ATP6V1B1 encodes the B1 isoform of the non-catalytic B subunit of the V-ATPase V1 sector. B1 supports assembly and operation of the ATP-driven proton pump rather than independently hydrolyzing ATP or forming a proton pore. In renal epithelia, B1-containing pumps at the apical membrane contribute to urinary acidification and systemic acid-base balance. B1 is also expressed in the cochlea and endolymphatic sac, and pathogenic variants cause distal renal tubular acidosis with sensorineural hearing loss. Its conserved nucleotide-binding property is inferred from related B subunits, while disease-associated B1 variants can disrupt complex assembly and trafficking.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:1902600 proton transmembrane transport | IBA GO_REF:0000033 | ACCEPT | Summary: Conserved proton transport is a core pump function. Reason: The PAINT assertion places proton transport in the inherited function of the V-ATPase family. B1 supplies an active structural contribution to pump assembly and operation, corroborated by B1-mutant coassembly and pH-transport observations in PMID:16769747. No donor-count or self-source objection is warranted. |
| GO:0000221 vacuolar proton-transporting V-type ATPase, V1 domain | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT V1-sector membership agrees with B1 identity. Reason: The PAINT V1-domain membership is consistent with B1 identity, its conserved subunit architecture and B1-containing complexes in PMID:16769747. Preserve the phylogenetic assertion. PMID:33065002 is family-level structural context because its identified human preparation contains B2; it is not substituted as a direct B1 structure. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Plasma-membrane activity is a location of the pump core. Reason: The PAINT is_active_in assertion places the B1-containing pump at the plasma membrane, where renal proton secretion is a central function. Human kidney apical-domain localization in PMID:29993276 independently corroborates this compartment. ACCEPT therefore reflects an actual location of the one pump core; the more specific apical row does not turn its parent into a separate non-core function. The ancestral PAINT node has not been newly reconstructed. |
| GO:0016324 apical plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Apical-membrane activity is supported by human kidney localization. Reason: The PAINT apical-membrane localization is consistent with the renal B1 pump role and human kidney light-microscopy localization in PMID:29993276. Rat immunoelectron microscopy in that study is separate evidence and is not described as a human ultrastructural experiment. |
| GO:0007035 vacuolar acidification | IBA GO_REF:0000033 | ACCEPT | Summary: Acidification is an inherited function of the assembled pump. Reason: The phylogenetically inherited acidification role agrees with B1 contribution to functional V-ATPase complexes. Retain the existing process without claiming that every intracellular compartment contains the same B-subunit isoform, or adding a separate lysosomal process from unverified provider statements. |
| GO:0000221 vacuolar proton-transporting V-type ATPase, V1 domain | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA V1-sector membership agrees with B1 coassembly. Reason: The ARBA V1-domain assignment agrees with B1 subunit identity and experimental B1 coassembly in PMID:16769747. It supports membership of the ATP-hydrolytic sector, without asserting that isolated B1 catalyzes ATP hydrolysis. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding is inferred from the conserved B-subunit nucleotide site. Reason: The InterPro ATP-binding inference agrees with the conserved non-catalytic B-subunit nucleotide site. Immutable UniProt residue 394 is annotated by similarity to B2/P21281. This is inferred B1 nucleotide binding, not a direct B1-binding measurement from the B2-containing human structure in PMID:33065002. |
| GO:0016323 basolateral plasma membrane | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Basolateral localization is retained as polarized-cell context. Reason: The combined electronic basolateral assignment is corroborated by the immutable UniProt transfer from mouse Q91YH6. Retain this contextual polarized-membrane localization without treating all B1-containing pumps as basolateral or making it a second core function. |
