ATP5F1B

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0045259 proton-transporting ATP synthase complex	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for CC. ATP5F1B is a core structural and catalytic component of the proton-transporting ATP synthase complex (Complex V). This is well supported by cryo-EM structural data (PMID:37244256), immunocapture studies (PMID:12110673), and assembly studies (PMID:26297831). Reason: This is the defining complex membership for ATP5F1B. The beta subunit is one of the major subunits of the F1 catalytic head. Cryo-EM structures show ATP5F1B as chains D/E/F in the alpha3-beta3 hexamer (PMID:37244256). IBA annotation is appropriate and well conserved across the ATPase alpha/beta chains family. Supporting Evidence: PMID:37244256 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 PMID:12110673 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))
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for MF with contributes_to qualifier. The beta subunit contributes to the proton-transporting ATP synthase activity of the holoenzyme complex via the rotational mechanism. The contributes_to qualifier is correct because this activity is a property of the whole complex, not the individual subunit. Reason: The contributes_to qualifier is appropriate for a subunit that is part of the catalytic core but requires the full complex for proton-transporting ATP synthase activity. The beta subunit houses the catalytic nucleotide-binding sites, but the rotational mechanism requires the assembled F1Fo complex including the proton channel (Fo). Well supported by structural data (PMID:37244256) and functional studies (PMID:36239646). Supporting Evidence: PMID:37244256 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 PMID:36239646 The catalytic core of F1 contains three α and three β subunits arranged around a γ subunit of the central stalk. Protons passing through FO (the pore) cause the γ stalk to rotate, inducing conformational transitions in the β subunit that are required for the synthesis of ATP from ADP
GO:0042776 proton motive force-driven mitochondrial ATP synthesis	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for BP. Proton motive force-driven mitochondrial ATP synthesis is the core biological process performed by ATP5F1B as part of Complex V. This is the more specific mitochondrial form of GO:0015986. Reason: This is the most specific and accurate BP annotation for ATP5F1B. The beta subunit is the catalytic component that directly synthesizes ATP from ADP driven by the proton motive force across the inner mitochondrial membrane. Supported by extensive experimental evidence (PMID:36239646, PMID:37244256, PMID:12110673). Supporting Evidence: PMID:36239646 Complex V (CV) is the central enzyme in energy conversion: it dissipates the proton gradient across the membrane, catalyzing the phosphorylation of ADP to ATP
GO:0000166 nucleotide binding	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation for MF based on UniProtKB keyword mapping. Nucleotide binding is correct but very general for ATP5F1B, which specifically binds ADP and ATP at its catalytic site. Reason: This is a broad but correct IEA annotation. The beta subunit has well-characterized nucleotide (ADP/ATP) binding sites documented by cryo-EM (PMID:37244256) and UniProt binding annotations at residues 209-214. More specific terms like GO:0005524 (ATP binding) are also present in the annotation set, so this broader term is acceptable as an IEA inference. Supporting Evidence: PMID:37244256 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
GO:0005524 ATP binding	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation for MF. ATP binding is a well-established function of the beta subunit, which contains the catalytic nucleotide-binding site. UniProt documents multiple ADP/ATP binding residues (positions 209-214, 238-239). Reason: Correct and well-supported. The beta subunit binds ATP at its catalytic site. Structural evidence from cryo-EM (PMID:37244256) and bovine structure by similarity confirm ADP/ATP binding. UniProt lists extensive binding site annotations with experimental evidence. Supporting Evidence: PMID:37244256 snapshot images for three main rotational states and one substate of human ATP synthase
GO:0005737 cytoplasm	IEA GO_REF:0000117	ACCEPT	Summary: IEA annotation for CC based on ARBA machine learning model. Cytoplasm is too broad and imprecise for ATP5F1B, whose primary localization is the mitochondrial matrix/inner membrane. Reason: While imprecise, this is not incorrect since the mitochondrion is within the cytoplasm. More specific CC annotations (mitochondrion, mitochondrial inner membrane, mitochondrial matrix) are present in the annotation set. As an IEA, this broad term is acceptable.
GO:0005743 mitochondrial inner membrane	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation for CC based on UniProt subcellular location mapping. ATP5F1B is a peripheral membrane protein on the matrix side of the mitochondrial inner membrane, as part of the F1 head of the ATP synthase complex. Reason: Correct. UniProt states ATP5F1B localizes to "Mitochondrion inner membrane; Peripheral membrane protein; Matrix side" with experimental evidence (PMID:25168243). The F1 head is attached to the inner membrane via the central and peripheral stalks. Supporting Evidence: PMID:25168243 Strap is localised at mitochondria where one of its key interaction partners is ATP synthase
GO:0006754 ATP biosynthetic process	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation for BP based on UniProt keyword mapping. ATP biosynthetic process is a core function of ATP5F1B as the catalytic subunit of ATP synthase. Reason: Correct and represents a core function. The beta subunit directly catalyzes ATP synthesis from ADP + Pi. This is supported by UniProt functional annotation with EC 7.1.2.2 and multiple experimental studies (PMID:37244256, PMID:36239646).
GO:0006811 monoatomic ion transport	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation for BP. This term refers to ion transport, which is related to the proton transport function of the ATP synthase complex but is extremely broad. Reason: While very general, this is not incorrect since the F1Fo-ATP synthase complex transports protons (H+) across the inner mitochondrial membrane. The beta subunit contributes to this function as part of the complex. More specific annotations for proton transport are also present.
GO:0015986 proton motive force-driven ATP synthesis	IEA GO_REF:0000002	ACCEPT	Summary: IEA annotation for BP based on InterPro mapping. Proton motive force-driven ATP synthesis is the core biological process of ATP5F1B. This is the parent of the more specific GO:0042776 (mitochondrial form). Reason: Correct. This broader term subsumes GO:0042776. Redundant with the IBA and IDA annotations for the same term, but as an IEA it is perfectly acceptable. ATP5F1B is a core component of the proton motive force-driven ATP synthesis machinery.
