node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CRYAA | CRYAB | ENSP00000291554 | ENSP00000227251 | crystallin, alpha A; 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 | crystallin, alpha B; 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 | 0.701 |
CRYAA | CRYBB2 | ENSP00000291554 | ENSP00000381273 | crystallin, alpha A; 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 | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.980 |
CRYAA | CRYGC | ENSP00000291554 | ENSP00000282141 | crystallin, alpha A; 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 | crystallin, gamma C; Crystallins are the dominant structural components of the vertebrate eye lens | 0.978 |
CRYAA | CRYGD | ENSP00000291554 | ENSP00000264376 | crystallin, alpha A; 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 | crystallin, gamma D; Crystallins are the dominant structural components of the vertebrate eye lens | 0.926 |
CRYAA | HSPB1 | ENSP00000291554 | ENSP00000248553 | crystallin, alpha A; 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 | heat shock 27kDa protein 1 | 0.821 |
CRYAA | HSPB2 | ENSP00000291554 | ENSP00000457706 | crystallin, alpha A; 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 | HSPB2-C11orf52 readthrough (non-protein coding); May regulate the kinase DMPK | 0.606 |
CRYAA | MIP | ENSP00000291554 | ENSP00000257979 | crystallin, alpha A; 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 | major intrinsic protein of lens fiber; Water channel. 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) | 0.943 |
CRYAB | CRYAA | ENSP00000227251 | ENSP00000291554 | crystallin, alpha B; 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 | crystallin, alpha A; 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 | 0.701 |
CRYAB | CRYBB2 | ENSP00000227251 | ENSP00000381273 | crystallin, alpha B; 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 | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.888 |
CRYAB | CRYGC | ENSP00000227251 | ENSP00000282141 | crystallin, alpha B; 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 | crystallin, gamma C; Crystallins are the dominant structural components of the vertebrate eye lens | 0.842 |
CRYAB | CRYGD | ENSP00000227251 | ENSP00000264376 | crystallin, alpha B; 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 | crystallin, gamma D; Crystallins are the dominant structural components of the vertebrate eye lens | 0.472 |
CRYAB | HSPB1 | ENSP00000227251 | ENSP00000248553 | crystallin, alpha B; 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 | heat shock 27kDa protein 1 | 0.672 |
CRYAB | MIP | ENSP00000227251 | ENSP00000257979 | crystallin, alpha B; 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 | major intrinsic protein of lens fiber; Water channel. 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) | 0.414 |
CRYBB2 | CRYAA | ENSP00000381273 | ENSP00000291554 | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, alpha A; 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 | 0.980 |
CRYBB2 | CRYAB | ENSP00000381273 | ENSP00000227251 | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, alpha B; 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 | 0.888 |
CRYBB2 | CRYGC | ENSP00000381273 | ENSP00000282141 | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, gamma C; Crystallins are the dominant structural components of the vertebrate eye lens | 0.827 |
CRYBB2 | HSPB1 | ENSP00000381273 | ENSP00000248553 | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | heat shock 27kDa protein 1 | 0.735 |
CRYBB2 | HSPB2 | ENSP00000381273 | ENSP00000457706 | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | HSPB2-C11orf52 readthrough (non-protein coding); May regulate the kinase DMPK | 0.595 |
CRYBB2 | MIP | ENSP00000381273 | ENSP00000257979 | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | major intrinsic protein of lens fiber; Water channel. 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) | 0.772 |
CRYGC | CRYAA | ENSP00000282141 | ENSP00000291554 | crystallin, gamma C; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, alpha A; 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 | 0.978 |