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
sirHCytochrome c maturation system periplasmic thioredoxin SirH. (194 aa)    
Predicted Functional Partners:
selR
methionine-R-sulfoxide reductase SelR; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
   
 0.974
sirE
Cytochrome c maturation system haem lyase subunit SirE.
  
  
 0.949
sirF
Cytochrome c maturation system haem lyase subunit SirF; Possible subunit of a heme lyase.
  
  
 0.878
senC
Cytochrome c oxidase biogenesis protein SenC.
 
 
 0.793
ccmI
Apo-cytochrome c chaperone CcmI.
  
  
 0.771
ccmG
Cytochrome c maturation system membrane anchored thioredoxin CcmG.
 
   
 0.761
ccmH
Cytochrome c synthetase subunit CcmH; Possible subunit of a heme lyase.
  
  
 0.747
ccmF
Cytochrome c synthetase cytochrome b containing quinol-haem oxidoreductase subunit CcmF.
  
  
 0.692
SO_3117
Thioredoxin.
  
     0.661
coxB
Aa3-type cytochrome c oxidase subunit II CoxB; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 
 0.653
Your Current Organism:
Shewanella oneidensis
NCBI taxonomy Id: 211586
Other names: S. oneidensis MR-1, Shewanella oneidensis ATCC 700550, Shewanella oneidensis MR-1, Shewanella oneidensis str. MR-1, Shewanella oneidensis strain MR-1, Shewanella sp. MR-1
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