• Version:
  • 11.0 [archived version]
STRINGSTRING
CRYA1 CRYA1 MIP MIP GJA8 GJA8 TMEM114 TMEM114 BFSP1 BFSP1 CRYAB CRYAB GJA3 GJA3 LIM2 LIM2 CRYBA4 CRYBA4 BFSP2 BFSP2 HSPB4 HSPB4
"CRYBA4" - Beta-crystallin A4 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.
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:
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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[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:
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)
     
   
  0.863
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)
     
   
  0.860
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; Small heat shock proteins (175 aa)
     
   
  0.799
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)
     
   
  0.765
BFSP2
Phakinin; Involved in stabilization of lens fiber cell cytoskeleton; Belongs to the intermediate filament family (415 aa)
     
   
  0.741
LIM2
Lens intrinsic membrane protein 2 (215 aa)
     
   
  0.735
GJA3
Gap 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)
           
  0.733
BFSP1
Filensin; Beaded filament structural protein 1; Belongs to the intermediate filament family (665 aa)
     
   
  0.716
GJA8
Gap junction alpha-8 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 (433 aa)
     
   
  0.714
TMEM114
Transmembrane protein 114 (223 aa)
           
  0.703
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
Server load: low (0%) [HD]