VPH1

  • Official Full Name

    Vph1p
  • Synonyms

    VPH1;Vph1p;vacuolar isoform;MSZ02;V-ATPase 95 kDa subunit;V-ATPase a 1 subunit;V-type proton ATPase subunit a;Vacuolar pH protein 1;Vacuolar proton pump a subunit;Vacuolar proton translocating ATPase subunit a 1;VPH1_YEAST;EC 3.6.3.14Subunit a of vacuolar-ATPase V0 domain, one of two isoforms (Vph1p and Stv1p);Vph1p is located in V-ATPase complexes of the vacuole while Stv1p is located in V-ATPase complexes of the Golgi and endosomes
Cat.# Product name Source (Host) Species Tag Protein Length Price

    Involved Pathway

    VPH1 involved in several pathways and played different roles in them. We selected most pathways VPH1 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with VPH1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    Protein Function

    VPH1 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by VPH1 itself. We selected most functions VPH1 had, and list some proteins which have the same functions with VPH1. You can find most of the proteins on our site.

    Function Related Protein

    Interacting Protein

    VPH1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with VPH1 here. Most of them are supplied by our site. Hope this information will be useful for your research of VPH1.

    Resources

    References

    • Kluge, C; Seidel, T; et al. Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex. BMC CELL BIOLOGY 5:-(2004).
    • Bayer, MJ; Reese, C; et al. Vacuole membrane fusion: V-o functions after trans-SNARE pairing and is coupled to the Ca2+-releasing channel. JOURNAL OF CELL BIOLOGY 162:211-222(2003).

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