| GO:0016324 apical plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: The electronic apical-membrane assignment has independent localization support. Reason: The combined electronic apical-membrane assignment agrees with direct human kidney localization in PMID:29993276 and the B1 fusion-protein observations in the rat IMCD host of PMID:16769747. The expressed cDNA species in the latter abstract remains unspecified. |
| GO:0033180 proton-transporting V-type ATPase, V1 domain | IEA GO_REF:0000002 | ACCEPT | Summary: The general V1-domain assignment describes B1 complex membership. Reason: InterPro identifies the conserved proton-transporting V-ATPase V1-domain subunit. This is the appropriate complex-membership context for B1; the general V1 term is not erroneous merely because a more specific V1 term also occurs. |
| GO:0046034 ATP metabolic process | IEA GO_REF:0000002 | ACCEPT | Summary: ATP metabolism is a mechanistic facet of the assembled pump. Reason: The ATP-dependent reaction of the assembled proton pump is part of its core mechanism. In PMID:16769747, wild-type GFP-B1 coassembles with other subunits and the immunoprecipitated complex has ATPase activity, whereas tested B1 mutant preparations do not. B1 supplies structural work to that ATP-hydrolyzing complex, so the existing involved_in assertion is retained as core. This does not assign isolated-subunit catalysis or ATP synthesis to B1; the expressed cDNA species remains unspecified in the abstract, which explicitly names a rat IMCD host. |
| GO:0046961 proton-transporting ATPase activity, rotational mechanism | IEA GO_REF:0000002 | ACCEPT | Summary: B1 contributes to rotary proton-pump activity. Reason: The InterPro pump-activity assignment reflects B1 contribution to the rotary V-ATPase. B1 coassembly supports ATPase activity of the immunoprecipitated complex in PMID:16769747. This is central holoenzyme function, not an autonomous B1 enzyme; preserve the machine qualifier and express the synthesized core through contributes_to_molecular_function. |
| GO:1902600 proton transmembrane transport | IEA GO_REF:0000120 | ACCEPT | Summary: B1-containing complexes support proton transmembrane transport. Reason: The combined electronic proton-transport assertion is consistent with B1-dependent assembly and operation of the V-ATPase. The pH-transport phenotype in PMID:16769747 corroborates complex function; B1 is not itself a membrane-spanning proton channel. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | UNDECIDED | Summary: The interaction-screen assertion awaits target-pair evidence. Reason: The complete PMID:32814053 abstract describes a systematic interaction screen but does not expose the exact ATP6V1B1 partner, constructs and target-level validation underlying this IPI row. Preserve the original assertion as UNDECIDED until those records are inspected. No informative replacement molecular function or biological contradiction has been established for this pair. |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cytoplasm is retained as subunit and assembly context. Reason: The Ensembl cytoplasmic localization is consistent with the peripheral cytoplasmic V1 sector and its soluble or assembling pool. It is retained as cellular context, not evidence for an additional independent cytoplasmic molecular activity. |
| GO:0005829 cytosol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cytosol is retained as peripheral V1 context. Reason: The Ensembl cytosolic localization is consistent with the peripheral V1 head. It is retained as context for the subunit and its assembling pool, without implying that ATP6V1B1 independently executes every cytosolic pathway in which a V-ATPase complex is represented. |
| GO:0005902 microvillus | IEA GO_REF:0000107 | UNDECIDED | Summary: Microvillus-specific donor evidence remains unresolved. Reason: The precise Ensembl donor assay for microvillus localization was not inspected. Apical-domain localization alone does not establish the microvillus subcompartment, and the available PMID:14585495 abstract does not resolve that detail. Preserve the electronic source while deferring this more specific location. |
| GO:0015078 proton transmembrane transporter activity | IEA GO_REF:0000107 | ACCEPT | Summary: The transporter assignment describes contribution to the assembled pump. Reason: The transferred proton-transporter activity is consistent with B1 participation in the functional proton pump. PMID:16769747 supports the assembled complex through coassembly and pH-transport effects. Its non-autonomous contribution is still core biology; no B1-only proton pore is asserted. |
