The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

VPH2  -  Vph2p

Saccharomyces cerevisiae S288c

Synonyms: CLS10, Protein VMA12, VMA12, Vacuolar ATPase assembly integral membrane protein VPH2, YKL119C, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on VPH2

  • Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex [1].
  • The interaction of the Vma12p/Vma22p complex with Vph1p was transient (half-life of approximately 5 min), reflecting trafficking of this V-ATPase subunit through the ER en route to the vacuolar membrane [1].
  • Biochemical analysis has revealed that Vma12p behaves as an integral membrane protein with both the N and C termini oriented toward the cytosol, and this protein immunolocalizes to the endoplasmic reticulum (ER) [2].
  • These results indicate that Vma22p, along with Vma21p and Vma12p, form a set of ER proteins required for V-ATPase assembly [3].
  • The association of Vma22p with ER membranes was perturbed by mutations in VMA12, a gene that encodes an ER membrane protein (Vma12p) that is also required for V-ATPase assembly [3].

Biological context of VPH2


Associations of VPH2 with chemical compounds

  • However, the Vma12 protein was not detected in the vacuolar membrane ATPase complex that had been solubilized with a zwitterionic detergent, ZW3-14, and purified by glycerol gradient centrifugation (Kane, P. M., Yamashiro, C. T., and Stevens, T. H. (1989) J. Biol. Chem. 264, 19236-19244) [5].

Other interactions of VPH2

  • Subcellular fractionation and chemical cross-linking studies have revealed that Vma12p and Vma22p form a stable membrane associated complex [1].

Analytical, diagnostic and therapeutic context of VPH2

  • Synthesis and targeting of the subunits of the H(+)-ATPase in the delta vma12 mutant cells were examined by Western blotting analyses of whole cell and vacuolar membrane protein extracts [5].


WikiGenes - Universities