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
OJY98844.1Cytochrome B6; Derived by automated computational analysis using gene prediction method: Protein Homology. (450 aa)    
Predicted Functional Partners:
OJZ01519.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
 
 0.564
OJZ00507.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
 
 0.564
OJY96683.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
     0.487
OJY97389.1
Restriction endonuclease subunit R; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.473
OJY97287.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.471
nuoK
NADH-quinone oxidoreductase subunit K; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family.
   
 
  0.455
nuoN
NADH-quinone oxidoreductase subunit N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family.
   
 
  0.446
nuoH
NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
   
 
  0.446
OJZ01676.1
NADH-quinone oxidoreductase subunit G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Belongs to the complex I 75 kDa subunit family.
   
 
  0.446
OJY98498.1
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.444
Your Current Organism:
Xanthomonadales bacterium 6970
NCBI taxonomy Id: 1895869
Other names: X. bacterium 69-70, Xanthomonadales bacterium 69-70
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