node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
T22F3.12 | fkb-6 | T22F3.12.1 | F31D4.3.1 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Peptidylprolyl isomerase. | 0.727 |
T22F3.12 | hsp-90 | T22F3.12.1 | C47E8.5.3 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 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 [...] | 0.514 |
Y17G9B.4 | daf-41 | Y17G9B.4a.1 | ZC395.10.2 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 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. | 0.417 |
Y17G9B.4 | fkb-6 | Y17G9B.4a.1 | F31D4.3.1 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Peptidylprolyl isomerase. | 0.734 |
Y17G9B.4 | hsp-90 | Y17G9B.4a.1 | C47E8.5.3 | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 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 [...] | 0.524 |
adsl-1 | fkb-6 | R06C7.5a.2 | F31D4.3.1 | Adenylosuccinate lyase; Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. | Peptidylprolyl isomerase. | 0.917 |
adsl-1 | git-1 | R06C7.5a.2 | F14F3.2.1 | Adenylosuccinate lyase; Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate. | GIT1 (Mammalian G protein-coupled receptor kinase InTeractor 1) homolog. | 0.747 |
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 | fkb-6 | C01G10.8.1 | F31D4.3.1 | Aha1_N domain-containing protein. | Peptidylprolyl isomerase. | 0.890 |
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 |
daf-41 | Y17G9B.4 | ZC395.10.2 | Y17G9B.4a.1 | 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. | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.417 |
daf-41 | ahsa-1 | ZC395.10.2 | C01G10.8.1 | 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. | Aha1_N domain-containing protein. | 0.982 |
daf-41 | fkb-6 | ZC395.10.2 | F31D4.3.1 | 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. | Peptidylprolyl isomerase. | 0.982 |
daf-41 | hsp-90 | ZC395.10.2 | C47E8.5.3 | 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. | 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 [...] | 0.998 |
daf-41 | pph-5 | ZC395.10.2 | Y39B6A.2a.1 | 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. | 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. | 0.987 |
daf-41 | sti-1 | ZC395.10.2 | R09E12.3.1 | 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. | Stress-induced-phosphoprotein 1; Plays a role in gonad development. Up-regulates longevity and thermotolerance. Binds daf-21/hsp90 and inhibits its ATPase activity. | 0.985 |
fkb-6 | T22F3.12 | F31D4.3.1 | T22F3.12.1 | Peptidylprolyl isomerase. | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.727 |
fkb-6 | Y17G9B.4 | F31D4.3.1 | Y17G9B.4a.1 | Peptidylprolyl isomerase. | Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.734 |