node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CRYAA | CRYAB | ENSP00000291554 | ENSP00000433560 | 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. | 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. | 0.996 |
CRYAA | CRYBA1 | ENSP00000291554 | ENSP00000225387 | 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. | Beta-crystallin A3, isoform A1, Delta4 form; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.987 |
CRYAA | CRYBA4 | ENSP00000291554 | ENSP00000346805 | 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. | Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.909 |
CRYAA | CRYBB1 | ENSP00000291554 | ENSP00000497249 | 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. | Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.860 |
CRYAA | CRYBB2 | ENSP00000291554 | ENSP00000498905 | 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. | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.984 |
CRYAA | CRYBB3 | ENSP00000291554 | ENSP00000215855 | 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. | Beta-crystallin B3, N-terminally processed; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.886 |
CRYAA | CRYGC | ENSP00000291554 | ENSP00000282141 | 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. | Gamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.919 |
CRYAA | CRYGD | ENSP00000291554 | ENSP00000264376 | 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. | Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.916 |
CRYAA | CRYGS | ENSP00000291554 | ENSP00000376287 | 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. | Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.960 |
CRYAA | GJA3 | ENSP00000291554 | ENSP00000241125 | 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. | 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. | 0.813 |
CRYAA | GJA8 | ENSP00000291554 | ENSP00000358238 | 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. | 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. | 0.828 |
CRYAB | CRYAA | ENSP00000433560 | ENSP00000291554 | 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. | 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. | 0.996 |
CRYAB | CRYBA1 | ENSP00000433560 | ENSP00000225387 | 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. | Beta-crystallin A3, isoform A1, Delta4 form; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.911 |
CRYAB | CRYBA4 | ENSP00000433560 | ENSP00000346805 | 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. | Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.811 |
CRYAB | CRYBB1 | ENSP00000433560 | ENSP00000497249 | 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. | Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.823 |
CRYAB | CRYBB2 | ENSP00000433560 | ENSP00000498905 | 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. | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.939 |
CRYAB | CRYBB3 | ENSP00000433560 | ENSP00000215855 | 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. | Beta-crystallin B3, N-terminally processed; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.820 |
CRYAB | CRYGC | ENSP00000433560 | ENSP00000282141 | 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. | Gamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.793 |
CRYAB | CRYGD | ENSP00000433560 | ENSP00000264376 | 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. | Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.924 |
CRYAB | CRYGS | ENSP00000433560 | ENSP00000376287 | 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. | Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.924 |