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 | Hspb7 | ENSMUSP00000019192 | ENSMUSP00000099544 | 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). | Heat shock protein beta-7. | 0.435 |
Cryaa | Hspb9 | ENSMUSP00000019192 | ENSMUSP00000130551 | 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). | Heat shock protein beta-9. | 0.527 |
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 | Hspb1 | ENSMUSP00000149803 | ENSMUSP00000005077 | 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 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 (By similarity). | 0.875 |
Cryab | Hspb2 | ENSMUSP00000149803 | ENSMUSP00000042374 | 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 protein beta-2; May regulate the kinase DMPK; Belongs to the small heat shock protein (HSP20) family. | 0.842 |
Cryab | Hspb6 | ENSMUSP00000149803 | ENSMUSP00000039172 | 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 protein beta-6; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. | 0.782 |
Cryab | Hspb7 | ENSMUSP00000149803 | ENSMUSP00000099544 | 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 protein beta-7. | 0.422 |
Cryab | Hspb8 | ENSMUSP00000149803 | ENSMUSP00000037007 | 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 protein beta-8; Displays temperature-dependent chaperone activity; Belongs to the small heat shock protein (HSP20) family. | 0.761 |
Cryab | Hspb9 | ENSMUSP00000149803 | ENSMUSP00000130551 | 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 protein beta-9. | 0.608 |
Hspb1 | Cryab | ENSMUSP00000005077 | ENSMUSP00000149803 | 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 (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. | 0.875 |
Hspb1 | Hspb6 | ENSMUSP00000005077 | ENSMUSP00000039172 | 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 (By similarity). | Heat shock protein beta-6; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. | 0.408 |
Hspb1 | Hspb7 | ENSMUSP00000005077 | ENSMUSP00000099544 | 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 (By similarity). | Heat shock protein beta-7. | 0.492 |
Hspb1 | Hspb8 | ENSMUSP00000005077 | ENSMUSP00000037007 | 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 (By similarity). | Heat shock protein beta-8; Displays temperature-dependent chaperone activity; Belongs to the small heat shock protein (HSP20) family. | 0.921 |
Hspb1 | Hspb9 | ENSMUSP00000005077 | ENSMUSP00000130551 | 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 (By similarity). | Heat shock protein beta-9. | 0.495 |
Hspb2 | Cryab | ENSMUSP00000042374 | ENSMUSP00000149803 | Heat shock protein beta-2; May regulate the kinase DMPK; Belongs to the small heat shock protein (HSP20) 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. | 0.842 |
Hspb2 | Hspb3 | ENSMUSP00000042374 | ENSMUSP00000054193 | Heat shock protein beta-2; May regulate the kinase DMPK; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein beta-3; Inhibitor of actin polymerization; Belongs to the small heat shock protein (HSP20) family. | 0.917 |
Hspb2 | Hspb7 | ENSMUSP00000042374 | ENSMUSP00000099544 | Heat shock protein beta-2; May regulate the kinase DMPK; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein beta-7. | 0.867 |
Hspb2 | Hspb8 | ENSMUSP00000042374 | ENSMUSP00000037007 | Heat shock protein beta-2; May regulate the kinase DMPK; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein beta-8; Displays temperature-dependent chaperone activity; Belongs to the small heat shock protein (HSP20) family. | 0.865 |
Hspb2 | Hspb9 | ENSMUSP00000042374 | ENSMUSP00000130551 | Heat shock protein beta-2; May regulate the kinase DMPK; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein beta-9. | 0.756 |