GO:0016469 proton-transporting two-sector ATPase complex	IEA GO_REF:0000117	ACCEPT	Summary: IEA annotation for CC. This term describes the broader class of two-sector ATPase complexes (F-type, V-type, A-type). The mitochondrial ATP synthase is an F-type two-sector ATPase. Reason: Correct but general. The F1Fo ATP synthase is indeed a proton-transporting two-sector ATPase complex. More specific annotations for the proton-transporting ATP synthase complex (GO:0045259) are also present. As an IEA from ARBA, the broader term is acceptable.
GO:0045259 proton-transporting ATP synthase complex	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation for CC, duplicating the IBA annotation for the same GO term. Correct. Reason: Correct and consistent with the IBA annotation. Duplicate evidence codes for the same term are fine.
GO:0046034 ATP metabolic process	IEA GO_REF:0000002	ACCEPT	Summary: IEA annotation for BP based on InterPro mapping. ATP metabolic process is very broad, encompassing both ATP synthesis and hydrolysis. Reason: Correct but very general. ATP5F1B is involved in ATP metabolism (primarily synthesis, but the complex can also hydrolyze ATP). More specific annotations for ATP biosynthetic process and proton motive force-driven ATP synthesis are present.
GO:0046872 metal ion binding	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation for MF based on UniProt keyword mapping. ATP5F1B binds Mg2+ as a cofactor for the ATP synthase catalytic reaction. UniProt documents Mg2+ binding at residues 213 and 238 (PMID:37244256). Reason: Correct. The beta subunit binds Mg2+ ions which are essential cofactors for the catalytic reaction. The cryo-EM structure (PMID:37244256) confirms Mg2+ binding. This is a broad IEA term; more specific magnesium ion binding could be considered, but metal ion binding is acceptable. Supporting Evidence: PMID:37244256 Biological energy currency ATP is produced by F1Fo-ATP synthase
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation for MF, duplicating the IBA and IDA annotations for the same GO term. Note this IEA lacks the contributes_to qualifier that the IBA has. Reason: Correct term but ideally should have the contributes_to qualifier as in the IBA annotation, since the activity is a property of the whole complex. However, as an IEA the absence of the qualifier is acceptable.
GO:1902495 transmembrane transporter complex	IEA GO_REF:0000117	ACCEPT	Summary: IEA annotation for CC based on ARBA. The ATP synthase complex is a transmembrane transporter complex that translocates protons across the membrane. Reason: Correct but very general. The F1Fo-ATP synthase is indeed a transmembrane transporter complex. More specific terms (GO:0045259, GO:0016469) are also annotated.
GO:1902600 proton transmembrane transport	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation for BP. Proton transmembrane transport is a core process of the ATP synthase complex. Reason: Correct. The F1Fo-ATP synthase transports protons across the inner mitochondrial membrane as part of its catalytic cycle. ATP5F1B contributes to this as the catalytic subunit of the F1 head.
GO:0005515 protein binding	IPI PMID:11410595 Atp11p and Atp12p are assembly factors for the F(1)-ATPase i...	UNDECIDED	Summary: IPI protein binding annotation. Publication not available for review (PMID:11410595 not cached). Likely a large-scale interaction study. Reason: Cannot assess without access to the publication. The generic protein binding term is uninformative. If from a large-scale study, it is likely a high-throughput detection of protein interaction without functional characterization.
GO:0005515 protein binding	IPI PMID:15161933 Comprehensive proteomic analysis of interphase and mitotic 1...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from a large-scale proteomic analysis of 14-3-3-binding proteins (Meek et al. 2004). ATP5F1B was identified as a 14-3-3-binding protein. UniProt also documents an interaction with YWHAZ (14-3-3 zeta). Reason: This is a high-throughput proteomic study identifying many 14-3-3-binding proteins. While the interaction may be real, the generic "protein binding" term is uninformative and the biological significance of 14-3-3 binding to ATP5F1B is not characterized. The interaction could reflect phosphorylation-dependent regulation but this is speculative. Supporting Evidence: PMID:15161933 14-3-3-binding proteins were purified from extracts of interphase and mitotic HeLa cells using specific peptide elution from 14-3-3 zeta affinity columns
GO:0005515 protein binding	IPI PMID:20618440 Proteomic and biochemical analysis of 14-3-3-binding protein...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from proteomic analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis (Pozuelo-Rubio 2010). ATP5F1B was identified as a 14-3-3-associated protein. Reason: Another 14-3-3 interaction proteomics study. The generic protein binding term is uninformative. The biological relevance to ATP5F1B function is unclear. Supporting Evidence: PMID:20618440 14-3-3 is a family of proteins comprising several isoforms that, in many cases, promote cell survival by association with proapoptotic proteins
GO:0005515 protein binding	IPI PMID:27499296 Mitochondrial Protein Interaction Mapping Identifies Regulat...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from mitochondrial protein interaction mapping study (Floyd et al. 2016). This is a focused mitochondrial interactome study that identified regulators of respiratory chain function. Reason: While this is a mitochondria-focused interaction study, the generic protein binding term is uninformative. The study mapped mitochondrial protein interactions but the specific interaction partners and functional significance for ATP5F1B are not captured by this annotation. Supporting Evidence: PMID:27499296 Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from a large-scale human interactome mapping study (Huttlin et al. 2017). This is a high-throughput study mapping the architecture of the human interactome. Reason: Large-scale interactome study. The generic protein binding term is uninformative for a well-characterized enzyme subunit. The specific interaction partners are not characterized in the annotation.
GO:0005515 protein binding	IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from an interactome perturbation framework study for developmental disorders (Sahni et al. 2018). High-throughput protein interaction study. Reason: High-throughput interactome study. Generic protein binding is uninformative for ATP5F1B.
