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.
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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.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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Score
CRYBA2Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens. (197 aa)    
Predicted Functional Partners:
LASP1
LIM and SH3 domain protein 1; Plays an important role in the regulation of dynamic actin- based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity).
    
   0.839
CRYAA
Alpha-crystallin A2(1-162); Contributes 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.
   
  
 0.793
CRYGA
Gamma-crystallin A; Crystallins are the dominant structural components of the vertebrate eye lens.
  
  
0.718
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. Involved in altering the calcium regulation of MIP water permeability.
   
  
 0.703
CRYBB2
Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
  
 
0.692
GJA3
Gap junction alpha-3 protein; Structural component of lens fiber gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells (By similarity). 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 ; Belongs to the connexin family. Alpha-type (group II) subfamily.
   
  
 0.651
BFSP2
Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
   
  
 0.651
CRYBB3
Beta-crystallin B3, N-terminally processed; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
  
 
0.637
LIM2
Lens fiber membrane intrinsic protein; Present in the thicker 16-17 nm junctions of mammalian lens fiber cells, where it may contribute to cell junctional organization. Acts as a receptor for calmodulin. May play an important role in both lens development and cataractogenesis; Belongs to the PMP-22/EMP/MP20 family.
   
  
 0.627
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 (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.
   
  
 0.626
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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