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
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Angiostatin binds ATP synthase on the surface of human endothelial cells.
Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria.
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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Human F1Fo ATP synthase was purified from heart tissue and fibroblasts by immunocapture and shown to be functionally active with oligomycin-sensitive ATP hydrolysis activity.
"The captured complex V displayed ATP hydrolysis activity that was fully oligomycin and inhibitor protein IF(1)-sensitive"
Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins.
Differential expression profiling of membrane proteins by quantitative proteomics in a human mesenchymal stem cell line undergoing osteoblast differentiation.
Angiostatin-like activity of a monoclonal antibody to the catalytic subunit of F1F0 ATP synthase.
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Cell surface ATP synthase on endothelial cells generates ATP and is inhibited by angiostatin and anti-beta antibodies, with effects on angiogenesis and intracellular pH.
"Like angiostatin, MAb3D5AB1 inhibits ATP generation by ATP synthase on the endothelial cell surface in acidic conditions, the typical tumor microenvironment where cell surface ATP synthase exhibits greater activity"
Ecto-F1-ATPase and MHC-class I close association on cell membranes.
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Ecto-F1-ATPase beta chain co-localizes and co-immunoprecipitates with MHC class I molecules on cell surfaces, with expression inversely correlated with MHC-I levels.
"biotinylated F1-ATPase cell surface components co-immunoprecipitate with MHC-I molecules confirming the association of both complexes on Raji cells"
The layered structure of human mitochondrial DNA nucleoids.
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ATP5F1B was identified in native nucleoid preparations as a peripheral component, not a core nucleoid protein.
"Several other metabolic proteins and chaperones identified in native nucleoids"
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
Defining the membrane proteome of NK cells.
MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis.
Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis.
Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes.
Regenerative protein thymosin beta-4 is a novel regulator of purinergic signaling.
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Thymosin beta-4 binds to the beta subunit of cell surface ATP synthase (Kd = 12 nM) and stimulates extracellular ATP production and endothelial cell migration via purinergic signaling.
"we determined for Tβ4 binding to the β subunit of ATP synthase a K(D) of 12 nM"
Proteomic characterization of the human sperm nucleus.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Cofactor Strap regulates oxidative phosphorylation and mitochondrial p53 activity through ATP synthase.
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Strap/TTC5 interacts with ATP synthase (beta subunit) at mitochondria and downregulates ATP production, sensitizing cells to apoptosis under glucose limitation.
"the interaction between Strap and ATP synthase downregulates mitochondrial ATP production"
Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex.
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Human mitochondrial ATP synthase assembles through two separate intermediates: the F1-c-ring (containing the beta subunit) and the b-e-g stator complex.
"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)"
The human ATP synthase beta subunit gene: sequence analysis, chromosome assignment, and differential expression.
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The human ATP5F1B gene is on chromosome 12, has 10 exons encoding a 49-aa leader peptide and 480-aa mature protein, with tissue-specific expression highest in heart.
"the functional F0F1-ATP synthase beta subunit gene is located on chromosome 12"
Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function.
Architecture of the human interactome defines protein communities and disease networks.
Human F1-ATPase: molecular cloning of cDNA for the beta subunit.
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First full-length cDNA cloning of the human F1-ATPase beta subunit, establishing it as the catalytic site of ATP synthesis with high homology to beef heart (97.5%) and E. coli (71.7%) beta subunits.
"F1-ATPase is the major enzyme for ATP synthesis, and its beta subunit is the catalytic site"
An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.
Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
Mitoregulin Controls β-Oxidation in Human and Mouse Adipocytes.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Congenital Hypermetabolism and Uncoupled Oxidative Phosphorylation.
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The L335P variant in ATP5F1B causes dominant mitochondrial uncoupling, loosening the coupling between proton motive force and ATP synthesis, resulting in hypermetabolism.
"a de novo heterozygous variant in ATP5F1B, which encodes the β subunit of mitochondrial ATP synthase"
Structure of the human ATP synthase.
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Cryo-EM structures of human ATP synthase at 2.53 A resolution reveal three rotational states, showing ADP release from the beta subunit in the open conformation and water molecules in the proton half-channels.
"These structures reveal that the release of ADP occurs when the β subunit of F1Fo-ATP synthase is in the open conformation, showing how ADP binding is coordinated during synthesis"
Multimodal cell maps as a foundation for structural and functional genomics.
The solute carrier superfamily interactome.
A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.
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The beta subunit of ATP synthase is expressed on the plasma membrane of tumor cells and functions as a ligand in NK cell and LAK cell-mediated cytotoxicity.
"A 51.5-kD protein (p51.5) bearing structural and immunologic characteristics of the beta subunit of H+ transporting ATP synthase"
Enzyme-bound ATP is released
ADP and Pi bind to ATPase
F1Fo ATP synthase dimerizes
CLPXP binds mitochondrial matrix proteins
LONP1 degrades mitochondrial matrix proteins
LONP1 binds mitochondrial matrix proteins
CLPXP degrades mitochondrial matrix proteins