Gene Ontology annotation through association of InterPro records with GO terms.
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Combined Automated Annotation using Multiple IEA Methods.
Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts.
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This paper supports a macroautophagy/lysosome context, but not a specific ATP6V0B regulatory function.
"macroautophagy is responsible for the uptake of lipofuscin into the lysosomes"
The identification of novel proteins that interact with the GLP-1 receptor and restrain its activity.
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The GLP-1R interaction study used a membrane yeast two-hybrid screen and does not define ATP6V0B core molecular function.
"A screen of a human fetal brain cDNA prey library with an unliganded human GLP-1R as bait in yeast revealed 38 novel interactor protein candidates."
Structure and Roles of V-type ATPases.
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V-ATPases are membrane-embedded ATP-driven proton pumps and are the primary source of organellar acidification in eukaryotes.
"V-ATPases are membrane-embedded protein complexes that function as ATP hydrolysis-driven proton pumps."
A reference map of the human binary protein interactome.
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The HuRI study is a large-scale binary interactome resource, not ATP6V0B-specific functional evidence.
"The dataset, versioned HI-III-20 (Human Interactome obtained from screening Space III, published in 2020), contains 52,569 verified PPIs involving 8,275 proteins"
Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.
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Human V-ATPase is an ATP-driven proton pump with a cytoplasmic V1 ATP-hydrolysis sector and a membrane-embedded Vo proton-transfer sector.
"Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-driven proton pumps comprised of a cytoplasmic V1 complex for ATP hydrolysis and a membrane-embedded Vo complex for proton transfer."
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Organellar V-ATPases maintain endosome and lysosome pH homeostasis and support trafficking and protein degradation.
"Vesicular and organellar V-ATPases are essential in establishing and maintaining the pH homeostasis of endosomes and lysosomes and in supporting intracellular membrane trafficking and protein degradation"
Identification and characterization of the gene encoding a second proteolipid subunit of human vacuolar H(+)-ATPase (ATP6F).
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ATP6V0B/ATP6F is the human second V-ATPase proteolipid, a five-transmembrane c subunit with conserved Glu98 required for H+ transport.
"hATP6F is a hydrophobic protein with five putative transmembrane segments, having 61% amino acid identity and 83% similarity to the yeast protein, except in the N-terminus, and contains a conserved glutamic acid residue (Glu98) that is essential for H(+)-transporting activity."
Intraphagosomal pH is lowered to 5 by V-ATPase
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Reactome describes V-ATPase rotary pumping into the phagosome.
"When pumping, ATP hydrolysis drives a 120 degree rotation of the rotor which leads to movement of three protons into the phagosome"
Acidification of Tf:TfR1 containing endosome
RRAGC,D exchanges GTP for GDP
RRAGA,B exchanges GDP for GTP
v-ATPase:Ragulator:RRAGA,B:GTP:RRAGC,D:GDP:SLC38A9:Arginine dissociates yielding v-ATPase:Ragulator:RRAGA,B:GTP:RRAGC,D:GDP and SLC38A9:Arginine
v-ATPase:Ragulator:RagA,B:GDP:RagC,D:GDP binds SLC38A9:Arginine
v-ATPase:Ragulator:RRAGA,B:GTP:RRAGC,D:GDP binds mTORC1
MITF-M-dependent ATP6V0B gene expression
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Reactome records MITF-dependent expression of ATP6V0B and the lysosome/endosome acidification role of V-ATPase.
"MITF has been implicated in the regulation of expression of many components of the v-ATPase, including the transmembrane component ATP6V0B"
Falcon deep research report on ATP6V0B
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Falcon deep research supports ATP6V0B as the human V-ATPase V0 c'' proteolipid subunit and highlights the PN-relevant lysosomal acidification role.
"ATP6V0B-containing V-ATPases acidify lysosomes, endosomes, Golgi, and secretory/synaptic vesicles and can localize to plasma membranes in specialized cells."
Cyberian deep research on ATP6V0B function
Proteostasis PN projected annotations for ATP6V0B
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PN projection maps ATP6V0B in the V0 lysosomal V-ATPase proton pump component leaf to GO:0046610.
"ATP6V0B Autophagy-Lysosome Pathway|Pre-initiation autophagy signaling|mTORC1 pathway, upstream|Nutrient sensing|V0 lysosomal v-ATPase proton pump component"