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 Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Large-scale proteomics and phosphoproteomics of urinary exosomes.
mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase.
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Shows V-ATPase is required for lysosomal amino-acid sensing and mTORC1 activation through Rag/Ragulator coupling.
"The v-ATPase is required for amino acid signaling to mTORC1 and functions between amino acids and the nucleotide loading of the Rag GTPases."
ATP6AP1 deficiency causes an immunodeficiency with hepatopathy, cognitive impairment and abnormal protein glycosylation.
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Identifies ATP6AP1/Ac45 deficiency, localizes Ac45 to ER/ERGIC in hepatocytes, and supports a Voa1-like V-ATPase assembly-factor role.
"Processed wild-type Ac45, but not its disease mutants, restored V-ATPase-dependent growth in Voa1 mutant yeast."
The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1α prolyl hydroxylation by regulating cellular iron levels.
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Links ATP6AP1/V-ATPase disruption to intracellular iron depletion and HIF activation in aerobic conditions.
"disrupting the V-ATPase results in intracellular iron depletion, thereby impairing PHD activity and leading to HIF activation."
Mutations in the X-linked ATP6AP2 cause a glycosylation disorder with autophagic defects.
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Shows ATP6AP2 disease mutations impair interaction with ATP6AP1 and supports an ATP6AP-family V0 assembly complex model.
"both ATP6AP2 mutations impaired protein stability and the interaction with ATP6AP1, a member of the V0 assembly complex."
Structure and Roles of V-type ATPases.
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Review source for V-ATPase acidification roles across organelles and specialized plasma membranes.
"V-ATPases are membrane-embedded protein complexes that function as ATP hydrolysis-driven proton pumps."
A SARS-CoV-2 protein interaction map reveals targets for drug repurposing.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.
Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.
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Cryo-EM study of complete human V-ATPase defining ATP6AP1 as a structural hub for V0 assembly.
"We define ATP6AP1 as a structural hub for Vo complex assembly because it connects to multiple Vo subunits and phospholipids in the c-ring."
Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV.
Interactomes of SARS-CoV-2 and human coronaviruses reveal host factors potentially affecting pathogenesis.
SARS-CoV-2 non-structural protein 6 triggers NLRP3-dependent pyroptosis by targeting ATP6AP1.
Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci.
ATP6AP1 binds V-ATPase
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Reactome event placing ATP6AP1 as an accessory V0 subunit that facilitates V-ATPase acidification.
"V-type proton ATPase subunit S1 (ATP6AP1) is thought to function as an accessory subunit of the V0 subcomplex of V-ATPase, facilitating acidification"
Acidification of Tf:TfR1 containing endosome
Proteostasis PN projected annotations report
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Projects ATP6AP1 to GO:0060590 ATPase regulator activity from regulator-of-lysosomal-V-ATPase PN leaves and recognizes GO:0007042 lysosomal lumen acidification as already present in GOA.
"ATPase regulator activity is the narrowest GO target that preserves the source mechanism without requiring a speculative complex-specific term."