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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
AOP35747.1Formate hydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (573 aa)    
Predicted Functional Partners:
AOP35742.1
Hydrogenase-4 subunit G; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
AOP35743.1
Metal (Ni/Fe) hydrogenase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
AOP35746.1
Formate hydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.993
AOP36090.1
NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.992
AOP35744.1
Formate hydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.936
AOP35745.1
Formate hydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.897
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.
 
  
 0.841
nuoB
NADH dehydrogenase; 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.
 
 
 0.829
nuoI
NADH-quinone oxidoreductase subunit I; 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.
 
 0.828
nuoD
NADH dehydrogenase; 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 49 kDa subunit family.
 
 
  0.826
Your Current Organism:
Leptospira alstonii
NCBI taxonomy Id: 28452
Other names: ATCC BAA-2439, L. alstonii, Leptospira alstoni, Leptospira alstonii Smythe et al. 2013, Leptospira genomosp. 1, strain 79601
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