Gene Ontology annotation through association of InterPro records with GO terms.
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
Combined Automated Annotation using Multiple IEA Methods.
Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex.
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Mitochondrial ATP synthase is a rotary motor enzyme whose central shaft rotates in stator casings fixed with the peripheral stator stalk.
"Mitochondrial ATP synthase is a motor enzyme in which a central shaft rotates in the stator casings fixed with the peripheral stator stalk."
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Human ATP synthase assembles via two separate subcomplexes, an F1-c-ring (central rotor shaft plus catalytic subunits, including the c-ring to which ATP5MC2 contributes) and a b-e-g stator stalk complex, which join later.
"human cells could not form ATP synthase holocomplex and instead accumulated two subcomplexes, one containing a central rotor shaft plus catalytic subunits (F1-c-ring) and the other containing stator stalk components ("b-e-g" complex)."
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The F1-c-ring intermediate also accumulates when mtDNA-encoded a-subunit and A6L are suppressed, supporting a conserved assembly strategy across organisms.
"F1-c-ring was also formed when expression of mitochondrial DNA-coded a-subunit and A6L was suppressed. Thus, the central rotor shaft and the stator stalk are formed separately and they assemble later."
The 7q11.23 Protein DNAJC30 Interacts with ATP Synthase and Links Mitochondria to Brain Development.
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DNAJC30 is identified as an auxiliary component of the mitochondrial ATP synthase machinery, linking ATP synthase function to brain development.
"we identify DNAJC30 as an auxiliary component of ATP-synthase machinery and reveal mitochondrial maladies as underlying certain defects in brain development and function associated with WS."
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DNAJC30 interacts with mitochondrial ATP synthase and facilitates ATP synthesis in neurons.
"DNAJC30 is enriched in developing and mature neurons where it interacts with the mitochondrial ATP synthase machinery and facilitates ATP synthesis."
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Loss of DNAJC30 reduces integrity of OXPHOS supercomplexes and ATP-synthase dimers, consistent with a role of ATP synthase in Williams syndrome pathology.
"The mitochondrial features are consistent with our observations of decreased integrity of oxidative phosphorylation supercomplexes and ATP-synthase dimers in WS."
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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A high-confidence human mitochondrial proteome (MitoCoP) of >1,100 proteins was defined, including ATP synthase subunits and assembly factor interactors.
"We classified >8,000 proteins in mitochondrial preparations of human cells and defined a mitochondrial high-confidence proteome of >1,100 proteins (MitoCoP). We identified interactors of translocases, respiratory chain, and ATP synthase assembly factors."
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OXPHOS subunits, including ATP synthase complex V components, are among the highly abundant mitochondrial proteins quantified in this proteomic atlas.
"Our data show a high abundance of OXPHOS subunits and factors involved in protein maturation and folding"
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Complex V (ATP synthase) disease genes show a strong association with cardiovascular clinical findings, reflecting the heart's dependence on ATP supply.
"88% of the complex V disease genes are associated with cardiovascular observations, reflecting the strong dependence of the heart on ATP supply."
Enzyme-bound ATP is released
ADP and Pi bind to ATPase
F1Fo ATP synthase dimerizes
Deep research on ATP5MC2 function
Cyberian deep research on ATP5MC2 function