| GO:0016020 membrane | IEA GO_REF:0000107 | MODIFY | Summary: Refine generic membrane localization to plasma membrane. Reason: The generic electronic membrane location can be made more informative using independently supported plasma-membrane localization. PMID:29993276 reports human kidney B1 localization, and PMID:16769747 reports apical B1 fusion proteins in a rat IMCD host. Plasma membrane accommodates the established polarized-cell contexts without asserting that the uninspected Ensembl donor measured only the apical domain. This is a refinement of the existing broad assertion, not a NEW annotation or additional core. Proposed replacements: plasma membrane |
| GO:0016328 lateral plasma membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The exact lateral-membrane donor evidence remains unresolved. Reason: The precise lateral-membrane donor localization was not inspected. The immutable UniProt basolateral transfer does not by itself resolve lateral versus basal domains, and the available mouse-source abstract does not expose the relevant images. Preserve this assertion pending that compartment-specific evidence. |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | UNDECIDED | Summary: The target complex in this binding transfer remains unresolved. Reason: The Ensembl protein-containing-complex binding donor and target complex are unresolved. The term could describe binding to an external complex rather than membership of the V-ATPase itself. The earlier assumption that it merely repeats complex membership is insufficient to judge the assertion. |
| GO:0097401 synaptic vesicle lumen acidification | IEA GO_REF:0000107 | UNDECIDED | Summary: The B1-specific synaptic-acidification transfer remains unresolved. Reason: The exact B1 synaptic-acidification transfer remains unresolved. The prior donor audit traced curated mouse experimental annotations to a study whose inspected mechanistic sections use V1B2; complete donor mapping and additional assays were not established. This does not justify a blanket claim that B1 cannot have neuronal functions, nor a positive B1 synaptic core. |
| GO:0098850 extrinsic component of synaptic vesicle membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The synaptic-vesicle membrane assertion lacks a resolved B1 donor route. Reason: The Ensembl assertion concerns activity at the extrinsic component of the synaptic-vesicle membrane. Its precise B1 donor route is not established by the inspected material. Retain the is_active_in source qualifier and defer the assertion, without inferring absence from the older kidney/testis Northern survey. |
| GO:0016323 basolateral plasma membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The curated basolateral transfer is retained as non-core context. Reason: The curated sequence-similarity basolateral localization agrees with the immutable UniProt mouse-Q91YH6 transfer. Retain this orthology-based context while distinguishing it from direct human apical localization and from an independently measured lateral-only compartment. |
| GO:0097254 renal tubular secretion | IMP PMID:12414817 Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive... | ACCEPT | Summary: Renal acid secretion is a physiological expression of pump function. Reason: PMID:12414817 directly links human ATP6V1B1 defects to recessive distal renal tubular acidosis and defective apical proton-pump function. Renal acid secretion is an established physiological expression of the pump core; the clinical-genetic evidence is not described as a purified B1 assay. |
| GO:0000221 vacuolar proton-transporting V-type ATPase, V1 domain | IDA PMID:33065002 Structures of a Complete Human V-ATPase Reveal Mechanisms of... | ACCEPT | Summary: Accept V1 membership while distinguishing the structural paper’s B2 preparation. Reason: B1 membership in the V1 sector is established by its subunit identity and independently supported B1 coassembly in PMID:16769747. Accept the existing curated IDA assertion without treating incomplete source inspection as a reason to reject an established function. Separately, the original PMID:33065002 Results, Structure Determination and Overall Architectures (https://pmc.ncbi.nlm.nih.gov/articles/PMC7655608/), identify B2 in the analyzed preparation. That external observation is structural context, not a direct B1 assay or an exhaustive finding that the curator was wrong. The precise IDA provenance remains a documentation question. |
| GO:0016324 apical plasma membrane | IDA PMID:16769747 Vacuolar H+ -ATPase B1 subunit mutations that cause inherite... | ACCEPT | Summary: The B1 fusion-protein study supports apical localization. Reason: PMID:16769747 reports apical GFP-B1 wild-type and mutant fusion proteins in a rat IMCD host. The abstract leaves expressed cDNA species unspecified; human kidney apical-domain localization is independently corroborated by PMID:29993276. Retain the source without relabeling the host experiment as human. |
