node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
F10D7.3 | Y49E10.4 | F10D7.3.1 | Y49E10.4.2 | Uncharacterized monothiol glutaredoxin F10D7.3; Belongs to the glutaredoxin family. Monothiol subfamily. | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | 0.714 |
F10D7.3 | ZC334.7 | F10D7.3.1 | ZC334.7.1 | Uncharacterized monothiol glutaredoxin F10D7.3; Belongs to the glutaredoxin family. Monothiol subfamily. | Glutaredoxin domain-containing protein. | 0.905 |
Y49E10.4 | F10D7.3 | Y49E10.4.2 | F10D7.3.1 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | Uncharacterized monothiol glutaredoxin F10D7.3; Belongs to the glutaredoxin family. Monothiol subfamily. | 0.714 |
Y49E10.4 | ZC334.7 | Y49E10.4.2 | ZC334.7.1 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | Glutaredoxin domain-containing protein. | 0.690 |
Y49E10.4 | crt-1 | Y49E10.4.2 | Y38A10A.5.2 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | 0.830 |
Y49E10.4 | dnj-20 | Y49E10.4.2 | T15H9.7a.1 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | DnaJ homolog dnj-20. | 0.781 |
Y49E10.4 | enpl-1 | Y49E10.4.2 | T05E11.3a.1 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | 0.889 |
Y49E10.4 | ero-1 | Y49E10.4.2 | Y105E8B.8c.2 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | Endoplasmic reticulum oxidoreductin-1; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). | 0.948 |
Y49E10.4 | hsp-3 | Y49E10.4.2 | C15H9.6a.5 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.743 |
Y49E10.4 | hsp-4 | Y49E10.4.2 | F43E2.8a.2 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | 0.751 |
Y49E10.4 | ostb-1 | Y49E10.4.2 | T09A5.11.2 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit; Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across t [...] | 0.778 |
Y49E10.4 | pdi-3 | Y49E10.4.2 | H06O01.1.3 | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | Protein disulfide-isomerase. | 0.696 |
ZC334.7 | F10D7.3 | ZC334.7.1 | F10D7.3.1 | Glutaredoxin domain-containing protein. | Uncharacterized monothiol glutaredoxin F10D7.3; Belongs to the glutaredoxin family. Monothiol subfamily. | 0.905 |
ZC334.7 | Y49E10.4 | ZC334.7.1 | Y49E10.4.2 | Glutaredoxin domain-containing protein. | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | 0.690 |
crt-1 | Y49E10.4 | Y38A10A.5.2 | Y49E10.4.2 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | Uncharacterized protein; Belongs to the protein disulfide isomerase family. | 0.830 |
crt-1 | dnj-20 | Y38A10A.5.2 | T15H9.7a.1 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | DnaJ homolog dnj-20. | 0.663 |
crt-1 | enpl-1 | Y38A10A.5.2 | T05E11.3a.1 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | 0.989 |
crt-1 | ero-1 | Y38A10A.5.2 | Y105E8B.8c.2 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | Endoplasmic reticulum oxidoreductin-1; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity). | 0.568 |
crt-1 | hsp-3 | Y38A10A.5.2 | C15H9.6a.5 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.948 |
crt-1 | hsp-4 | Y38A10A.5.2 | F43E2.8a.2 | Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...] | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | 0.881 |