GO:0005515 protein binding	IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from a histone interaction landscape study using crosslinking mass spectrometry in intact cell nuclei (Fasci et al. 2018). ATP5F1B detected as a histone-interacting protein in this study. Reason: This study focused on histone interactions by crosslinking mass spectrometry. Detection of ATP5F1B likely reflects its abundance rather than a specific functional interaction with histones. The generic protein binding term is uninformative.
GO:0005515 protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from a study on disruption of protein interactions by genetic variants across the allele frequency spectrum (Sahni et al. 2019). High-throughput study. Reason: Large-scale interactome study focused on variant effects on protein interactions. Generic protein binding is uninformative.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: IPI protein binding from a reference map of the human binary protein interactome (Luck et al. 2020). High-throughput Y2H/AP-MS study. Reason: Large-scale binary interactome reference map. Generic protein binding is uninformative for a well-characterized enzyme subunit.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from an interactome mapping study focused on neurodegenerative disease proteins (Haenig et al. 2020). Reason: Disease-focused interactome study. Generic protein binding is uninformative. The interaction with neurodegenerative disease proteins is likely not a core function of ATP5F1B.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from dual proteome-scale network study showing cell-specific remodeling of the human interactome (Huttlin et al. 2021). Reason: Large-scale interactome study. Generic protein binding is uninformative.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from multimodal cell maps study (2024). High-throughput study mapping structural and functional genomics. Reason: Large-scale high-throughput study. Generic protein binding is uninformative for ATP5F1B.
GO:0005515 protein binding	IPI PMID:40355756 The solute carrier superfamily interactome.	MARK AS OVER ANNOTATED	Summary: IPI protein binding from solute carrier superfamily interactome study (2024). Reason: Focused interactome study for SLC superfamily. Generic protein binding is uninformative for ATP5F1B, which is not a solute carrier.
GO:0005739 mitochondrion	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation for CC based on Ensembl Compara ortholog transfer. Mitochondrial localization is well established for ATP5F1B. Reason: Correct. ATP5F1B is a mitochondrial protein with a mitochondrial transit peptide (residues 1-47, UniProt). Localization to mitochondria is confirmed by multiple experimental methods.
GO:0005739 mitochondrion	IDA GO_REF:0000052	ACCEPT	Summary: IDA annotation for CC based on curation of immunofluorescence data. Mitochondrial localization confirmed by immunofluorescence. Reason: Correct. Direct experimental evidence for mitochondrial localization via immunofluorescence.
GO:0005743 mitochondrial inner membrane	NAS PMID:26297831 Assembly of human mitochondrial ATP synthase through two sep...	ACCEPT	Summary: NAS annotation for CC citing the assembly study of human mitochondrial ATP synthase (Fujikawa et al. 2015). The study demonstrates that ATP5F1B assembles into the F1-c-ring intermediate at the inner mitochondrial membrane. Reason: Correct. The beta subunit is part of the F1 head which is attached to the inner mitochondrial membrane via the central stalk connected to the Fo sector. This is well-established from the assembly pathway described in this study. Supporting Evidence: PMID:26297831 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)
GO:0015986 proton motive force-driven ATP synthesis	NAS PMID:26297831 Assembly of human mitochondrial ATP synthase through two sep...	ACCEPT	Summary: NAS annotation for BP citing the assembly study. The study addresses assembly of the ATP synthase rather than directly demonstrating the proton motive force-driven ATP synthesis activity, but the function is well established. Reason: While the cited study focuses on assembly, proton motive force-driven ATP synthesis is the core function of the complex that ATP5F1B assembles into. Well supported by other references.
GO:0045259 proton-transporting ATP synthase complex	NAS PMID:2870059 Human F1-ATPase: molecular cloning of cDNA for the beta subu...	ACCEPT	Summary: NAS annotation for CC citing the original cDNA cloning of the human F1-ATPase beta subunit (Ohta & Kagawa 1986). This foundational paper established the identity of ATP5F1B. Reason: Correct. The original cloning paper established that this gene encodes the beta subunit of human F1-ATPase, which is part of the proton-transporting ATP synthase complex. Supporting Evidence: PMID:2870059 F1-ATPase is the major enzyme for ATP synthesis, and its beta subunit is the catalytic site
GO:0015986 proton motive force-driven ATP synthesis	IDA PMID:37244256 Structure of the human ATP synthase.	ACCEPT	Summary: IDA annotation for BP from the cryo-EM structure of human ATP synthase (Lai et al. 2023). The study resolved multiple rotational states demonstrating the proton motive force-driven ATP synthesis mechanism. Reason: Correct. The structural study directly visualizes the rotary mechanism of ATP synthesis in the human enzyme. Represents core function. Supporting Evidence: PMID:37244256 Biological energy currency ATP is produced by F1Fo-ATP synthase
GO:0015986 proton motive force-driven ATP synthesis	IDA PMID:25168243 Cofactor Strap regulates oxidative phosphorylation and mitoc...	ACCEPT	Summary: IDA annotation for BP from the Strap/TTC5 study (Maniam et al. 2015). The study showed that Strap interaction with ATP synthase downregulates mitochondrial ATP production, demonstrating that ATP5F1B is involved in ATP synthesis. Reason: Correct. The study demonstrated that interaction with Strap downregulated ATP synthase activity, confirming the role of ATP5F1B in ATP synthesis. The fact that inhibiting ATP synthase reduces ATP production directly demonstrates the BP. Supporting Evidence: PMID:25168243 the interaction between Strap and ATP synthase downregulates mitochondrial ATP production
