STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
VOA1ER protein that functions in assembly of the V0 sector of V-ATPase; functions with other assembly factors; null mutation enhances the vacuolar ATPase (V-ATPase) deficiency of a vma21 mutant impaired in endoplasmic reticulum (ER) retrieval; Belongs to the VOA1 family (265 aa)    
Predicted Functional Partners:
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; relative distribution to the vacuolar membrane decreases upon DNA replication stress; human homolog ATP6V0A4 implicated in renal tubular acidosis, can complement yeast null mutant
    
 
 0.975
VMA13
Subunit H of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; serves as an activator or a structural stabilizer of the V-ATPase; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits
    
 
 0.965
VMA21
Integral membrane protein required for V-ATPase function; not an actual component of the vacuolar H+-ATPase (V-ATPase) complex; diverged ortholog of human XMEA (X-linked Myopathy with Excessive Autophagy); functions in the assembly of the V-ATPase; localized to the yeast endoplasmic reticulum (ER)
   
 
 0.937
VMA6
Subunit d of the V0 integral membrane domain of V-ATPase; part of the electrogenic proton pump found in the endomembrane system; required for V1 domain assembly on the vacuolar membrane; the V0 integral membrane domain of vacuolar H+-ATPase (V-ATPase) has five subunits
   
 
 0.924
VMA5
Subunit C of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; required for the V1 domain to assemble onto the vacuolar membrane; the V1 peripheral membrane domain of vacuolar H+-ATPase (V-ATPase) has eight subunits
   
 
 0.916
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
   
 
 0.915
VMA16
Subunit c'' of the vacuolar ATPase; v-ATPase functions in acidification of the vacuole; one of three proteolipid subunits of the V0 domain
   
 
 0.914
VMA3
V-type proton ATPase subunit c; 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; Belongs to the V-ATPase proteolipid subunit family
   
 
 0.906
STV1
V-type proton ATPase subunit a, Golgi isoform; 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
    
 
 0.900
VMA22
Coiled-coil domain-containing protein 115; Protein that is required for vacuolar H+-ATPase (V-ATPase) function; peripheral membrane protein; not an actual component of the V-ATPase complex; functions in the assembly of the V-ATPase; localized to the yeast endoplasmic reticulum (ER)
      
 0.897
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
Server load: low (8%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.