STRINGSTRING
Cryba4 Cryba4 Cryaa Cryaa Bfsp1 Bfsp1 Cryab Cryab Grifin Grifin Cryga-2 Cryga-2 Bfsp2 Bfsp2 Hsf4 Hsf4 Gja3 Gja3 Gja8 Gja8 Srrd Srrd
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
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[Homology]
Score
Cryba4Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (196 aa)    
Predicted Functional Partners:
Cryaa
Alpha-crystallin A(1-151); 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. Belongs to the small heat shock protein (HSP20) family.
   
 
 0.849
Bfsp1
Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity).
      
 0.827
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.
   
 
 0.800
Grifin
Grifin.
   
  
 0.763
Cryga-2
Gamma-crystallin A.
   
  
 0.723
Bfsp2
Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA.
   
  
 0.677
Hsf4
Heat shock transcription factor 4.
      
 0.655
Gja3
Gap junction alpha-3 protein; Structural component of lens fiber gap junctions (Probable). Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore (Probable); Belongs to the connexin family. Alpha-type (group II) subfamily.
   
  
 0.637
Gja8
Gap junction alpha-8 protein; Structural component of eye lens gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.
      
 0.623
Srrd
SRR1 domain containing.
      
 0.610
Your Current Organism:
Rattus norvegicus
NCBI taxonomy Id: 10116
Other names: Buffalo rat, Norway rat, R. norvegicus, Rattus PC12 clone IS, Rattus sp. strain Wistar, Sprague-Dawley rat, Wistar rats, brown rat, laboratory rat, rat, rats, zitter rats
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