node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Cryaa | Cryab | ENSMUSP00000019192 | ENSMUSP00000149803 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | 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. | 0.993 |
Cryaa | Cryba1 | ENSMUSP00000019192 | ENSMUSP00000077693 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Beta-crystallin A1; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.969 |
Cryaa | Cryba2 | ENSMUSP00000019192 | ENSMUSP00000006721 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.899 |
Cryaa | Crybb1 | ENSMUSP00000019192 | ENSMUSP00000031286 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Beta-crystallin B1B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.904 |
Cryaa | Crybb2 | ENSMUSP00000019192 | ENSMUSP00000107955 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.965 |
Cryaa | Crybb3 | ENSMUSP00000019192 | ENSMUSP00000112618 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Beta-crystallin B3, N-terminally processed; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.852 |
Cryaa | Crygb | ENSMUSP00000019192 | ENSMUSP00000027090 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Gamma-crystallin B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.891 |
Cryaa | Crygc | ENSMUSP00000019192 | ENSMUSP00000109698 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Gamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.900 |
Cryaa | Crygd | ENSMUSP00000019192 | ENSMUSP00000045327 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.959 |
Cryaa | Crygs | ENSMUSP00000019192 | ENSMUSP00000043588 | Alpha-crystallin A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.952 |
Cryab | Cryaa | ENSMUSP00000149803 | ENSMUSP00000019192 | 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 A chain; 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 (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | 0.993 |
Cryab | Cryba1 | ENSMUSP00000149803 | ENSMUSP00000077693 | 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 A1; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.820 |
Cryab | Cryba2 | ENSMUSP00000149803 | ENSMUSP00000006721 | 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 A2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.761 |
Cryab | Crybb1 | ENSMUSP00000149803 | ENSMUSP00000031286 | 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 B1B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.759 |
Cryab | Crybb2 | ENSMUSP00000149803 | ENSMUSP00000107955 | 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. | 0.849 |
Cryab | Crybb3 | ENSMUSP00000149803 | ENSMUSP00000112618 | 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. | 0.738 |
Cryab | Crygb | ENSMUSP00000149803 | ENSMUSP00000027090 | 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 B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.680 |
Cryab | Crygc | ENSMUSP00000149803 | ENSMUSP00000109698 | 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. | 0.655 |
Cryab | Crygd | ENSMUSP00000149803 | ENSMUSP00000045327 | 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; Belongs to the beta/gamma-crystallin family. | 0.782 |
Cryab | Crygs | ENSMUSP00000149803 | ENSMUSP00000043588 | 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. | 0.851 |