| GO:0016324 apical plasma membrane | IDA PMID:29993276 H(+)-ATPase B1 subunit localizes to thick ascending limb and... | ACCEPT | Summary: Human kidney staining supports the apical compartment. Reason: PMID:29993276 supports apical-domain B1 staining in human kidney and rodent kidney. Human light-microscopy observations are distinguished from the rat immunoelectron microscopy. These localization data do not establish the quantitative acid-transport contribution of human TAL or DCT cells. |
| GO:0045851 pH reduction | IMP PMID:16769747 Vacuolar H+ -ATPase B1 subunit mutations that cause inherite... | ACCEPT | Summary: B1 mutant effects support the pump’s pH-reduction role. Reason: PMID:16769747 reports inhibition of proton-pump-mediated intracellular pH transport by B1-mutant fusion proteins in rat IMCD cells. This supports the pH-reduction role of functional B1-containing complexes, with construct species unassigned and no isolated B1 catalytic claim. |
| GO:0070072 vacuolar proton-transporting V-type ATPase complex assembly | IMP PMID:16769747 Vacuolar H+ -ATPase B1 subunit mutations that cause inherite... | ACCEPT | Summary: B1 coassembly is experimentally connected to pump assembly. Reason: The B1-mutant coimmunoprecipitation results in PMID:16769747 directly concern assembly: wild-type GFP-B1 associates with other V-ATPase subunits whereas the tested mutant preparations do not. Preserve this existing assembly process; it need not be manufactured as a NEW assertion. |
| GO:1902600 proton transmembrane transport | IMP PMID:16769747 Vacuolar H+ -ATPase B1 subunit mutations that cause inherite... | ACCEPT | Summary: B1 mutant effects connect assembly to proton transport. Reason: The B1-mutant study PMID:16769747 connects defective coassembly and trafficking to impaired proton-pump-mediated pH transport. It supports B1 contribution to transmembrane proton pumping by the complex in the rat IMCD host; donor cDNA species remains unverified. |
| GO:0016241 regulation of macroautophagy | NAS PMID:22982048 Lipofuscin is formed independently of macroautophagy and lys... | UNDECIDED | Summary: The B1-specific macroautophagy assertion remains unresolved. Reason: The available PMID:22982048 abstract concerns lipofuscin formation and macroautophagy in senescent human fibroblasts, but does not resolve the B1-specific NAS assertion. Full relevant text was not obtained in this audit. Defer rather than infer a wrong gene or assert that B1 has no autophagy role. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | KEEP AS NON CORE | Summary: Detected in an extracellular-vesicle proteome. The protein is plausible EV content, but this is not where it functions. Reason: V-ATPase V1 subunit of the apical membrane of renal intercalated cells. Cytosolic protein with lipid or membrane-protein binding ability; MISEV2018 (PMID:30637094) category 2a lists such proteins (ESCRT components, ALIX, annexins, HSPA8 and others) as expected EV contents. True, but not its core location. (Manual re-review for OMICS_EVIDENCE, 2026-10-10; previous action: UNDECIDED.) |
| GO:0070062 extracellular exosome | HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid... | KEEP AS NON CORE | Summary: Detected in an extracellular-vesicle proteome. The protein is plausible EV content, but this is not where it functions. Reason: V-ATPase V1 subunit of the apical membrane of renal intercalated cells. Cytosolic protein with lipid or membrane-protein binding ability; MISEV2018 (PMID:30637094) category 2a lists such proteins (ESCRT components, ALIX, annexins, HSPA8 and others) as expected EV contents. True, but not its core location. (Manual re-review for OMICS_EVIDENCE, 2026-10-10; previous action: UNDECIDED.) |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: Detected in an extracellular-vesicle proteome. The protein is plausible EV content, but this is not where it functions. Reason: V-ATPase V1 subunit of the apical membrane of renal intercalated cells. Cytosolic protein with lipid or membrane-protein binding ability; MISEV2018 (PMID:30637094) category 2a lists such proteins (ESCRT components, ALIX, annexins, HSPA8 and others) as expected EV contents. True, but not its core location. (Manual re-review for OMICS_EVIDENCE, 2026-10-10; previous action: UNDECIDED.) |