GO:0015986 proton motive force-driven ATP synthesis	IDA PMID:36239646 Congenital Hypermetabolism and Uncoupled Oxidative Phosphory...	ACCEPT	Summary: IDA annotation for BP from the congenital hypermetabolism study (Ganetzky et al. 2022, NEJM). The L335P variant in ATP5F1B uncouples proton motive force from ATP synthesis, demonstrating the role of the beta subunit in coupling. Reason: Strong direct evidence. The study engineered the L335P variant and demonstrated uncoupling of the proton motive force from ATP synthesis, directly implicating ATP5F1B in this process. Supporting Evidence: PMID:36239646 Oxygen consumption and membrane potential studies in both patient fibroblasts and cells with genetic introduction of the Leu335 variant show loosened coupling between the proton motive force (generated by mitochondrial respiration) and ATP synthesis due to intrinsic dysfunction of Complex V
GO:0045259 proton-transporting ATP synthase complex	IDA PMID:37244256 Structure of the human ATP synthase.	ACCEPT	Summary: IDA annotation for CC from the cryo-EM structure of human ATP synthase. The study directly resolved ATP5F1B as part of the intact complex. Reason: Direct structural evidence. The cryo-EM structure (PDB: 8H9E and others) shows ATP5F1B as chains D/E/F in the intact human ATP synthase complex. Supporting Evidence: PMID:37244256 Structure of the human ATP synthase
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism	IDA PMID:25168243 Cofactor Strap regulates oxidative phosphorylation and mitoc...	ACCEPT	Summary: IDA annotation for MF from the Strap study. The study demonstrated that ATP5F1B has ATP synthase activity that is modulated by Strap binding. Reason: Supported. The study demonstrated functional ATP synthase activity involving the beta subunit. While the study focused on Strap regulation, it confirmed the catalytic activity of the complex containing ATP5F1B. Supporting Evidence: PMID:25168243 the interaction between Strap and ATP synthase downregulates mitochondrial ATP production
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism	IDA PMID:36239646 Congenital Hypermetabolism and Uncoupled Oxidative Phosphory...	ACCEPT	Summary: IDA annotation for MF from the NEJM uncoupling study. The study showed that the L335P variant disrupts coupling, demonstrating the role of the beta subunit in the rotational mechanism. Reason: Strong evidence. The uncoupling phenotype of L335P, which lies near the hydrophobic sleeve that contacts the rotating gamma subunit, directly demonstrates the beta subunit's role in the rotational ATP synthase mechanism. Supporting Evidence: PMID:36239646 Leu335 lies close to the hydrophobic sleeve in the α3β3 assembly that holds the tip of the γ subunit of the central stalk
GO:0005739 mitochondrion	HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an...	ACCEPT	Summary: HTP annotation for CC from the quantitative high-confidence human mitochondrial proteome study (Morgenstern et al. 2021, Cell Metabolism). ATP5F1B was identified with high confidence as part of the mitochondrial proteome. Reason: Correct. This high-quality mitochondrial proteomics study provides strong quantitative evidence for mitochondrial localization. ATP5F1B is one of the most abundant mitochondrial proteins.
GO:0005739 mitochondrion	IC PMID:12110673 A functionally active human F1F0 ATPase can be purified by i...	ACCEPT	Summary: IC (inferred by curator) annotation for CC based on the immunocapture study of human F1F0 ATPase from heart tissue and fibroblasts (Aggeler et al. 2002). The study purified functionally active F1Fo from mitochondria. Reason: Correct. The study isolated F1Fo-ATPase from mitochondria using immunocapture, confirming the mitochondrial localization of the complex and its subunits including beta. Supporting Evidence: PMID:12110673 Human mitochondrial F(1)F(0) ATP synthase was isolated with a one-step immunological approach, using a monoclonal antibody against F(1) in a 96-well microplate activity assay system
GO:0045259 proton-transporting ATP synthase complex	IDA PMID:12110673 A functionally active human F1F0 ATPase can be purified by i...	ACCEPT	Summary: IDA annotation for CC from the immunocapture study. ATP5F1B (beta subunit) was identified as part of the purified F1Fo complex. Reason: Direct experimental evidence. The beta subunit was identified by specific antibodies in the immunocaptured F1Fo complex. Supporting Evidence: PMID:12110673 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))
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism	IDA PMID:12110673 A functionally active human F1F0 ATPase can be purified by i...	ACCEPT	Summary: IDA annotation for MF with contributes_to qualifier from the immunocapture study. The purified complex displayed ATP hydrolysis activity that was oligomycin-sensitive, confirming functional ATP synthase activity. Reason: Direct functional evidence. The immunocaptured complex showed ATP hydrolysis activity that was sensitive to oligomycin (an ATP synthase inhibitor) and IF1, confirming that the complex containing the beta subunit has proton-transporting ATP synthase activity. The contributes_to qualifier is appropriate. Supporting Evidence: PMID:12110673 The captured complex V displayed ATP hydrolysis activity that was fully oligomycin and inhibitor protein IF(1)-sensitive
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-1592247	ACCEPT	Summary: TAS annotation for CC from Reactome pathway "Expression of ATP5B". The F1 head containing the beta subunit faces the mitochondrial matrix. Reason: Correct. UniProt confirms the beta subunit is on the matrix side of the inner mitochondrial membrane. The F1 catalytic head protrudes into the matrix.
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-164832	ACCEPT	Summary: TAS annotation for CC from Reactome pathway "ATPase synthesizes ATP". Correct localization for ATP synthesis at the matrix side. Reason: Correct. ATP synthesis occurs in the matrix, where the F1 head containing ATP5F1B catalyzes ADP + Pi to ATP.
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-164834	ACCEPT	Summary: TAS annotation for CC from Reactome pathway "Enzyme-bound ATP is released". Reason: Correct. ATP release from the beta subunit occurs in the matrix.
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-164840	ACCEPT	Summary: TAS annotation for CC from Reactome pathway "ADP and Pi bind to ATPase". Reason: Correct. ADP and Pi bind to the catalytic site of the beta subunit on the matrix side.
