node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
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; Small heat shock proteins | Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens | 0.873 |
CRYAB | CRYBA2 | ENSP00000433560 | ENSP00000295728 | 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 | Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.662 |
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; Small heat shock proteins | Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | 0.799 |
CRYAB | CRYBB2 | ENSP00000433560 | ENSP00000381273 | 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 | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | 0.903 |
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; Small heat shock proteins | Beta-crystallin B3; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | 0.808 |
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; Small heat shock proteins | Gamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | 0.833 |
CRYAB | HSPB1 | ENSP00000433560 | ENSP00000248553 | 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 | 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 | 0.513 |
CRYAB | HSPB4 | 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; Small heat shock proteins | 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 | 0.898 |
CRYAB | MIP | ENSP00000433560 | ENSP00000257979 | 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 | 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 | 0.675 |
CRYBA1 | CRYAB | ENSP00000225387 | ENSP00000433560 | Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens | 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 | 0.873 |
CRYBA1 | CRYBB2 | ENSP00000225387 | ENSP00000381273 | Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | 0.413 |
CRYBA1 | CRYBB3 | ENSP00000225387 | ENSP00000215855 | Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens | Beta-crystallin B3; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | 0.424 |
CRYBA1 | HSPB4 | ENSP00000225387 | ENSP00000291554 | Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens | 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 | 0.938 |
CRYBA1 | MIP | ENSP00000225387 | ENSP00000257979 | Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens | 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 | 0.660 |
CRYBA2 | CRYAB | ENSP00000295728 | ENSP00000433560 | Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens | 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 | 0.662 |
CRYBA2 | CRYBB2 | ENSP00000295728 | ENSP00000381273 | Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | 0.405 |
CRYBA2 | CRYBB3 | ENSP00000295728 | ENSP00000215855 | Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens | Beta-crystallin B3; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | 0.400 |
CRYBA2 | HSPB4 | ENSP00000295728 | ENSP00000291554 | Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens | 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 | 0.788 |
CRYBA4 | CRYAB | ENSP00000346805 | ENSP00000433560 | Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin 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; Small heat shock proteins | 0.799 |
CRYBA4 | CRYBB2 | ENSP00000346805 | ENSP00000381273 | Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family | 0.408 |