ATP6V1B2 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0046034Biological processATP metabolic process
GO_0097401Biological processsynaptic vesicle lumen acidification
GO_0007035Biological processvacuolar acidification
GO_0016241Biological processregulation of macroautophagy
GO_1902600Biological processproton transmembrane transport
GO_0001726Cellular componentruffle
GO_0005902Cellular componentmicrovillus
GO_0016324Cellular componentapical plasma membrane
GO_0005886Cellular componentplasma membrane
GO_0070062Cellular componentextracellular exosome
GO_0000221Cellular componentvacuolar proton-transporting V-type ATPase, V1 domain
GO_0005829Cellular componentcytosol
GO_0098850Cellular componentextrinsic component of synaptic vesicle membrane
GO_0043231Cellular componentintracellular membrane-bounded organelle
GO_0005765Cellular componentlysosomal membrane
GO_0042470Cellular componentmelanosome
GO_0030665Cellular componentclathrin-coated vesicle membrane
GO_0046961Molecular functionproton-transporting ATPase activity, rotational mechanism
GO_0015078Molecular functionproton transmembrane transporter activity
GO_0005524Molecular functionATP binding
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameATP6V1B2
Protein nameV-type proton ATPase subunit B, brain isoform (V-ATPase subunit B 2) (Endomembrane proton pump 58 kDa subunit) (HO57) (Vacuolar proton pump subunit B 2)
ATPase H+ transporting V1 subunit B2
SynonymsATP6B2
VPP3
DescriptionFUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment . In renal intercalated cells, can partially compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine under base-line conditions but not in conditions of acid load (By similarity). .

AccessionsENST00000276390.7
H0YC04
ENST00000523478.5
H0YC45
H0YAT8
E5RGH6
P21281
ENST00000520830.1
ENST00000521442.1
ENST00000519667.1