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-8949580	ACCEPT	Summary: TAS annotation for CC from Reactome pathway "F1Fo ATP synthase dimerizes". The beta subunit is part of the complex that dimerizes. Reason: Correct. ATP synthase dimerization involves the F1 head containing the beta subunit on the matrix side.
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-9838035	ACCEPT	Summary: TAS annotation for CC from Reactome pathway "CLPXP binds mitochondrial matrix proteins". ATP5F1B is a substrate for the CLPXP protease quality control system. Reason: Correct. The beta subunit resides in the matrix and is subject to mitochondrial quality control by CLPXP protease.
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-9838081	ACCEPT	Summary: TAS annotation for CC from Reactome pathway "LONP1 degrades mitochondrial matrix proteins". Reason: Correct. The beta subunit in the matrix is subject to LONP1 protease quality control.
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-9838093	ACCEPT	Summary: TAS annotation for CC from Reactome pathway "LONP1 binds mitochondrial matrix proteins". Reason: Correct. Same as above, localization to matrix confirmed.
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-9838289	ACCEPT	Summary: TAS annotation for CC from Reactome pathway "CLPXP degrades mitochondrial matrix proteins". Reason: Correct. Redundant with other Reactome matrix annotations. Matrix localization is well established.
GO:0006754 ATP biosynthetic process	IMP PMID:21106936 Regenerative protein thymosin beta-4 is a novel regulator of...	KEEP AS NON CORE	Summary: IMP annotation for BP from the thymosin beta-4/purinergic signaling study (Freeman et al. 2011). The study demonstrated that blocking cell surface ATP synthase with oligomycin or antibodies inhibited extracellular ATP generation, confirming the biosynthetic function. Reason: This annotation relates to ATP biosynthesis at the cell surface (ecto-ATP synthase), not the core mitochondrial function. The study showed extracellular ATP generation by cell surface ATP synthase, which is a real but non-core function. The mutant phenotype was measured for cell surface ATP production by endothelial cells. Supporting Evidence: PMID:21106936 Blocking antibodies and antagonists (oligomycin, IC(50) ∼1.8 μM; piceatannol, IC(50) ∼1.05 μM; and angiostatin, IC(50) ∼2.9 μg/ml) of ATP synthase inhibited the Tβ4-induced increase in cell surface ATP levels
GO:0043536 positive regulation of blood vessel endothelial cell migration	IGI PMID:21106936 Regenerative protein thymosin beta-4 is a novel regulator of...	KEEP AS NON CORE	Summary: IGI annotation for BP from the thymosin beta-4 study. The study showed that ATP synthase on endothelial cell surfaces mediates thymosin beta-4-induced endothelial cell migration. Blocking ATP synthase with antibodies or antagonists inhibited this migration. Reason: This is a non-core function related to the ecto-ATP synthase role on endothelial cell surfaces. The study demonstrates that cell surface ATP synthase contributes to angiogenesis-related endothelial migration via purinergic signaling, but this is not the primary evolved function of ATP5F1B. Supporting Evidence: PMID:21106936 Blocking antibodies and antagonists (oligomycin, IC(50) ∼1.8 μM; piceatannol, IC(50) ∼1.05 μM; and angiostatin, IC(50) ∼2.9 μg/ml) of ATP synthase inhibited the Tβ4-induced increase in cell surface ATP levels, as measured by luciferase assay, and the Tβ4-induced increase in HUVEC migration
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism	IMP PMID:36239646 Congenital Hypermetabolism and Uncoupled Oxidative Phosphory...	ACCEPT	Summary: IMP annotation for MF from the NEJM uncoupling study. The L335P variant in ATP5F1B disrupted ATP synthase coupling, demonstrating the beta subunit's role in the rotational mechanism via mutant phenotype analysis. Reason: Strong direct evidence from mutant phenotype. The L335P variant near the hydrophobic sleeve that contacts the rotating gamma subunit caused uncoupled ATP synthase activity, demonstrating the beta subunit's essential role in the rotational mechanism. Supporting Evidence: PMID:36239646 we propose that Leu335Pro is a group 1 mutation, because it probably impairs engagement of the γ subunit by the α–β hexamer by disrupting contact between the β and γ subunits. It thereby disrupts ATP synthesis, even with normal translocation of protons through FO
GO:0005515 protein binding	IPI PMID:25168243 Cofactor Strap regulates oxidative phosphorylation and mitoc...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from the Strap/TTC5 study. The study demonstrated a specific interaction between TTC5/Strap and ATP synthase (beta subunit) that downregulates ATP production. Reason: While this is a well-characterized interaction with functional consequences (Strap binding downregulates ATP production), the generic "protein binding" term is uninformative. The interaction is better captured by other annotations in this set. UniProt documents this as "Interacts with TTC5/STRAP; the interaction results in decreased mitochondrial ATP production." Supporting Evidence: PMID:25168243 one of its key interaction partners is ATP synthase. Significantly, the interaction between Strap and ATP synthase downregulates mitochondrial ATP production
GO:0005739 mitochondrion	IDA PMID:25168243 Cofactor Strap regulates oxidative phosphorylation and mitoc...	ACCEPT	Summary: IDA annotation for CC from the Strap study. The study confirmed mitochondrial localization of ATP5F1B through co-localization studies. Reason: Correct. The study demonstrated mitochondrial localization through interaction studies and subcellular fractionation. Supporting Evidence: PMID:25168243 Strap is localised at mitochondria where one of its key interaction partners is ATP synthase
GO:0005515 protein binding	IPI PMID:32243843 Mitoregulin Controls β-Oxidation in Human and Mouse Adipocyt...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from the Mitoregulin study (Friesen et al. 2020). The study showed that Mitoregulin (MTLN) interacts with ATP5F1B. UniProt confirms "Interacts with MTLN". Reason: While the MTLN interaction is documented, the generic "protein binding" term is uninformative. The interaction with Mitoregulin may regulate beta-oxidation but this is not a core function of ATP5F1B.
