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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_4473Putative membrane protein precursor. (522 aa)    
Predicted Functional Partners:
CAP_4474
Hypothetical protein.
 
     0.880
CAP_4475
Hypothetical protein.
       0.547
srkA
YihE protein, required for LPS synthesis; A protein kinase that phosphorylates Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Probably involved in the extracytoplasmic stress response.
       0.530
CAP_7575
Hypothetical protein.
  
     0.498
CAP_1568
Hypothetical protein.
  
     0.475
CAP_1458
Hypothetical protein.
  
     0.472
CAP_2154
FadL family outer membrane protein.
  
     0.468
CAP_7987
Hypothetical protein.
  
     0.467
CAP_1143
Capsule biosynthesis protein capA.
  
     0.455
CAP_4359
Hypothetical protein.
  
     0.453
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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