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EDO96901 protein (Chlamydomonas reinhardtii) - STRING interaction network
"EDO96901" - Predicted protein 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
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textmining
co-expression
protein homology
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EDO96901Predicted protein; RuBisCO catalyzes two reactions- the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (139 aa)    
Predicted Functional Partners:
rbcL
Ribulose bisphosphate carboxylase small subunit; RuBisCO catalyzes two reactions- the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (475 aa)
 
 
  0.999
PRK1
Phosphoribulokinase (375 aa)
   
 
  0.945
PGK1
Phosphoglycerate kinase (462 aa)
   
 
  0.943
GLYK
Glycerate kinase (351 aa)
         
    0.932
RBCS2B
Ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit 2; RuBisCO catalyzes two reactions- the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (188 aa)
   
 
 
0.913
PGP3
Phosphoglycolate phosphatase (347 aa)
     
 
    0.903
PGP1
Phosphoglycolate phosphatase 1 (330 aa)
     
 
    0.903
PGP2
Phosphoglycolate phosphatase (304 aa)
     
 
    0.903
RBCS1
Ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit 1, chloroplast precursor; RuBisCO catalyzes two reactions- the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (185 aa)
   
   
 
0.801
CPLD2
Predicted protein (290 aa)
 
   
  0.562
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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