| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CRYAA | CRYAB | ENSBTAP00000004073 | ENSBTAP00000059200 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); 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; Belongs to the small heat shock protein (HSP20) family. | 0.995 |
| CRYAA | CRYBA1 | ENSBTAP00000004073 | ENSBTAP00000007037 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); 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; Belongs to the beta/gamma-crystallin family. | 0.972 |
| CRYAA | CRYBA2 | ENSBTAP00000004073 | ENSBTAP00000019735 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); Belongs to the small heat shock protein (HSP20) family. | Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.869 |
| CRYAA | CRYBB1 | ENSBTAP00000004073 | ENSBTAP00000069768 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); 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. | 0.866 |
| CRYAA | CRYBB2 | ENSBTAP00000004073 | ENSBTAP00000068239 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); Belongs to the small heat shock protein (HSP20) family. | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.962 |
| CRYAA | CRYGD | ENSBTAP00000004073 | ENSBTAP00000029019 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); Belongs to the small heat shock protein (HSP20) family. | Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.852 |
| CRYAA | CRYGS | ENSBTAP00000004073 | ENSBTAP00000004084 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); Belongs to the small heat shock protein (HSP20) family. | Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.891 |
| CRYAA | GJA8 | ENSBTAP00000004073 | ENSBTAP00000029102 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); Belongs to the small heat shock protein (HSP20) family. | Gap junction 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. | 0.857 |
| CRYAA | HSPB1 | ENSBTAP00000004073 | ENSBTAP00000041898 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); Belongs to the small heat shock protein (HSP20) family. | Heat 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. | 0.911 |
| CRYAA | HSPB6 | ENSBTAP00000004073 | ENSBTAP00000024749 | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); Belongs to the small heat shock protein (HSP20) family. | Heat shock protein beta-6; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. | 0.875 |
| CRYAB | CRYAA | ENSBTAP00000059200 | ENSBTAP00000004073 | 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; Belongs to the small heat shock protein (HSP20) family. | Alpha-crystallin A(1-168); Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity); Belongs to the small heat shock protein (HSP20) family. | 0.995 |
| CRYAB | CRYBA1 | ENSBTAP00000059200 | ENSBTAP00000007037 | 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; 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; Belongs to the beta/gamma-crystallin family. | 0.945 |
| CRYAB | CRYBA2 | ENSBTAP00000059200 | ENSBTAP00000019735 | 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; Belongs to the small heat shock protein (HSP20) family. | Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.655 |
| CRYAB | CRYBB1 | ENSBTAP00000059200 | ENSBTAP00000069768 | 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; 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. | 0.761 |
| CRYAB | CRYBB2 | ENSBTAP00000059200 | ENSBTAP00000068239 | 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; Belongs to the small heat shock protein (HSP20) family. | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.959 |
| CRYAB | CRYGD | ENSBTAP00000059200 | ENSBTAP00000029019 | 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; Belongs to the small heat shock protein (HSP20) family. | Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.827 |
| CRYAB | CRYGS | ENSBTAP00000059200 | ENSBTAP00000004084 | 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; Belongs to the small heat shock protein (HSP20) family. | Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.920 |
| CRYAB | GJA8 | ENSBTAP00000059200 | ENSBTAP00000029102 | 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; Belongs to the small heat shock protein (HSP20) family. | Gap junction 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. | 0.718 |
| CRYAB | HSPB1 | ENSBTAP00000059200 | ENSBTAP00000041898 | 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; Belongs to the small heat shock protein (HSP20) family. | Heat 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. | 0.987 |
| CRYAB | HSPB6 | ENSBTAP00000059200 | ENSBTAP00000024749 | 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; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein beta-6; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. | 0.918 |