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
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[Homology]
Score
A0A0G2FRW4Putative vacuolar atp synthase subunit. (75 aa)    
Predicted Functional Partners:
A0A0G2FVG7
V-type proton ATPase subunit a; Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
    
 0.911
A0A0G2HPT7
Putative 6-phosphogluconate dehydrogenase.
 
      0.899
A0A0G2I9V6
V-type proton ATPase subunit; 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 involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores; Belongs to the V-ATPase V0D/AC39 subunit family.
    
 0.878
A0A0G2FCT4
Putative v-atpase proteolipid subunit; Belongs to the V-ATPase proteolipid subunit family.
    
 0.873
A0A0G2FA50
Putative vacuolar atp synthase catalytic subunit a.
    
 0.860
A0A0G2I2X0
V-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.
    
 0.846
A0A0G2FGU1
V-type proton ATPase subunit G; Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
    
 0.794
A0A0G2HQ75
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.
    
 0.781
A0A0G2FDG3
Vacuolar proton pump subunit B; Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase; Belongs to the ATPase alpha/beta chains family.
   
 0.773
A0A0G2FPA5
V-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.
    
 0.770
Your Current Organism:
Diaporthe ampelina
NCBI taxonomy Id: 1214573
Other names: CBS 114016, D. ampelina, Diaporthe ampelina (Berk. & M.A. Curtis) R.R. Gomes, C. Glienke & Crous, Diaporthe neoviticola, Diaporthe sp. DU-2012e, Fusicoccum viticolum, Phoma ampelina, Phoma viticola, Phomopsis ampelina, Phomopsis sp. Pho06, Phomopsis sp. Pho07, Phomopsis sp. Pho10, Phomopsis sp. Pho16, Phomopsis sp. Pho18, Phomopsis sp. Pho24, Phomopsis sp. Pho25, Phomopsis sp. Pho26, Phomopsis sp. Pho28, Phomopsis sp. Pho32, Phomopsis sp. PhoCT1L, Phomopsis sp. taxon 2, Phomopsis viticola, STEU 2660
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