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
urosUroporphyrinogen III synthase. (264 aa)    
Predicted Functional Partners:
hmbs
Hydroxymethylbilane synthase a.
  
 0.995
alad
Uncharacterized protein; Belongs to the ALAD family.
  
 0.993
urod
Uroporphyrinogen decarboxylase; Belongs to the uroporphyrinogen decarboxylase family.
  
 
 0.952
ENDOV
Endonuclease V.
  
 
 0.936
ppox
Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
  
  
 0.728
ttf2
Uncharacterized protein.
  
  
 0.690
pcna
Proliferating cell nuclear antigen; This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand; Belongs to the PCNA family.
     
 0.679
mmp21
Matrix metallopeptidase 21; Belongs to the peptidase M10A family.
 
      0.658
eprs1
Glutamyl-prolyl-tRNA synthetase.
  
  
 0.657
lias
Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
      
 0.636
Your Current Organism:
Poecilia reticulata
NCBI taxonomy Id: 8081
Other names: Acanthophacelus reticulata, P. reticulata, Poecilia (Acanthophacelus) reticulata, Poecilia latipinna reticulata, guppy
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.