• Version:
  • 11.0 [archived version]
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CRYBB1 CRYBB1 CRYBA1 CRYBA1 CRYA1 CRYA1 CRYBB2 CRYBB2 HSPB4 HSPB4 BFSP2 BFSP2 CRYGS CRYGS MIP MIP GJA3 GJA3 CRYBB3 CRYBB3 CRYGC CRYGC
"GJA3" - Gap junction alpha-3 protein in Homo sapiens
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:
some 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 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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Cooccurence
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[Homology]
Score
GJA3Gap junction alpha-3 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; Belongs to the connexin family. Alpha-type (group II) subfamily (435 aa)    
Predicted Functional Partners:
CRYBB2
Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family (205 aa)
           
  0.921
CRYBB1
Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family (252 aa)
           
  0.857
HSPB4
Crystallin, alpha A; 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; Small heat shock proteins (173 aa)
           
  0.850
CRYA1
Alpha-crystallin A chain; 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; Small heat shock proteins (173 aa)
           
  0.850
BFSP2
Phakinin; Involved in stabilization of lens fiber cell cytoskeleton; Belongs to the intermediate filament family (415 aa)
           
  0.835
MIP
Lens fiber major intrinsic protein; Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core (By similarity). Plays a role in cell-to-cell adhesion and facilitates gap junction coupling; Belongs to the MIP/aquaporin (TC 1.A.8) family (263 aa)
       
 
  0.829
CRYBA1
Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens (215 aa)
           
  0.818
CRYGC
Gamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family (174 aa)
           
  0.800
CRYBB3
Beta-crystallin B3; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family (211 aa)
           
  0.793
CRYGS
Beta-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family (178 aa)
           
  0.772
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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