini.
"In contrast to yeast, two TIM17 genes were found to be expressed in humans."
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hTim23 is organized into two distinct TIM23 complexes of native mass ~110 kDa in the inner membrane, one containing hTim17a and one containing hTim17b.
"hTim23 is organized into two distinct complexes in the inner membrane, one containing hTim17a and one containing hTim17b."
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TIM23.17 preprotein translocase organization is conserved between yeast and humans.
"We suggest that the structural organization of TIM23.17 preprotein translocases is conserved from low to high eukaryotes."
Role of Magmas in protein transport and human mitochondria biogenesis.
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Human Magmas (PAM16 ortholog) is essential for protein translocation across the mitochondrial inner membrane and forms a stable subcomplex with DnaJC19/Pam18 tethered to TIM23.
"Human Magmas shows a complete growth complementation of Deltapam16 yeast cells at all temperatures."
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Magmas peripherally associates with the inner mitochondrial membrane and is tethered to the TIM23 complex in yeast and humans, supporting the TIM23-dependent matrix import pathway in which TIMM17A participates.
"Magmas forms a stable subcomplex with J-protein Pam18 or DnaJC19 through its C-terminal region and is tethered to TIM23 complex of yeast and humans."
ROMO1 is a constituent of the human presequence translocase required for YME1L protease import.
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Mass-spectrometry definition of the human TIM23 complex constituents recovers TIMM17A in authentic human TIM23 assemblies and identifies ROMO1 as a new translocase subunit.
"Here, we define the constituents of the human TIM23 complex using mass spectrometry and identified ROMO1 as a new translocase constituent with an exceptionally short half-life."
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ROMO1 is dispensable for general presequence-pathway import but is specifically required for YME1L import; this defines a regulatory layer on the TIM23/TIMM17A-dependent inner membrane import system.
"While ROMO1 is dispensable for general protein import along the presequence pathway, we show that it participates in the dynamics of TIM21 during respiratory chain biogenesis and is specifically required for import of YME1L."
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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TIMM17A is a known short-lived subunit of the TIM23-PAM presequence import system, identified within the high-confidence human mitochondrial proteome (MitoCoP) with characterised turnover dynamics.
"Not only the TIM23-PAM import system contains the known short-lived subunits TIMM17A (Opalińska et al., 2018; Rainbolt et al., 2013) and ROMO1 (Richter et al., 2019), but also the PAM import motor system consists of proteins of different half-lives."
Falcon deep research report for human TIMM17A
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TIMM17A is an integral mitochondrial inner membrane component of the TIM23 core presequence translocase.
"TIMM17A is an **integral mitochondrial inner membrane** component of the **TIM23 core**"
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TIM23 imports presequence-containing precursors destined for the mitochondrial matrix and many destined for the inner membrane.
"TIM23 imports **presequence‑containing precursors** destined to the **matrix** and many destined to the **inner membrane**"
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TIMM17A acts at the inner membrane as part of the translocation pore/cavity rather than as a stand-alone enzyme.
"TIMM17A acts at the **inner membrane** as part of the translocation pore/cavity"