GO:0042776 proton motive force-driven mitochondrial ATP synthesis	IDA PMID:12110673 A functionally active human F1F0 ATPase can be purified by i...	ACCEPT	Summary: IDA annotation for BP from the immunocapture study. The purified human F1Fo displayed functional ATP hydrolysis activity (reverse of synthesis), confirming the complex's role in mitochondrial ATP synthesis. Reason: Direct functional evidence. The immunocaptured complex from human heart mitochondria showed oligomycin-sensitive ATP hydrolysis activity, confirming the functional involvement of ATP5F1B in the ATP synthesis/hydrolysis cycle. Supporting Evidence: PMID:12110673 The captured complex V displayed ATP hydrolysis activity that was fully oligomycin and inhibitor protein IF(1)-sensitive
GO:0001649 osteoblast differentiation	HDA PMID:16210410 Differential expression profiling of membrane proteins by qu...	MARK AS OVER ANNOTATED	Summary: HDA annotation for BP from a quantitative proteomics study of membrane proteins during osteoblast differentiation of human mesenchymal stem cells (Foster et al. 2005). ATP5F1B was identified as differentially expressed during this process. Reason: This annotation appears to be based on differential protein expression during osteoblast differentiation, not direct involvement in the differentiation process. ATP5F1B expression changes likely reflect altered metabolic demands during differentiation rather than a specific role in osteoblast biology. Supporting Evidence: PMID:16210410 We identified 463 unique proteins with extremely high confidence
GO:0016020 membrane	HDA PMID:16210410 Differential expression profiling of membrane proteins by qu...	ACCEPT	Summary: HDA annotation for CC from the same osteoblast differentiation proteomics study. ATP5F1B was detected in the membrane fraction. Reason: Correct but very broad. ATP5F1B is associated with the mitochondrial inner membrane. Detection in a membrane fraction is consistent with this.
GO:0045259 proton-transporting ATP synthase complex	IDA PMID:21106936 Regenerative protein thymosin beta-4 is a novel regulator of...	ACCEPT	Summary: IDA annotation for CC from the thymosin beta-4 study. The study identified F1-F0 ATP synthase on the endothelial cell surface using pulldown and mass spectrometry. Reason: Correct. The study demonstrated the presence of ATP synthase complex on endothelial cell surfaces, consistent with the ecto-ATP synthase literature. Supporting Evidence: PMID:21106936 we identified F1-F0 ATP synthase, a known target of antiangiogenic angiostatin. By surface plasmon resonance, we determined for Tβ4 binding to the β subunit of ATP synthase a K(D) of 12 nM
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism	IMP PMID:21106936 Regenerative protein thymosin beta-4 is a novel regulator of...	KEEP AS NON CORE	Summary: IMP annotation for MF from the thymosin beta-4 study. The study showed that ATP synthase inhibitors (oligomycin, piceatannol, angiostatin) blocked cell surface ATP generation, demonstrating functional ATP synthase activity on the cell surface. Reason: This demonstrates functional ATP synthase activity on the cell surface (ecto-ATP synthase), which is a real but non-core function. The MF annotation is correct but relates to the non-canonical cell surface localization. Supporting Evidence: PMID:21106936 Blocking antibodies and antagonists (oligomycin, IC(50) ∼1.8 μM; piceatannol, IC(50) ∼1.05 μM; and angiostatin, IC(50) ∼2.9 μg/ml) of ATP synthase inhibited the Tβ4-induced increase in cell surface ATP levels
GO:0005515 protein binding	IPI PMID:21106936 Regenerative protein thymosin beta-4 is a novel regulator of...	MARK AS OVER ANNOTATED	Summary: IPI protein binding from the thymosin beta-4 study. The study identified ATP5F1B as an interactor of thymosin beta-4 with high affinity (Kd = 12 nM). Reason: While the thymosin beta-4 interaction is well-characterized (Kd = 12 nM by SPR), the generic "protein binding" term is uninformative. The angiostatin binding annotation (GO:0043532) from the same study is more informative. Supporting Evidence: PMID:21106936 we determined for Tβ4 binding to the β subunit of ATP synthase a K(D) of 12 nM
GO:0016020 membrane	IDA PMID:21106936 Regenerative protein thymosin beta-4 is a novel regulator of...	ACCEPT	Summary: IDA annotation for CC from the thymosin beta-4 study. ATP5F1B detected in membrane fraction of endothelial cells. Reason: Correct but very broad. ATP5F1B is associated with membranes both as part of the mitochondrial inner membrane complex and as ecto-ATP synthase on the cell surface.
GO:0043532 angiostatin binding	IPI PMID:21106936 Regenerative protein thymosin beta-4 is a novel regulator of...	KEEP AS NON CORE	Summary: IPI annotation for MF from the thymosin beta-4 study. The study showed that angiostatin binds to and inhibits cell surface ATP synthase, and used angiostatin as an antagonist (IC50 ~2.9 ug/ml). Reason: Angiostatin binding to the beta subunit of cell surface ATP synthase is well documented in the ecto-ATP synthase literature (PMID:17510399, PMID:21106936). This is a real binding activity but relates to the non-canonical cell surface function rather than the core mitochondrial role. Supporting Evidence: PMID:21106936 Blocking antibodies and antagonists (oligomycin, IC(50) ∼1.8 μM; piceatannol, IC(50) ∼1.05 μM; and angiostatin, IC(50) ∼2.9 μg/ml) of ATP synthase inhibited the Tβ4-induced increase in cell surface ATP levels
GO:0070062 extracellular exosome	HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres...	KEEP AS NON CORE	Summary: HDA annotation for CC from proteomic analysis of exosomes from expressed prostatic secretions in urine. Reason: Detection of ATP5F1B in extracellular exosomes is consistent with the known presence of mitochondrial proteins in exosomes. This is a non-core localization. ATP5F1B is one of the most abundant mitochondrial proteins, and abundant proteins are commonly detected in exosome proteomics.
