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ATPC2 protein (Arabidopsis thaliana) - STRING interaction network
"ATPC2" - ATP synthase gamma chain 2 in Arabidopsis thaliana
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Predicted Interactions
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textmining
co-expression
protein homology
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ATPC2ATP synthase gamma chain 2; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex (386 aa)    
Predicted Functional Partners:
ATPA
ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (507 aa)
 
  0.999
ATP1
ATPase subunit 1; 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 subunits to [...] (507 aa)
 
  0.999
PB
ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits (498 aa)
 
  0.999
AT5G08690
ATP synthase subunit beta-2; 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 [...] (556 aa)
 
  0.999
AT5G08680
ATP synthase subunit beta-3; 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 [...] (559 aa)
 
  0.999
ATP5
ATP synthase subunit O; 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 [...] (238 aa)
   
  0.999
AT2G07698
ATPase, F1 complex, alpha subunit protein (777 aa)
 
  0.999
AT5G08670
F-type H+-transporting ATPase subunit beta (556 aa)
 
  0.999
ATPE
ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane (132 aa)
   
  0.999
AT5G47030
ATP synthase subunit delta’; 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 turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk s [...] (203 aa)
   
  0.999
Your Current Organism:
Arabidopsis thaliana
NCBI taxonomy Id: 3702
Other names: A. thaliana, Arabidopsis thaliana, Arabidopsis thaliana (L.) Heynh., mouse-ear cress, thale cress, thale-cress
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