Aliases:This biomarker is also known as:
- Vacuolar proton pump subunit M16,
- Vacuolar proton pump subunit G 1,
- ATPase, H+ transporting, lysosomal (vacuolar proton pump), member J,
- vacuolar proton pump subunit M16,
- V-type proton ATPase subunit G 1,
- V-ATPase subunit G 1,
- ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G1,
- ATPase, H+ transporting, lysosomal 13kDa, V1 subunit G isoform 1,
- V-ATPase 13 kDa subunit 1,
- vacuolar proton pump subunit G 1,
- vacuolar H(+)-ATPase subunit G 1,
- vacuolar ATP synthase subunit M16,
ATP6V1G1 is a subunit of vacuolar ATPase (V-ATPase), a multisubunit enzyme. V-ATPase is an enzyme transporter that functions to acidify intracellular compartments in eukaryotic cells. This acidification process is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is ubiquitously expressed and is present in endomembrane organelles such as vacuoles, lysosomes, endosomes, the Golgi apparatus, chromaffin granules and coated vesicles, as well as in the plasma membrane. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site.
There are no datasets associated with this biomarker.
The following organs have data associated with this biomarker…
|QA State:||Under Review|
No additional breast data available.
ATP6V1G1 was one of numerous potential early detection biomarkers specific to triple-negative breast cancer in multiple pathways identified.