node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Bfsp2 | Nol3 | G3GZG8 | G3HZK7 | Phakinin; Belongs to the intermediate filament family. | Heat shock factor protein 4; Belongs to the HSF family. | 0.622 |
Cryab | HSPA5 | G3H2H2 | G3I8R9 | 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. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | 0.576 |
Cryab | Hspb2 | G3H2H2 | G3H2H3 | 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; Belongs to the small heat shock protein (HSP20) family. | 0.698 |
Cryab | Mapkapk2 | G3H2H2 | G3HB00 | 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. | MAPKAPK2. | 0.447 |
Cryab | Nol3 | G3H2H2 | G3HZK7 | 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; Belongs to the HSF family. | 0.584 |
HSPA5 | Cryab | G3I8R9 | G3H2H2 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | 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. | 0.576 |
HSPA5 | Hspb2 | G3I8R9 | G3H2H3 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | Heat shock protein beta-2; Belongs to the small heat shock protein (HSP20) family. | 0.534 |
HSPA5 | I79_004332 | G3I8R9 | G3H2C4 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | Heat shock 70 kDa protein 4. | 0.724 |
HSPA5 | I79_012144 | G3I8R9 | G3HN14 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | Transitional endoplasmic reticulum ATPase; Belongs to the AAA ATPase family. | 0.740 |
HSPA5 | Nol3 | G3I8R9 | G3HZK7 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | Heat shock factor protein 4; Belongs to the HSF family. | 0.574 |
HSPA5 | Ptges3 | G3I8R9 | G3HRM9 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | Prostaglandin E synthase 3. | 0.711 |
HSPA5 | Sirt1 | G3I8R9 | G3HAB1 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | NAD-dependent deacetylase sirtuin-1. | 0.458 |
Hspb2 | Cryab | G3H2H3 | G3H2H2 | Heat shock protein beta-2; 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. | 0.698 |
Hspb2 | HSPA5 | G3H2H3 | G3I8R9 | Heat shock protein beta-2; Belongs to the small heat shock protein (HSP20) family. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | 0.534 |
Hspb2 | I79_004332 | G3H2H3 | G3H2C4 | Heat shock protein beta-2; Belongs to the small heat shock protein (HSP20) family. | Heat shock 70 kDa protein 4. | 0.731 |
Hspb2 | Mapkapk2 | G3H2H3 | G3HB00 | Heat shock protein beta-2; Belongs to the small heat shock protein (HSP20) family. | MAPKAPK2. | 0.662 |
Hspb2 | Nol3 | G3H2H3 | G3HZK7 | Heat shock protein beta-2; Belongs to the small heat shock protein (HSP20) family. | Heat shock factor protein 4; Belongs to the HSF family. | 0.583 |
I79_004332 | HSPA5 | G3H2C4 | G3I8R9 | Heat shock 70 kDa protein 4. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | 0.724 |
I79_004332 | Hspb2 | G3H2C4 | G3H2H3 | Heat shock 70 kDa protein 4. | Heat shock protein beta-2; Belongs to the small heat shock protein (HSP20) family. | 0.731 |
I79_004332 | I79_012144 | G3H2C4 | G3HN14 | Heat shock 70 kDa protein 4. | Transitional endoplasmic reticulum ATPase; Belongs to the AAA ATPase family. | 0.515 |