Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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.
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ATP5F1A identified as the angiostatin binding protein on endothelial cell surface by N-terminal sequencing, peptide mass fingerprinting, and immunologic analyses. Angiostatin bound recombinant alpha subunit with binding not inhibited by plasminogen. Anti-alpha-subunit antibody blocked angiostatin's antiproliferative effect by 90%.
"The presence of this protein on the cell surface was confirmed by flow cytometry and immunofluorescence analysis."
Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria.
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ATPAF2 (Atp12p) is an assembly factor for the F1 component, interacting with the alpha subunit to facilitate F1 assembly.
"Atp11p and Atp12p were first described as proteins required for assembly of the F(1) component of the mitochondrial ATP synthase in Saccharomyces cerevisiae"
Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation.
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EMAP II binds the alpha subunit of ATP synthase on the cell surface. The interaction inhibits endothelial cell proliferation. Soluble alpha-ATP synthase relieves the antiproliferative effect.
"The isolated protein was determined to be the alpha subunit of ATP synthase. The interaction of EMAP II and alpha-ATP synthase was confirmed by enzyme-linked immunosorbent assay and in vitro pull down assays"
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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F1F0 ATP synthase immunocaptured from human heart tissue and fibroblasts contained a full complement of subunits including alpha, beta, OSCP, d, and IF1. The captured complex displayed oligomycin-sensitive and IF1-sensitive ATP hydrolysis activity.
"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))"
Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins.
Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.
Ecto-F1-ATPase and MHC-class I close association on cell membranes.
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Ecto-F1-ATPase (including alpha and beta chains) co-immunoprecipitates and co-localizes with MHC class I molecules in punctate membrane domains. Ecto-F1-ATPase epitope detection inversely correlates with MHC-I expression level.
"biotinylated F1-ATPase cell surface components co-immunoprecipitate with MHC-I molecules confirming the association of both complexes on Raji cells."
Nucleotide sequence of a cDNA for the alpha subunit of human mitochondrial ATP synthase.
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Original cDNA cloning of the human ATP5F1A gene. Encoded polypeptide of 553 residues highly homologous to ATP synthase alpha subunit from other species.
"A full length cDNA clone of the alpha subunit of mitochondrial ATP synthase (EC 3.6.1.34) has been isolated"
Identification of mitochondrial F(1)F(0)-ATP synthase interacting with galectin-3 in colon cancer cells.
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Galectin-3 co-localizes with ATP synthase in the inner membrane vesicles of mitochondria and has an inhibitory activity against ATP synthase.
"Galectin-3 and ATP synthase were co-isolated in the inner membrane vesicles of mitochondria."
Large-scale proteomics and phosphoproteomics of urinary exosomes.
High affinity interaction between histidine-rich glycoprotein and the cell surface type ATP synthase on T-cells.
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HRG binds the alpha subunit of ATP synthase on the surface of T-cells with K_D of 66 nM. The HRG/Con A-induced morphological changes of MOLT-4 cells were specifically inhibited by anti-beta-subunit antibody.
"HRG specifically interacted with mitochondrial ATP synthase with a dissociation constant of 66 nM."
Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins.
LC-MS/MS as an alternative for SDS-PAGE in blue native analysis of protein complexes.
Defining the membrane proteome of NK cells.
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 the beta subunit of ecto-ATP synthase (K_D 12 nM) and increases cell surface ATP levels. Blocking antibodies and antagonists (oligomycin, piceatannol, angiostatin) inhibited the effect. P2X4 receptor mediates downstream migration.
"we identified F1-F0 ATP synthase, a known target of antiangiogenic angiostatin"
Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1.
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GCN5L1 (BLOC1S1) is a mitochondrial acetyltransferase that interacts with and promotes acetylation of SIRT3 respiratory chain targets including ATP5F1A. GCN5L1 reverses global SIRT3 effects on mitochondrial protein acetylation.
"GCN5L1 interacts with and promotes acetylation of SIRT3 respiratory chain targets and reverses global SIRT3 effects on mitochondrial protein acetylation, respiration and bioenergetics."
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex.
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ATP synthase assembles through two intermediates: F1-c-ring (containing alpha, beta, and other catalytic subunits with the central rotor) and the b-e-g stator complex. The central rotor shaft and stator stalk form separately and assemble later.
"Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex."
Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function.
Architecture of the human interactome defines protein communities and disease networks.
Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
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.
Structure of the human ATP synthase.
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Cryo-EM structures of human ATP synthase in three main rotational states and one substate. Alpha subunit (chains A/B/C) alternates with beta subunit (chains D/E/F) in the F1 head. Structures reveal ADP release mechanism, symmetry mismatch accommodation, and water molecules in proton channels. Clinically relevant mutations mapped to subunit interfaces.
"Structure of the human ATP synthase."
Falcon deep research synthesis for ATP5F1A
Multimodal cell maps as a foundation for structural and functional genomics.
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
AFG3L2 degrades mitochondrial matrix proteins
AFG3L2 binds mitochondrial matrix proteins