GO:0016020 membrane	HDA PMID:19946888 Defining the membrane proteome of NK cells.	ACCEPT	Summary: HDA annotation for CC from NK cell membrane proteome study. ATP5F1B detected in the membrane proteome of NK cells. Reason: Correct but broad. Detection in membrane fractions is consistent with the mitochondrial inner membrane association and/or cell surface ecto-ATP synthase presence. NK cells are known to have cell surface ATP synthase which is involved in immune cytotoxicity (PMID:8006588).
GO:0005634 nucleus	HDA PMID:21630459 Proteomic characterization of the human sperm nucleus.	MARK AS OVER ANNOTATED	Summary: HDA annotation for CC from proteomic characterization of the human sperm nucleus. ATP5F1B detected in the sperm nuclear fraction. Reason: Detection of ATP5F1B in sperm nuclear fractions is likely a contamination artifact from the abundant mitochondrial sheath surrounding the sperm nucleus. Mitochondrial proteins are common contaminants in nuclear preparations, especially from sperm where mitochondria are densely packed around the flagellum adjacent to the nucleus. There is no evidence for a functional role of ATP5F1B in the nucleus.
GO:0005739 mitochondrion	HDA PMID:20833797 Phosphoproteome analysis of functional mitochondria isolated...	ACCEPT	Summary: HDA annotation for CC from phosphoproteome analysis of functional mitochondria from resting human muscle. ATP5F1B identified as a phosphorylated mitochondrial protein. Reason: Correct. Detection in isolated functional mitochondria from human muscle tissue provides strong evidence for mitochondrial localization. The phosphorylation data is consistent with UniProt PTM annotations (Ser-415, Ser-529 phosphorylation).
GO:0070062 extracellular exosome	HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid...	KEEP AS NON CORE	Summary: HDA annotation for CC from proteomic analysis of human parotid gland exosomes. Reason: Detection in parotid gland exosomes. Non-core localization, likely reflecting abundance of the protein.
GO:0070062 extracellular exosome	HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos...	KEEP AS NON CORE	Summary: HDA annotation for CC from large-scale proteomics of urinary exosomes. Reason: Non-core localization. Detection in urinary exosomes likely reflects protein abundance.
GO:0070062 extracellular exosome	HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote...	KEEP AS NON CORE	Summary: HDA annotation for CC from MHC class II-associated proteins in B-cell exosomes study. Reason: Non-core localization. Detection in B-cell exosomes.
GO:0042645 mitochondrial nucleoid	IDA PMID:18063578 The layered structure of human mitochondrial DNA nucleoids.	KEEP AS NON CORE	Summary: IDA annotation for CC from the study on layered structure of human mitochondrial DNA nucleoids (Bogenhagen et al. 2008). ATP5F1B was identified in native nucleoid preparations but was characterized as a peripheral rather than core nucleoid component. Reason: The study identified ATP5F1B in nucleoid preparations but noted that metabolic proteins and chaperones in native nucleoids may represent peripheral associations rather than core components. The authors describe a layered nucleoid structure where "translation and complex assembly may occur in the peripheral region." ATP5F1B association with nucleoids likely reflects proximity during complex assembly rather than a direct role in mtDNA maintenance. Supporting Evidence: PMID:18063578 Several other metabolic proteins and chaperones identified in native nucleoids
GO:0001525 angiogenesis	IMP PMID:17510399 Angiostatin-like activity of a monoclonal antibody to the ca...	KEEP AS NON CORE	Summary: IMP annotation for BP from the angiostatin-like activity study (Chi et al. 2007). The study showed that a monoclonal antibody against ATP5F1B inhibited tube formation and ATP generation by cell surface ATP synthase, demonstrating a role in angiogenesis. Reason: This relates to the ecto-ATP synthase function on endothelial cell surfaces. Blocking cell surface ATP synthase inhibits tube formation (a hallmark of angiogenesis). This is a real but non-core function of ATP5F1B. Supporting Evidence: PMID:17510399 MAb3D5AB1 disrupts tube formation and decreases intracellular pH in endothelial cells exposed to low extracellular pH
GO:0006754 ATP biosynthetic process	IMP PMID:17510399 Angiostatin-like activity of a monoclonal antibody to the ca...	KEEP AS NON CORE	Summary: IMP annotation for BP from the angiostatin-like activity study. The study demonstrated that blocking cell surface ATP synthase with antibodies inhibited ATP generation. Reason: This relates to extracellular ATP generation by cell surface ATP synthase rather than mitochondrial ATP synthesis. Real but non-core function. Supporting Evidence: PMID:17510399 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
GO:0009986 cell surface	IDA PMID:17510399 Angiostatin-like activity of a monoclonal antibody to the ca...	KEEP AS NON CORE	Summary: IDA annotation for CC. The study demonstrated cell surface localization of ATP5F1B on endothelial cells using antibody binding and functional assays. Reason: Cell surface localization of ATP5F1B is well documented in the ecto-ATP synthase literature. This is a real but non-canonical localization, distinct from the primary mitochondrial localization. Supporting Evidence: PMID:17510399 The antiangiogenic protein angiostatin inhibits ATP synthase on the endothelial cell surface
