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
CAP_6393Oxidoreductase, short chain dehydrogenase/reductase family; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (262 aa)    
Predicted Functional Partners:
CAP_5153
Long-chain-fatty-acid--CoA ligase.
  
 0.968
CAP_1339
Malonyl CoA-acyl carrier protein transacylase.
   
 0.942
CAP_3199
Malonyl CoA-acyl carrier protein transacylase.
   
 0.936
CAP_6601
Glutamate synthase [NADPH] large chain.
    
  0.911
CAP_3203
Malonyl CoA-acyl carrier protein transacylase.
   
 0.825
CAP_0469
Malonyl CoA-acyl carrier protein transacylase.
   
 0.822
CAP_3198
Malonyl CoA-acyl carrier protein transacylase.
   
 0.809
CAP_2264
Enoyl-[acyl-carrier-protein] reductase.
 
 
 0.779
CAP_3725
3-oxoacyl-[acyl-carrier protein] reductase.
  
 
  0.779
CAP_2266
Hypothetical protein.
  
 0.754
Your Current Organism:
Chondromyces apiculatus
NCBI taxonomy Id: 1192034
Other names: C. apiculatus DSM 436, Chondromyces apiculatus Cm a2, Chondromyces apiculatus DSM 436, Chondromyces apiculatus str. DSM 436, Chondromyces apiculatus strain DSM 436
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