| GO:0005737 cytoplasm | ISS PMID:14585495 Molecular cloning and characterization of Atp6v1b1, the muri... | KEEP AS NON CORE | Summary: Mouse orthology supports contextual cytoplasmic localization. Reason: The mouse-orthology source PMID:14585495 establishes the murine B1 ortholog and intercalated-cell expression. Cytoplasmic localization is compatible with the peripheral V1 sector and is retained as context; the source is not relabeled as a direct human assay. |
| GO:0005902 microvillus | ISS PMID:14585495 Molecular cloning and characterization of Atp6v1b1, the muri... | UNDECIDED | Summary: The mouse microvillus localization panels were not inspected. Reason: The complete PMID:14585495 abstract establishes the mouse ortholog and kidney intercalated-cell localization, but not the precise microvillus compartment. The relevant full localization panels were unavailable in this bounded reading. Defer that specific ISS assertion while preserving its mouse-to-human provenance. |
| GO:0016323 basolateral plasma membrane | ISS PMID:14585495 Molecular cloning and characterization of Atp6v1b1, the muri... | KEEP AS NON CORE | Summary: Mouse basolateral localization is retained as contextual evidence. Reason: The PMID:14585495 mouse-orthology localization is compatible with the independently retained UniProt basolateral transfer from Q91YH6. Retain this context without implying a universal membrane polarity or direct human measurement in the mouse paper. |
| GO:0016328 lateral plasma membrane | ISS PMID:14585495 Molecular cloning and characterization of Atp6v1b1, the muri... | UNDECIDED | Summary: The mouse lateral-only localization panels were not inspected. Reason: The mouse-source PMID:14585495 abstract does not resolve lateral-only localization. Basolateral location in UniProt is broader and cannot substitute for an uninspected lateral-domain panel. Preserve the ISS record and defer this subcompartment assertion. |
| GO:0015078 proton transmembrane transporter activity | ISS PMID:14585495 Molecular cloning and characterization of Atp6v1b1, the muri... | ACCEPT | Summary: The orthology assignment agrees with B1 pump contribution. Reason: The mouse-orthology proton-transporter assertion is consistent with conserved B1 participation in V-ATPase assembly and operation, independently corroborated by PMID:16769747. A structural contribution to the assembled transporter remains core function; it need not be an autonomous B1 channel. |
| GO:0042472 inner ear morphogenesis | IMP PMID:19639346 Inner ear abnormalities in four patients with dRTA and SNHL:... | KEEP AS NON CORE | Summary: Inner-ear morphology is retained as a downstream clinical context. Reason: PMID:19639346 links human ATP6V1B1 variants, hearing impairment and enlarged vestibular aqueduct. Retain this existing developmental context as non-core, while the clinical abstract does not establish a distinct morphogenetic molecular activity or prove that every ear abnormality follows the same mechanism. |
| GO:0007605 sensory perception of sound | IMP PMID:20622307 Distal renal tubular acidosis and its relationship with hear... | KEEP AS NON CORE | Summary: Hearing is retained as a physiological consequence of pump function. Reason: PMID:20622307 reports the clinical association of ATP6V1B1 variants with sensorineural hearing loss. This is a supported downstream physiological context of the proton-pump system, not a second molecular-function core or a direct auditory-cell proton-flux assay. |
| GO:0045851 pH reduction | IMP PMID:20622307 Distal renal tubular acidosis and its relationship with hear... | ACCEPT | Summary: Clinical genetics corroborates the pH-reduction role. Reason: The clinical-genetic source PMID:20622307 places ATP6V1B1 defects in distal renal tubular acidosis. The pH-reduction function is corroborated more directly by B1-mutant pump experiments in PMID:16769747. Retain the core process without describing this clinical paper as a biochemical pH assay. |
| GO:0055074 calcium ion homeostasis | IMP PMID:20622307 Distal renal tubular acidosis and its relationship with hear... | UNDECIDED | Summary: The cited calcium-homeostasis endpoints remain unresolved. Reason: The available PMID:20622307 clinical abstract does not expose the calcium-homeostasis endpoints underlying this IMP annotation. It cannot establish that such endpoints were absent from the full study or necessarily indirect. Preserve the assertion and defer adjudication pending the relevant clinical measurements. