node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Bfsp2 | Cryab | ENSMUSP00000116249 | ENSMUSP00000149803 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | 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. | 0.674 |
Bfsp2 | Cryba1 | ENSMUSP00000116249 | ENSMUSP00000077693 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | Beta-crystallin A1; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.741 |
Bfsp2 | Crybb1 | ENSMUSP00000116249 | ENSMUSP00000031286 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | Beta-crystallin B1B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.849 |
Bfsp2 | Crybb2 | ENSMUSP00000116249 | ENSMUSP00000107955 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.808 |
Bfsp2 | Crygd | ENSMUSP00000116249 | ENSMUSP00000045327 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.797 |
Bfsp2 | Crygs | ENSMUSP00000116249 | ENSMUSP00000043588 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.832 |
Bfsp2 | Hsf4 | ENSMUSP00000116249 | ENSMUSP00000048904 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | Heat shock factor protein 4; DNA-binding protein that specifically binds heat shock promoter elements (HSE). The HSF4A isoform represses transcription while the HSF4B isoform activates transcription. | 0.864 |
Bfsp2 | Mip | ENSMUSP00000116249 | ENSMUSP00000026455 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | 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. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.796 |
Cryab | Bfsp2 | ENSMUSP00000149803 | ENSMUSP00000116249 | 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. | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | 0.674 |
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 | 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 | 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 |
Cryab | Hsf4 | ENSMUSP00000149803 | ENSMUSP00000048904 | 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. | Heat shock factor protein 4; DNA-binding protein that specifically binds heat shock promoter elements (HSE). The HSF4A isoform represses transcription while the HSF4B isoform activates transcription. | 0.689 |
Cryab | Mip | ENSMUSP00000149803 | ENSMUSP00000026455 | 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. | 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. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.649 |
Cryba1 | Bfsp2 | ENSMUSP00000077693 | ENSMUSP00000116249 | Beta-crystallin A1; Crystallins are the dominant structural components of the vertebrate eye lens. | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | 0.741 |
Cryba1 | Cryab | ENSMUSP00000077693 | ENSMUSP00000149803 | Beta-crystallin A1; 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. | 0.820 |
Cryba1 | Crybb1 | ENSMUSP00000077693 | ENSMUSP00000031286 | Beta-crystallin A1; Crystallins are the dominant structural components of the vertebrate eye lens. | Beta-crystallin B1B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.741 |
Cryba1 | Crybb2 | ENSMUSP00000077693 | ENSMUSP00000107955 | Beta-crystallin A1; 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. | 0.728 |