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
cycCytochrome c5. (121 aa)    
Predicted Functional Partners:
Cc4
Cytochrome c4.
 
   
 0.764
petC
Ubiquinol-cytochrome c oxydoreductase, cytochrome c1.
 
  
 0.689
petA
Ubiquinol--cytochrome c reductase, iron-sulfur subunit; 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.
 
  
 0.656
flgA
Flagellar basal body P-ring biosynthesis protein FlgA; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly; Belongs to the FlgA family.
       0.611
Lche_1005
Hypothetical protein.
       0.568
CtaA
Cytochrome c oxidase assembly protein.
 
     0.535
coxB
Cytochrome c oxidase subunit II; 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).
 
  
 0.492
Lche_0464
Fatty acid desaturase.
  
     0.436
Lche_1002
Hypothetical protein.
       0.433
Lche_1001
Flagellar biosynthesis/type III secretory pathway chaperone.
       0.417
Your Current Organism:
Legionella cherrii
NCBI taxonomy Id: 28084
Other names: ATCC 35252, CCUG 29666, CIP 103842, DSM 19213, L. cherrii, Legionella cherryi, NCTC 11976, strain ORW
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