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1222516 | KEEP AS NON CORE | Summary: Retain the phagosomal-acidification event’s cytosolic context. Reason: R-HSA-1222516 describes proton pumping that acidifies the phagosomal lumen. Retain its cytosolic assignment as context for the peripheral V1 component of the represented pump. The pump contributes to acidification; this location row does not establish a separate B1-specific phagosomal mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5252133 | KEEP AS NON CORE | Summary: Retain cytosolic context for ATP6AP1–V-ATPase association. Reason: R-HSA-5252133 describes ATP6AP1 association with V-ATPase and accessory-subunit contributions to acidification. Retain the cytosolic context of the represented V1 component. The event does not by itself establish a direct B1–ATP6AP1 interaction or transfer ATP6AP1-specific mouse osteoclast results to B1. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-74723 | KEEP AS NON CORE | Summary: Retain the endosome-acidification event’s cytosolic context. Reason: R-HSA-74723 describes entry of protons into the endosome and lumenal pH reduction. Its cytosolic assignment is compatible with the pump’s peripheral V1 sector and is retained as context. It does not require an independent B1 activity beyond contribution to the assembled proton pump. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-917841 | KEEP AS NON CORE | Summary: Retain cytosolic context for the transferrin-endosome event. Reason: The R-HSA-917841 title identifies a transferrin/receptor-containing endosome, whereas the cached generic summary describes phagosomal proton pumping. Retain the source’s cytosolic V1 placement as pathway context without silently treating that generic summary as a B1-specific transferrin-endosome assay. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9639286 | KEEP AS NON CORE | Summary: Retain cytosolic context for RagC/D nucleotide exchange. Reason: R-HSA-9639286 assigns unconventional nucleotide-exchange activity on RagC/D to Ragulator. Retain the cytosolic context of the represented V-ATPase component without attributing that GEF activity to B1. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9640167 | KEEP AS NON CORE | Summary: Retain cytosolic context for RagA/B nucleotide exchange. Reason: R-HSA-9640167 describes RagA/B nucleotide exchange promoted by arginine-bound SLC38A9 and Ragulator. B1’s cytosolic placement is retained as complex context; the source does not assign the exchange chemistry to B1. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9640168 | KEEP AS NON CORE | Summary: Retain cytosolic context for SLC38A9 dissociation. Reason: R-HSA-9640168 describes dissociation of SLC38A9 after RagA nucleotide exchange. The modeled V-ATPase component supplies cytosolic pathway context, without establishing an independent B1-mediated dissociation reaction. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9640175 | KEEP AS NON CORE | Summary: Retain cytosolic context for SLC38A9 association. Reason: R-HSA-9640175 describes association of arginine-bound SLC38A9 through Rag GTPases. Retain B1’s cytosolic placement in the represented complex without inferring a direct B1–SLC38A9 binding interface. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9640195 | KEEP AS NON CORE | Summary: Retain cytosolic context for RagA/B GTP hydrolysis. Reason: R-HSA-9640195 describes RagA/B GTP hydrolysis promoted by the GATOR1 complex. Retain the cytosolic location as pathway context; neither the Rag GTPase reaction nor GATOR1 GAP activity is assigned to B1. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9645598 | KEEP AS NON CORE | Summary: Retain cytosolic context for RagC/D GTP hydrolysis. Reason: R-HSA-9645598 describes RagC/D GTP hydrolysis and FLCN/FNIP GAP activity. Retain B1’s cytosolic complex context without transferring those catalytic functions to a V1 subunit. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9645608 | KEEP AS NON CORE | Summary: Retain cytosolic context for mTORC1 recruitment. Reason: R-HSA-9645608 describes active Rag recruitment of mTORC1 and a requirement for V-ATPase ATP hydrolysis. Retain the source’s cytosolic complex context while distinguishing a complex-level requirement from a demonstrated B1-specific mTORC1-recruitment mechanism. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9646468 | KEEP AS NON CORE | Summary: Retain cytosolic context for RHEB–mTORC1 association. Reason: R-HSA-9646468 describes RHEB association with mTORC1 and stimulation of MTOR kinase activity. Retain the cytosolic placement of the represented V-ATPase component; this is not evidence that B1 performs RHEB signaling or MTOR catalysis. |
