node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
C21orf62 | CRYBA2 | ENSP00000418511 | ENSP00000295728 | chromosome 21 open reading frame 62 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.506 |
CALCOCO1 | CRYBA2 | ENSP00000449960 | ENSP00000295728 | calcium binding and coiled-coil domain 1; Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1- mediated transcriptional activation via its inte [...] | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.506 |
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 | CRYBA2 | ENSP00000291554 | ENSP00000295728 | 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 A2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.685 |
CRYAA | CRYBB1 | ENSP00000291554 | ENSP00000215939 | 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 B1; Crystallins are the dominant structural components of the vertebrate eye lens | 0.774 |
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 | CRYBB3 | ENSP00000291554 | ENSP00000215855 | 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 B3; Crystallins are the dominant structural components of the vertebrate eye lens | 0.896 |
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 | CRYBA2 | ENSP00000227251 | ENSP00000295728 | 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 A2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.509 |
CRYAB | CRYBB1 | ENSP00000227251 | ENSP00000215939 | 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 B1; Crystallins are the dominant structural components of the vertebrate eye lens | 0.700 |
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 | CRYBB3 | ENSP00000227251 | ENSP00000215855 | 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 B3; Crystallins are the dominant structural components of the vertebrate eye lens | 0.750 |
CRYBA2 | C21orf62 | ENSP00000295728 | ENSP00000418511 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | chromosome 21 open reading frame 62 | 0.506 |
CRYBA2 | CALCOCO1 | ENSP00000295728 | ENSP00000449960 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | calcium binding and coiled-coil domain 1; Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1- mediated transcriptional activation via its inte [...] | 0.506 |
CRYBA2 | CRYAA | ENSP00000295728 | ENSP00000291554 | crystallin, beta A2; 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 | 0.685 |
CRYBA2 | CRYAB | ENSP00000295728 | ENSP00000227251 | crystallin, beta A2; 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 | 0.509 |
CRYBA2 | CRYBB1 | ENSP00000295728 | ENSP00000215939 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta B1; Crystallins are the dominant structural components of the vertebrate eye lens | 0.602 |
CRYBA2 | CRYBB2 | ENSP00000295728 | ENSP00000381273 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.603 |
CRYBA2 | CRYBB3 | ENSP00000295728 | ENSP00000215855 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta B3; Crystallins are the dominant structural components of the vertebrate eye lens | 0.603 |
CRYBA2 | CRYM | ENSP00000295728 | ENSP00000219599 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, mu; Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors | 0.481 |