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VMA21 protein (Saccharomyces cerevisiae) - STRING interaction network
"VMA21" - Integral membrane protein that is required for vacuolar H+-ATPase in Saccharomyces cerevisiae
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VMA21Integral 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)    
Predicted Functional Partners:
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)
       
 
  0.928
VOA1
Endoplasmic reticulum protein that functions, together with other assembly factors, in assembly of the V0 sector of the vacuolar ATPase (V-ATPase); null mutation enhances the V-ATPase deficiency of a vma21 mutant impaired in ER retrieval; Functions with VMA21 in assembly of the integral membrane sector (also called V0 complex) of the V-ATPase in the endoplasmic reticulum (265 aa)
     
      0.878
VMA3
Proteolipid subunit c of the V0 domain of vacuolar H(+)-ATPase; dicyclohexylcarbodiimide binding subunit; required for vacuolar acidification and important for copper and iron metal ion homeostasis; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mv, inside positive and acidic, in the vacuolar membrane vesicles (160 aa)
     
 
  0.871
VMA11
Vacuolar ATPase V0 domain subunit c’, involved in proton transport activity; hydrophobic integral membrane protein (proteolipid) containing four transmembrane segments; N and C termini are in the vacuolar lumen; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (164 aa)
       
 
  0.843
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)
       
 
  0.842
PKR1
V-ATPase assembly factor, functions with other V-ATPase assembly factors in the ER to efficiently assemble the V-ATPase membrane sector (V0); Functions together with the other V-type ATPase assembly factors in the endoplasmic reticulum to efficiently assemble the V-type ATPase membrane sector V(0) (122 aa)
     
 
  0.828
VMA9
Vacuolar H+ ATPase subunit e of the V-ATPase V0 subcomplex; essential for vacuolar acidification; interacts with the V-ATPase assembly factor Vma21p in the ER; involved in V0 biogenesis; Subunit of the integral membrane V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (73 aa)
       
 
  0.818
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)
     
 
  0.804
VMA16
Subunit c’’ of the vacuolar ATPase, which functions in acidification of the vacuole; one of three proteolipid subunits of the V0 domain; Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (213 aa)
       
 
  0.797
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)
     
   
  0.749
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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