node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ahsa-1 | cyn-8 | C01G10.8.1 | D1009.2a.1 | Aha1_N domain-containing protein. | Peptidyl-prolyl cis-trans isomerase 8; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | 0.944 |
ahsa-1 | cyn-9 | C01G10.8.1 | T27D1.1.1 | Aha1_N domain-containing protein. | Peptidyl-prolyl cis-trans isomerase 9; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Thought to function as a catalyst in the folding and modification of cuticle collagens. | 0.943 |
ahsa-1 | daf-41 | C01G10.8.1 | ZC395.10.2 | Aha1_N domain-containing protein. | Co-chaperone protein daf-41; Co-chaperone for hsp90/daf-21. Involved in regulation of longevity, larval entry and exit from the dauer stage of development and response to environmental cues, such as oxidative stress, in a temperature-dependent manner. Role in daf-16 and hsf-1 inhibition at elevated temperatures. Belongs to the p23/wos2 family. | 0.982 |
ahsa-1 | dnj-13 | C01G10.8.1 | F54D5.8.2 | Aha1_N domain-containing protein. | J domain-containing protein. | 0.883 |
ahsa-1 | enpl-1 | C01G10.8.1 | T05E11.3a.1 | Aha1_N domain-containing protein. | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | 0.938 |
ahsa-1 | fkb-6 | C01G10.8.1 | F31D4.3.1 | Aha1_N domain-containing protein. | Peptidylprolyl isomerase. | 0.890 |
ahsa-1 | hsp-75 | C01G10.8.1 | R151.7a.2 | Aha1_N domain-containing protein. | HATPase_c domain-containing protein. | 0.957 |
ahsa-1 | hsp-90 | C01G10.8.1 | C47E8.5.3 | Aha1_N domain-containing protein. | Heat shock protein 90; 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. 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. By stabilizing the receptor-type guanylate cyclase daf-11 or another sig [...] | 0.994 |
ahsa-1 | pph-5 | C01G10.8.1 | Y39B6A.2a.1 | Aha1_N domain-containing protein. | Serine/threonine-protein phosphatase 5; Serine/threonine-protein phosphatase. Dephosphorylates cdc-37. Probably by dephosphorylating separase sep-1, may be involved in sep-1-mediated exocytosis of cortical granules during meiotic anaphase and mitotic cytokinesis. | 0.894 |
ahsa-1 | sti-1 | C01G10.8.1 | R09E12.3.1 | Aha1_N domain-containing protein. | Stress-induced-phosphoprotein 1; Plays a role in gonad development. Up-regulates longevity and thermotolerance. Binds daf-21/hsp90 and inhibits its ATPase activity. | 0.993 |
cyn-8 | ahsa-1 | D1009.2a.1 | C01G10.8.1 | Peptidyl-prolyl cis-trans isomerase 8; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | Aha1_N domain-containing protein. | 0.944 |
cyn-8 | daf-41 | D1009.2a.1 | ZC395.10.2 | Peptidyl-prolyl cis-trans isomerase 8; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | Co-chaperone protein daf-41; Co-chaperone for hsp90/daf-21. Involved in regulation of longevity, larval entry and exit from the dauer stage of development and response to environmental cues, such as oxidative stress, in a temperature-dependent manner. Role in daf-16 and hsf-1 inhibition at elevated temperatures. Belongs to the p23/wos2 family. | 0.864 |
cyn-8 | dnj-13 | D1009.2a.1 | F54D5.8.2 | Peptidyl-prolyl cis-trans isomerase 8; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | J domain-containing protein. | 0.893 |
cyn-8 | enpl-1 | D1009.2a.1 | T05E11.3a.1 | Peptidyl-prolyl cis-trans isomerase 8; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family. | 0.419 |
cyn-8 | hsp-75 | D1009.2a.1 | R151.7a.2 | Peptidyl-prolyl cis-trans isomerase 8; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | HATPase_c domain-containing protein. | 0.815 |
cyn-8 | hsp-90 | D1009.2a.1 | C47E8.5.3 | Peptidyl-prolyl cis-trans isomerase 8; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | Heat shock protein 90; 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. 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. By stabilizing the receptor-type guanylate cyclase daf-11 or another sig [...] | 0.815 |
cyn-8 | sti-1 | D1009.2a.1 | R09E12.3.1 | Peptidyl-prolyl cis-trans isomerase 8; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | Stress-induced-phosphoprotein 1; Plays a role in gonad development. Up-regulates longevity and thermotolerance. Binds daf-21/hsp90 and inhibits its ATPase activity. | 0.874 |
cyn-9 | ahsa-1 | T27D1.1.1 | C01G10.8.1 | Peptidyl-prolyl cis-trans isomerase 9; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Thought to function as a catalyst in the folding and modification of cuticle collagens. | Aha1_N domain-containing protein. | 0.943 |
cyn-9 | daf-41 | T27D1.1.1 | ZC395.10.2 | Peptidyl-prolyl cis-trans isomerase 9; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Thought to function as a catalyst in the folding and modification of cuticle collagens. | Co-chaperone protein daf-41; Co-chaperone for hsp90/daf-21. Involved in regulation of longevity, larval entry and exit from the dauer stage of development and response to environmental cues, such as oxidative stress, in a temperature-dependent manner. Role in daf-16 and hsf-1 inhibition at elevated temperatures. Belongs to the p23/wos2 family. | 0.932 |
cyn-9 | dnj-13 | T27D1.1.1 | F54D5.8.2 | Peptidyl-prolyl cis-trans isomerase 9; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Thought to function as a catalyst in the folding and modification of cuticle collagens. | J domain-containing protein. | 0.890 |