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
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[Homology]
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VMA5Subunit 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 (392 aa)    
Predicted Functional Partners:
VMA2
V-type proton ATPase subunit B; Subunit B of V1 peripheral membrane domain of vacuolar H+-ATPase; electrogenic proton pump found throughout the endomembrane system; contains nucleotide binding sites; also detected in the cytoplasm; protein abundance increases in response to DNA replication stress; human homolog ATP6V1B1, implicated in autosomal-recessive distal renal tubular acidosis (RTA) with sensorineural deafness, complements yeast null mutant; Belongs to the ATPase alpha/beta chains family
   
 0.999
VMA1
Subunit A of the V1 peripheral membrane domain of V-ATPase; protein precursor undergoes self-catalyzed splicing to yield the extein Tfp1p and the intein Vde (PI-SceI), which is a site-specific endonuclease; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner; Belongs to the ATPase alpha/beta chains family
   
 0.999
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
   
 0.999
VMA8
Subunit D of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; plays a role in the coupling of proton transport and ATP hydrolysis; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits
   
 0.999
VMA7
Subunit F 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
   
 0.999
VMA16
Subunit c'' of the vacuolar ATPase; v-ATPase functions in acidification of the vacuole; one of three proteolipid subunits of the V0 domain
   
 0.999
VMA10
Subunit G of the V1 peripheral membrane domain of V-ATPase; part of the electrogenic proton pump found throughout the endomembrane system; involved in vacuolar acidification; the V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase) has eight subunits
   
 0.999
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
   
 0.999
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
   
 0.999
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
   
 0.999
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 (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.