GO:0042288 MHC class I protein binding	IDA PMID:17643490 Ecto-F1-ATPase and MHC-class I close association on cell mem...	KEEP AS NON CORE	Summary: IDA annotation for MF from the ecto-F1-ATPase and MHC-class I study (Vantourout et al. 2008). The study demonstrated close association and co-immunoprecipitation of ecto-F1-ATPase beta chain with MHC class I molecules on cell membranes. Reason: This is a well-documented interaction at the cell surface where ecto-F1-ATPase associates with MHC class I molecules. The interaction is relevant to gammadelta T cell recognition and immune function, but this is a non-core function of ATP5F1B. Supporting Evidence: PMID:17643490 biotinylated F1-ATPase cell surface components co-immunoprecipitate with MHC-I molecules confirming the association of both complexes on Raji cells. Confocal microscopy analysis of MHC-I and ecto-F1-ATPase beta chain expression on HepG2 cells shows a co-localization of both complexes in punctate membrane domains
GO:0046961 proton-transporting ATPase activity, rotational mechanism	IMP PMID:17510399 Angiostatin-like activity of a monoclonal antibody to the ca...	KEEP AS NON CORE	Summary: IMP annotation for MF. Note this is the ATPase (hydrolysis) direction, not synthase. The study demonstrated that cell surface ATP synthase also has ATPase (hydrolytic) activity that was inhibited by the anti-beta antibody. Reason: This annotation for ATPase activity (hydrolysis direction) on the cell surface is supported by the study. The cell surface enzyme can work in both directions. Non-core as it relates to ecto-ATP synthase. Supporting Evidence: PMID:17510399 MAb3D5AB1 inhibits the hydrolytic activity of F(1) ATP synthase at lower concentrations than angiostatin
GO:0051453 regulation of intracellular pH	IMP PMID:17510399 Angiostatin-like activity of a monoclonal antibody to the ca...	KEEP AS NON CORE	Summary: IMP annotation for BP. The study showed that blocking cell surface ATP synthase with antibodies decreased intracellular pH in endothelial cells at low extracellular pH. Reason: This is a downstream consequence of ecto-ATP synthase activity on pH regulation. Non-core pleiotropic effect of the cell surface function. Supporting Evidence: PMID:17510399 MAb3D5AB1 disrupts tube formation and decreases intracellular pH in endothelial cells exposed to low extracellular pH
GO:1902600 proton transmembrane transport	IMP PMID:17510399 Angiostatin-like activity of a monoclonal antibody to the ca...	KEEP AS NON CORE	Summary: IMP annotation for BP from the cell surface ATP synthase study. Proton transport activity of the cell surface ATP synthase. Reason: This relates to proton transport by cell surface ATP synthase. While proton transport is a core function in the mitochondrial context, here it refers to the ecto-enzyme. The IEA annotation for the same term covers the general case.
GO:0005739 mitochondrion	IDA PMID:2870059 Human F1-ATPase: molecular cloning of cDNA for the beta subu...	ACCEPT	Summary: IDA annotation for CC from the original cDNA cloning study (Ohta & Kagawa 1986). The study established that the protein has a mitochondrial transit peptide and localizes to mitochondria. Reason: Correct. The founding study established that the beta subunit is a mitochondrial protein with a presequence (transit peptide) for mitochondrial import. Supporting Evidence: PMID:2870059 The open reading frame started from a putative signal presequence, which was rich in both serine and arginine
GO:0005759 mitochondrial matrix	NAS PMID:2687158 The human ATP synthase beta subunit gene: sequence analysis,...	ACCEPT	Summary: NAS annotation for CC from the gene sequence/expression study (Neckelmann et al. 1989). The study described the gene encoding the beta subunit which is imported to the mitochondrial matrix. Reason: Correct. The beta subunit resides on the matrix side of the inner mitochondrial membrane as part of the F1 head. Supporting Evidence: PMID:2687158 the functional F0F1-ATP synthase beta subunit gene is located on chromosome 12
GO:0005886 plasma membrane	IDA PMID:10077593 Angiostatin binds ATP synthase on the surface of human endot...	UNDECIDED	Summary: IDA annotation for CC. Publication not cached (PMID:10077593). Based on the title and context, this likely documents the ecto-ATP synthase on the plasma membrane. Reason: Cannot fully assess without the publication. However, plasma membrane localization of ATP5F1B is well supported by the ecto-ATP synthase literature (PMID:8006588, PMID:17510399). If confirmed, this would be a non-core localization.
GO:0006091 generation of precursor metabolites and energy	NAS PMID:2870059 Human F1-ATPase: molecular cloning of cDNA for the beta subu...	ACCEPT	Summary: NAS annotation for BP from the original cDNA cloning study. Generation of precursor metabolites and energy is the broad process encompassing oxidative phosphorylation. Reason: Correct but very broad. ATP synthesis by the F1Fo-ATP synthase is a central part of energy generation. More specific annotations are present (GO:0042776, GO:0015986). Supporting Evidence: PMID:2870059 F1-ATPase is the major enzyme for ATP synthesis
GO:0031966 mitochondrial membrane	IDA PMID:8006588 A novel ligand in lymphocyte-mediated cytotoxicity: expressi...	ACCEPT	Summary: IDA annotation for CC from the study demonstrating beta subunit expression on tumor cell surfaces (Das et al. 1994). While the study focused on cell surface expression, the protein was identified as having "structural and immunologic characteristics of the beta subunit of H+ transporting ATP synthase" from mitochondria. Reason: Correct. ATP5F1B is associated with the mitochondrial inner membrane as part of the ATP synthase complex. The study confirmed the identity of the cell surface protein as the mitochondrial beta subunit. Supporting Evidence: PMID:8006588 A 51.5-kD protein (p51.5) bearing structural and immunologic characteristics of the beta subunit of H+ transporting ATP synthase
GO:0005515 protein binding	IPI PMID:10077593 Angiostatin binds ATP synthase on the surface of human endot...	UNDECIDED	Summary: IPI protein binding annotation. Publication not cached (PMID:10077593). Reason: Cannot assess without access to the publication. Generic protein binding is uninformative.

Gene Description

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