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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
CRYAAAlpha-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. (173 aa)    
Predicted Functional Partners:
CRYAB
Alpha-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.
  
 
0.995
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.
   
 
 0.972
CRYBB2
Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens.
   
 
 0.962
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.
   
 0.911
CRYGS
Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens.
   
 
 0.891
HSPB6
Heat shock protein beta-6; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity.
   
 0.875
CRYBA2
Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens.
   
  
 0.869
CRYBB1
Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
   
 
 0.866
GJA8
Gap junction protein; One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
      
 0.857
CRYGD
Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
   
 
 0.852
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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