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:
a 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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
atp6v0caV-type proton ATPase proteolipid subunit; 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. (154 aa)    
Predicted Functional Partners:
atp6v1f
V-type proton ATPase subunit F; Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
  
 0.998
atp6v0d1
V-type proton ATPase subunit d 1; Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar 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. May play a role in coupling of proton transport and ATP hydrolysis. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) p [...]
  
 0.997
atp6v1h
V-type proton ATPase subunit H; Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar 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.
   
 0.996
atp6v0b
ATPase H+-transporting V0 subunit b; Belongs to the V-ATPase proteolipid subunit family.
   
0.996
atp6v1ba
Vacuolar proton pump subunit B; Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase; Belongs to the ATPase alpha/beta chains family.
  
 0.992
atp6v1d
ATPase, H+ transporting, V1 subunit D.
  
 0.991
ATP6
ATP synthase subunit a; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subuni [...]
  
 0.990
atp6v1e1b
ATPase H+-transporting V1 subunit E1b.
  
 0.989
atp6v1b2
Vacuolar proton pump subunit B; Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase; Belongs to the ATPase alpha/beta chains family.
  
 0.985
atp5fa1
ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane.
  
 0.984
Your Current Organism:
Danio rerio
NCBI taxonomy Id: 7955
Other names: Brachydanio rerio, Brachydanio rerio frankei, Cyprinus rerio, D. rerio, Danio frankei, Danio rerio frankei, leopard danio, zebra danio, zebra fish, zebrafish
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