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.
|Gene References into Functions
- We conclude that the effects of variation in the vacuolar ATPase may point to a new molecular mechanism that influences the long-term development of depression. This mechanism may involve dysfunction specifically in hippocampal circuitry and cognitive impairment that characterizes recurrent and chronic depression. PMID: 27824360
- ATP6V1B2 is somatically mutated in 22% of follicular lymphoma tumors. Mutation hotspots found at Y371 and R400. PMID: 25713363
- A missense mutation in ATP6V1B2 associated with Zimmermann-Laband syndrome. PMID: 25915598
- The ATP6V1B2 p.Arg506X is a haploinsufficient mutation and resulted in abnormal acidification in lysosomes. PMID: 24913193
- This protein has been found differentially expressed in the anterior cingulate cortex from patients with schizophrenia PMID: 20381070
|Involvement in disease
||Zimmermann-Laband syndrome 2 (ZLS2); Deafness, congenital, with onychodystrophy, autosomal dominant (DDOD)
||Apical cell membrane. Melanosome. Cytoplasm.
||ATPase alpha/beta chains family
||Kidney; localizes to early distal nephron, encompassing thick ascending limbs and distal convoluted tubules (at protein level).