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
AIS16612.1Cytochrome B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (404 aa)    
Predicted Functional Partners:
AIS16611.1
Ubiquinol-cytochrome C reductase; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 
 0.999
AIS16613.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
nuoC
NADH:ubiquinone oxidoreductase; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
   
 
 0.997
AIS18002.1
NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.992
AIS16490.1
Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.987
AIS16489.1
Ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.986
nuoH
NADH:ubiquinone oxidoreductase; 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.
  
 
 0.984
AIS18812.1
Alcohol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.977
AIS19765.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.939
nuoN
NADH:ubiquinone 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.
   
 
 0.934
Your Current Organism:
Pseudomonas rhizosphaerae
NCBI taxonomy Id: 216142
Other names: CECT 5726, DSM 16299, LMG 21640, LMG:21640, P. rhizosphaerae, Pseudomonas rhizosphaerae Peix et al. 2003, strain IH5
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