| GO:0016324 apical plasma membrane | IDA PMID:16928804 Expression of the ammonia transporter, rh C glycoprotein, in... | ACCEPT | Summary: Retain curated apical localization with independent B1 corroboration. Reason: PMID:16928804 uses H+-ATPase in renal epithelial localization comparisons while studying RhCG. The exact B1 antibody specificity was not independently re-established from the selected material, but human B1 apical localization is corroborated by PMID:29993276. Retain the curated location without inferring RhCG transport activity for B1. |
| GO:0001503 ossification | IMP PMID:16433694 Molecular investigation and long-term clinical progress in G... | UNDECIDED | Summary: The clinical ossification evidence remains unresolved. Reason: The PMID:16433694 clinical-genetic abstract does not resolve the ossification evidence behind this IMP annotation. It is not sufficient to assign all skeletal findings to secondary systemic acidosis or to exclude a more specific role. Defer the assertion rather than use an uninspected mechanism to mark it over-annotated. |
| GO:0006885 regulation of pH | IMP PMID:12414817 Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive... | ACCEPT | Summary: Human genetics supports renal pH regulation. Reason: PMID:12414817 establishes ATP6V1B1-dependent renal acid-base physiology through human distal renal tubular acidosis genetics. Regulation of pH is an established pump-core process, without converting clinical necessity evidence into an autonomous B1 enzyme claim. |
| GO:0016471 vacuolar proton-transporting V-type ATPase complex | IMP PMID:12414817 Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive... | ACCEPT | Summary: Retain the existing V-ATPase complex-membership assertion. Reason: The existing vacuolar V-type ATPase complex membership in PMID:12414817 is consistent with B1 identity and B1-dependent pump assembly. Preserve the machine term; the synthesized core uses the general proton-transporting V-type complex rather than implying that the renal pump is confined to an intracellular vacuole. |
| GO:1902600 proton transmembrane transport | IMP PMID:12414817 Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive... | ACCEPT | Summary: Human genetics corroborates proton secretion by B1-containing pumps. Reason: PMID:12414817 links human B1 defects to failure of renal proton secretion. Together with B1-mutant coassembly and pH-transport evidence, this supports participation in proton transmembrane transport by the assembled V-ATPase. |
| GO:0006885 regulation of pH | IMP PMID:9916796 Mutations in the gene encoding B1 subunit of H+-ATPase cause... | ACCEPT | Summary: Retain the established pH-regulation relationship and source qualifier. Reason: PMID:9916796 identifies human ATP6B1 variants causing impaired renal acid secretion and reports cochlear/endolymphatic-sac expression. Retain the existing acts_upstream_of_or_within qualifier and pH-regulation process without inventing a direct isolated-subunit transport measurement. |
| GO:0007605 sensory perception of sound | IMP PMID:9916796 Mutations in the gene encoding B1 subunit of H+-ATPase cause... | KEEP AS NON CORE | Summary: Retain hearing as a non-core physiological context. Reason: PMID:9916796 links human ATP6B1 variants to hearing loss and reports inner-ear expression, supporting normal auditory-function context. The abstract infers an endolymph-pH connection; it does not directly quantify B1-mediated inner-ear proton flux. Hearing remains a downstream context of one pump core. |
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Download this section (compressed HTML)Q: What exact donor assays support the B1 synaptic-vesicle activity and microvillus/lateral-membrane transfers, and how do they distinguish B1 from B2?
Q: Which B1-specific experiments or curator source mapping underlie the PMID:33065002 IDA membership record, given the B2 identity in its inspected human structural preparation?
Q: What exact target-pair, peptide and clinical endpoint records support the unresolved interaction, vesicle, calcium-homeostasis and ossification assertions?
Q: What is the quantitative acid-transport contribution of B1-positive human TAL/DCT cells, beyond their demonstrated apical localization?
Experiment: Compare defined B1 and B2 preparations in matched complexes with assembly, nucleotide-binding and ATP-dependent proton-flux readouts, separating isolated-subunit properties from holoenzyme activity.
Experiment: Use validated isoform-specific localization and functional perturbation to distinguish B1 from B2 in renal, inner-ear and neuronal contexts.
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