• Version:
  • 11.0 [archived version]
STRINGSTRING
CRYBA2 CRYBA2 CRYBB3 CRYBB3 CRYBA1 CRYBA1 MIP MIP CRYBA4 CRYBA4 CRYAB CRYAB HSPB4 HSPB4 CRYBB2 CRYBB2 CRYGC CRYGC HSPB1 HSPB1
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:
CRYBB3Beta-crystallin B3; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family (211 aa)
CRYBA1Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens (215 aa)
HSPB1Heat 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 (205 aa)
MIPLens 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)
CRYGCGamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family (174 aa)
HSPB4Crystallin, 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)
CRYBA2Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens (197 aa)
CRYBA4Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family (196 aa)
CRYBB2Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family (205 aa)
CRYABAlpha-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)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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