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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
A functionally active human F1F0 ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines. Subunit structure and activity studies.
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Immunocaptured human F1F0 contains its full subunit complement.
"The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection."
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The captured complex V is an active, oligomycin-sensitive ATPase.
"The captured complex V displayed ATP hydrolysis activity that was fully oligomycin and inhibitor protein IF(1)-sensitive."
A comprehensive resource of interacting protein regions for refining human transcription factor networks.
Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex.
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Subunit e assembles in a b-e-g stator subcomplex.
"When expression of d-subunit, a stator stalk component, was knocked-down, 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)."
A reference map of the human binary protein interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Mapping adipocyte interactome networks by HaloTag-enrichment-mass spectrometry.
Enzyme-bound ATP is released
ADP and Pi bind to ATPase
F1Fo ATP synthase dimerizes
Structure of the human ATP synthase.
The role of ATP synthase subunit e (ATP5I) in mediating the metabolic and antiproliferative effects of metformin in cancer cells.
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ATP5I stabilizes ATP synthase dimers for cristae shape.
"ATP5I maintains the stability of F₁F₀-ATP synthase dimers, which is crucial for shaping cristae morphology."
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ATP5I knockout loses subunit g and lowers OSCP.
"The results show that all ATP5I knockout clones (ATP5I KO) did not express ATP5I or its partner ATP5L (subunit g in yeast) and had lower levels of ATP5O (oligomycin sensitivity-conferring protein, OSCP in yeast) (Figure 2A)."
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ATP5I knockout alters morphology and inhibits OXPHOS.
"We demonstrate that ATP5I interacts with a biguanide analogue in vitro, and disabling its expression by CRISPR-Cas9 in pancreatic cancer cells leads to the same phenotype as biguanide-treated cells, including mitochondrial morphology alterations, reduction of the NAD+/NADH ratio, inhibition of oxidative phosphorylation (OXPHOS), rescue of respiration by uncouplers, and a compensatory increase in glycolysis."
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ATP5I loss leaves oligomerization intermediates.
"Notably, metformin disrupts F₁F₀-ATP synthase oligomerization, leading to the accumulation of vestigial assembly intermediates in pancreatic and osteosarcoma cancer cells, a phenotype also observed upon ATP5I inactivation in pancreatic cancer cells."
UniProt entry P56385 (ATP5I_HUMAN)
Affinage mechanistic annotation for ATP5ME (human)