GO_REF:0000002
Gene Ontology annotation through association of InterPro records with GO terms
GO_REF:0000024
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
GO_REF:0000033
Annotation inferences using phylogenetic trees
GO_REF:0000044
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
GO_REF:0000107
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
PMID:10973252
Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing.
PMID:12414817
Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss.
PMID:12649290
The a-subunit of the V-type H+-ATPase interacts with phosphofructokinase-1 in humans.
PMID:14638902
Localization and regulation of the ATP6V0A4 (a4) vacuolar H+-ATPase subunit defective in an inherited form of distal renal tubular acidosis.
PMID:14675051
Comparative ontogeny, processing, and segmental distribution of the renal chloride channel, ClC-5.
PMID:15800125
Vacuolar H+-ATPase d2 subunit: molecular characterization, developmental regulation, and localization to specialized proton pumps in kidney and bone.
PMID:17360703
V1 and V0 domains of the human H+-ATPase are linked by an interaction between the G and a subunits.
PMID:17897319
Integral and associated lysosomal membrane proteins.
PMID:18632794
Human H+ATPase a4 subunit mutations causing renal tubular acidosis reveal a role for interaction with phosphofructokinase-1.
PMID:19056867
Large-scale proteomics and phosphoproteomics of urinary exosomes.
PMID:19199708
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
PMID:32001091
Structure and Roles of V-type ATPases.
PMID:32814053
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
PMID:33065002
Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.
Reactome:R-HSA-1222516
Intraphagosomal pH is lowered to 5 by V-ATPase
Reactome:R-HSA-5252133
ATP6AP1 binds V-ATPase
Reactome:R-HSA-74723
Endosome acidification
Reactome:R-HSA-917841
Acidification of Tf:TfR1 containing endosome
file:human/ATP6V0A4/ATP6V0A4-uniprot.txt
UniProtKB record for human ATP6V0A4/Q9HBG4
file:projects/PROTEOSTASIS/reports/pn_projection/pn_projected_candidate_additions.tsv
Proteostasis Network projected candidate additions for ATP6V0A4
file:projects/PROTEOSTASIS/mappings/autophagy_lysosome_pathway.yaml
Proteostasis Network autophagy-lysosome pathway GO mappings