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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
hmuOHeme oxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (224 aa)    
Predicted Functional Partners:
hemH
Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.
 
  
 0.929
ANW21955.1
Nitrilase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
  0.912
ANW20468.1
Copper oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.909
ctaB
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.
     
 0.902
BB341_04660
Protease; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.901
ANW20593.1
Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.
     
  0.900
map
Type I methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
     
 0.759
ANW20458.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.679
gunC
Endoglucanase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.579
ANW18825.1
Dihydrofolate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
      
 0.550
Your Current Organism:
Streptomyces clavuligerus
NCBI taxonomy Id: 1901
Other names: ATCC 27064, BCRC 11518, CBS 226.75, CCRC 11518, CCRC:11518, CECT 3125, DSM 40751, DSM 738, IFO 13307, IMET 43657, JCM 4710, KCTC 9095, NBRC 13307, NCIMB 12785, NCIMB 14335, NRRL 3585, S. clavuligerus, Streptomyces clavuligerus ATCC 27064, Streptomyces clavuligerus NRRL 3585, VKM Ac-602
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