node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CALR | CANX | ENSSSCP00000014615 | ENSSSCP00000048577 | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin family. | Calnexin. | 0.968 |
CALR | DNAJB11 | ENSSSCP00000014615 | ENSSSCP00000012569 | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin family. | DnaJ homolog subfamily B member 11. | 0.635 |
CALR | HSP90AA1 | ENSSSCP00000014615 | ENSSSCP00000046159 | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin family. | Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] | 0.717 |
CALR | HSP90B1 | ENSSSCP00000014615 | ENSSSCP00000000906 | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin family. | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Belongs to the heat shock protein 90 family. | 0.997 |
CALR | HSPA5 | ENSSSCP00000014615 | ENSSSCP00000055982 | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin 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 [...] | 0.975 |
CALR | PDIA3 | ENSSSCP00000014615 | ENSSSCP00000005064 | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin family. | Protein disulfide-isomerase. | 0.999 |
CALR | PDIA4 | ENSSSCP00000014615 | ENSSSCP00000016385 | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin family. | Protein disulfide-isomerase. | 0.965 |
CALR | PDIA6 | ENSSSCP00000014615 | ENSSSCP00000009202 | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin family. | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | 0.931 |
CALR3 | CANX | ENSSSCP00000014732 | ENSSSCP00000048577 | Calreticulin. | Calnexin. | 0.939 |
CALR3 | DNAJB11 | ENSSSCP00000014732 | ENSSSCP00000012569 | Calreticulin. | DnaJ homolog subfamily B member 11. | 0.415 |
CALR3 | HSP90AA1 | ENSSSCP00000014732 | ENSSSCP00000046159 | Calreticulin. | Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] | 0.717 |
CALR3 | HSP90B1 | ENSSSCP00000014732 | ENSSSCP00000000906 | Calreticulin. | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Belongs to the heat shock protein 90 family. | 0.977 |
CALR3 | HSPA5 | ENSSSCP00000014732 | ENSSSCP00000055982 | Calreticulin. | 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 [...] | 0.946 |
CALR3 | PDIA3 | ENSSSCP00000014732 | ENSSSCP00000005064 | Calreticulin. | Protein disulfide-isomerase. | 0.929 |
CALR3 | PDIA4 | ENSSSCP00000014732 | ENSSSCP00000016385 | Calreticulin. | Protein disulfide-isomerase. | 0.832 |
CALR3 | PDIA6 | ENSSSCP00000014732 | ENSSSCP00000009202 | Calreticulin. | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | 0.780 |
CANX | CALR | ENSSSCP00000048577 | ENSSSCP00000014615 | Calnexin. | Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis; Belongs to the calreticulin family. | 0.968 |
CANX | CALR3 | ENSSSCP00000048577 | ENSSSCP00000014732 | Calnexin. | Calreticulin. | 0.939 |
CANX | DNAJB11 | ENSSSCP00000048577 | ENSSSCP00000012569 | Calnexin. | DnaJ homolog subfamily B member 11. | 0.432 |
CANX | HSP90AA1 | ENSSSCP00000048577 | ENSSSCP00000046159 | Calnexin. | Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] | 0.614 |