close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
KB13_13[C] COG2010 Cytochrome c, mono- and diheme variants. (152 aa)    
Predicted Functional Partners:
KB13_598
Cytochrome oxidase assembly; [O] COG1612 Uncharacterized protein required for cytochrome oxidase assembly.
 
  
  0.932
cyoE
Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
    
  0.879
KB13_321
Cytochrome c, class I; [C] COG2863 Cytochrome c553.
 
  
 0.863
KB13_1166
[C] COG2857 Cytochrome c1.
  
  
 0.771
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).
 
  
 0.764
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.
 
 
 0.708
apaH
Bis(5-nucleosyl)-tetraphosphatase; [T] COG0639 Diadenosine tetraphosphatase and related serine/threonine protein phosphatases.
       0.697
coxC
[C] COG1845 Heme/copper-type cytochrome/quinol oxidase, subunit 3.
 
  
  0.680
ctaD
Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
    
  0.604
KB13_122
Molybdopterin dependent oxidoreductase; [C] COG0243 Anaerobic dehydrogenases, typically selenocysteine-containing; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
    
  0.576
Your Current Organism:
beta proteobacterium KB13
NCBI taxonomy Id: 314607
Other names: b. proteobacterium KB13
Server load: medium (48%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.