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. (261 aa)    
Predicted Functional Partners:
hmbs
Hydroxymethylbilane synthase a.
  
 0.999
urod
Uroporphyrinogen decarboxylase; Belongs to the uroporphyrinogen decarboxylase family.
  
 
 0.995
ENDOV
Endonuclease V.
  
 
 0.944
fech
Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX.
  
  
 0.772
Ppox
Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
  
  
 0.764
cpox
Coproporphyrinogen oxidase.
     
 0.746
ttf2
Transcription termination factor, RNA polymerase II.
  
  
 0.729
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.
     
 0.720
eprs1
Glutamyl-prolyl-tRNA synthetase.
  
  
 0.701
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.
      
 0.682
Your Current Organism:
Oreochromis niloticus
NCBI taxonomy Id: 8128
Other names: Nile tilapia, O. niloticus, Oreochromis nilotica, Tilapia nilotica
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