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VPH2 protein (Saccharomyces cerevisiae) - STRING interaction network
"VPH2" - Integral membrane protein required for vacuolar H+-ATPase in Saccharomyces cerevisiae
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VPH2Integral membrane protein required for vacuolar H+-ATPase (V-ATPase) function, although not an actual component of the V-ATPase complex; functions in the assembly of the V-ATPase; localized to the endoplasmic reticulum (ER); Required for vacuolar ATPase assembly (215 aa)    
Predicted Functional Partners:
VMA22
Peripheral membrane protein that is required for vacuolar H+-ATPase (V-ATPase) function, although not an actual component of the V-ATPase complex; functions in the assembly of the V-ATPase; localized to the yeast endoplasmic reticulum (ER); Required for V-ATPase activity (181 aa)
     
  0.986
VMA6
Subunit d of the five-subunit V0 integral membrane domain of vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found in the endomembrane system; stabilizes VO subunits; required for V1 domain assembly on the vacuolar membrane; Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. The active enzyme consists of a catalytic V1 domain attached to an integral membrane V0 proton pore complex. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be [...] (345 aa)
       
 
  0.934
VPH1
Subunit 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; Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. Is present only in vacuolar V-ATPase complexes. Enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose deple [...] (840 aa)
       
 
  0.883
VMA8
Subunit D of the eight-subunit V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found throughout the endomembrane system; plays a role in the coupling of proton transport and ATP hydrolysis; Subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (256 aa)
     
   
  0.823
VMA5
Subunit C of the eight-subunit V1 peripheral membrane domain of vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found throughout the endomembrane system; required for the V1 domain to assemble onto the vacuolar membrane; Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic act [...] (392 aa)
     
   
  0.755
VMA21
Integral membrane protein that is required for vacuolar H+-ATPase (V-ATPase) function, although not an actual component of the V-ATPase complex; functions in the assembly of the V-ATPase; localized to the yeast endoplasmic reticulum (ER); Functions with VOA1 in assembly of the integral membrane sector (also called V0 sector) of the V-ATPase in the endoplasmic reticulum. Escorts the assembled V0 sector in COPII vesicles. Also required for normal packaging of the SNARE BOS1 and possibly the ER to Golgi transport receptor ERV29 (77 aa)
     
   
  0.738
DRS2
Aminophospholipid translocase (flippase) that maintains membrane lipid asymmetry in post-Golgi secretory vesicles; contributes to clathrin-coated vesicle formation and endocytosis; mutations in human homolog ATP8B1 result in liver disease; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Seems to be involved in ribosome assembly (1355 aa)
       
 
  0.712
SSM4
Ubiquitin-protein ligase involved in ER-associated protein degradation; located in the ER/nuclear envelope; ssm4 mutation suppresses mRNA instability caused by an rna14 mutation; E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of a broad range of substrates, inluding endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC). Component of the DOA10 ubiquitin ligase co [...] (1319 aa)
       
 
  0.652
STV1
Subunit a of the vacuolar-ATPase V0 domain, one of two isoforms (Stv1p and Vph1p); Stv1p is located in V-ATPase complexes of the Golgi and endosomes while Vph1p is located in V-ATPase complexes of the vacuole; Subunit of the integral membrane V0 complex of vacuolar ATPase essential for assembly and catalytic activity. Is present only in Golgi- and endosome-residing V-ATPase complexes. Enzymes containing this subunit have a 4-fold lower ratio of proton transport to ATP hydrolysis than complexes containing the vacuolar isoform and do not dissociate V1 and V0 in response to glucose deplet [...] (890 aa)
       
      0.647
NDC80
Component of the evolutionarily conserved kinetochore-associated Ndc80 complex (Ndc80p-Nuf2p-Spc24p-Spc25p); conserved coiled-coil protein involved in chromosome segregation, spindle checkpoint activity, kinetochore assembly and clustering; Acts as a component of the essential kinetochore- associated NDC80 complex, which is involved in chromosome segregation and spindle checkpoint activity (691 aa)
       
      0.647
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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