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
CRYABAlpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions; Belongs to the small heat shock protein (HSP20) family. (223 aa)    
Predicted Functional Partners:
CRYAA
Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); Belongs to the small heat shock protein (HSP20) family.
  
 
0.985
CRYBB2
Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens.
   
 
 0.856
CRYBA1
Beta-crystallin A3, isoform A1, Delta4 form; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
   
 
 0.853
HSPB1
Heat shock protein beta-1; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.
   
 
0.810
CRYGS
Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens.
   
 
 0.800
CRYGD
Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
   
 
 0.790
CRYBB1
Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
      
 0.776
CRYBB3
Beta-crystallin B3, N-terminally processed; Crystallins are the dominant structural components of the vertebrate eye lens.
   
  
 0.765
HSPB2
Heat shock protein family B (small) member 2; Belongs to the small heat shock protein (HSP20) family.
  
 
0.763
CRYGC
Gamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
   
 
 0.748
Your Current Organism:
Bos taurus
NCBI taxonomy Id: 9913
Other names: B. taurus, Bos bovis, Bos primigenius taurus, Bovidae sp. Adi Nefas, bovine, cattle, cow, dairy cow, domestic cattle, domestic cow
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.