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ATPvL2 protein (Chlamydomonas reinhardtii) - STRING interaction network
"ATPvL2" - Vacuolar proton-ATPase subunit c'' proteolipid in Chlamydomonas reinhardtii
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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ATPvL2Vacuolar proton-ATPase subunit c’’ proteolipid (205 aa)    
Predicted Functional Partners:
atpF
CF0 ATP synthase subunit I; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 subunits to proton translocation (175 aa)
   
  0.993
ATP1A
Mitochondrial F1F0 ATP synthase, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane (569 aa)
   
  0.992
ATP1B
Mitochondrial F1F0 ATP synthase, alpha subunit (736 aa)
   
  0.992
atpA
CF1 ATP synthase alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (508 aa)
   
  0.992
ATPvL1
Vacuolar H(+)-ATPase V0 sector, c/c’ subunits; 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 (176 aa)
     
0.989
ATP2
Beta subunit of mitochondrial ATP synthase; Produces ATP from ADP in the presence of a proton gradient across the membrane (574 aa)
   
  0.984
atpB
CF1 ATP synthase beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits (491 aa)
   
  0.984
ATPC
Chloroplast ATP synthase gamma chain (358 aa)
   
  0.983
ATP3
F1F0 ATP synthase gamma subunit (324 aa)
   
  0.983
ATP6
F1F0 ATP synthase subunit 6 (340 aa)
   
  0.983
Your Current Organism:
Chlamydomonas reinhardtii
NCBI taxonomy Id: 3055
Other names: C. reinhardtii, Chlamydomonadaceae, Chlamydomonadales, Chlamydomonas, Chlamydomonas reinhardtii, Chlamydomonas reinhardtii P.A.Dangeard, Chlamydomonas smithii, Chlamydomonas smithii R.W.Howshaw & H.Ettl, Chlorophyceae, Volvocales, Volvocida
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