node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CG1416 | CG15676 | FBpp0085258 | FBpp0309728 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | Prefoldin subunit 3; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins; Belongs to the prefoldin subunit alpha family. | 0.835 |
CG1416 | CG8336 | FBpp0085258 | FBpp0076113 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | GH06403p; Peptidyl-prolyl cis-trans isomerase activity; cyclosporin A binding. It is involved in the biological process described with: protein peptidyl-prolyl isomerization; protein folding. | 0.953 |
CG1416 | Gp93 | FBpp0085258 | FBpp0084623 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | Glycoprotein 93 (Gp93) encodes a heat shock protein Hsp90 family member that is involved in midgut development. | 0.961 |
CG1416 | Hsc70Cb | FBpp0085258 | FBpp0292999 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | Hsc70Cb, isoform G; Hsc70Cb (Hsc70Cb) encodes an HSP110 family protein that interacts physically with the product of DnaJ-1 as a chaperone of misfolded proteins. It functions together with the product of DnaJ-1 to prevent the toxicity of aggregation-prone proteins. | 0.892 |
CG1416 | Hsp83 | FBpp0085258 | FBpp0305095 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | Heat shock protein 83; 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. Together with Hop and piwi, mediates canalization, also known as develop [...] | 0.985 |
CG1416 | Moca-cyp | FBpp0085258 | FBpp0084655 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | Moca-cyp, isoform A; Moca-cyp (Moca-cyp) encodes a peptidyl-prolyl cis-trans isomerase. | 0.951 |
CG1416 | Stip1 | FBpp0085258 | FBpp0077790 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | Stress induced phosphoprotein 1; Hsp90 protein binding. | 0.989 |
CG1416 | Trap1 | FBpp0085258 | FBpp0085482 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | Trap1, isoform A; Trap1 (Trap1) encodes a mitochondrial chaperone protein of the heat shock protein (HSP90) family. It shows an ATPase activity and is involved in neurodegeneration associated with mitochondrial dysfunction. | 0.908 |
CG1416 | Tsc1 | FBpp0085258 | FBpp0083931 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | LD23779p; Tsc1 (Tsc1) encodes a tumour suppressor protein that forms a complex with the product of gig. They control cellular growth via antagonizing insulin and TOR signalling pathways. | 0.904 |
CG1416 | p23 | FBpp0085258 | FBpp0081560 | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | Uncharacterized protein CG16817; prostaglandin-E synthase activity; Hsp90 protein binding; chaperone binding. It is involved in the biological process described with: protein folding; positive regulation of small RNA loading onto RISC; chaperone-mediated protein complex assembly; Belongs to the p23/wos2 family. | 0.927 |
CG15676 | CG1416 | FBpp0309728 | FBpp0085258 | Prefoldin subunit 3; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins; Belongs to the prefoldin subunit alpha family. | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | 0.835 |
CG15676 | Hsp83 | FBpp0309728 | FBpp0305095 | Prefoldin subunit 3; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins; Belongs to the prefoldin subunit alpha family. | Heat shock protein 83; 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. Together with Hop and piwi, mediates canalization, also known as develop [...] | 0.463 |
CG15676 | Stip1 | FBpp0309728 | FBpp0077790 | Prefoldin subunit 3; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins; Belongs to the prefoldin subunit alpha family. | Stress induced phosphoprotein 1; Hsp90 protein binding. | 0.593 |
CG8336 | CG1416 | FBpp0076113 | FBpp0085258 | GH06403p; Peptidyl-prolyl cis-trans isomerase activity; cyclosporin A binding. It is involved in the biological process described with: protein peptidyl-prolyl isomerization; protein folding. | LD43819p; Hsp90 protein binding; chaperone binding; ATPase activator activity. It is involved in the biological process described with: protein folding; positive regulation of ATPase activity. | 0.953 |
CG8336 | Hsc70Cb | FBpp0076113 | FBpp0292999 | GH06403p; Peptidyl-prolyl cis-trans isomerase activity; cyclosporin A binding. It is involved in the biological process described with: protein peptidyl-prolyl isomerization; protein folding. | Hsc70Cb, isoform G; Hsc70Cb (Hsc70Cb) encodes an HSP110 family protein that interacts physically with the product of DnaJ-1 as a chaperone of misfolded proteins. It functions together with the product of DnaJ-1 to prevent the toxicity of aggregation-prone proteins. | 0.471 |
CG8336 | Hsp83 | FBpp0076113 | FBpp0305095 | GH06403p; Peptidyl-prolyl cis-trans isomerase activity; cyclosporin A binding. It is involved in the biological process described with: protein peptidyl-prolyl isomerization; protein folding. | Heat shock protein 83; 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. Together with Hop and piwi, mediates canalization, also known as develop [...] | 0.987 |
CG8336 | Stip1 | FBpp0076113 | FBpp0077790 | GH06403p; Peptidyl-prolyl cis-trans isomerase activity; cyclosporin A binding. It is involved in the biological process described with: protein peptidyl-prolyl isomerization; protein folding. | Stress induced phosphoprotein 1; Hsp90 protein binding. | 0.887 |
CG8336 | Trap1 | FBpp0076113 | FBpp0085482 | GH06403p; Peptidyl-prolyl cis-trans isomerase activity; cyclosporin A binding. It is involved in the biological process described with: protein peptidyl-prolyl isomerization; protein folding. | Trap1, isoform A; Trap1 (Trap1) encodes a mitochondrial chaperone protein of the heat shock protein (HSP90) family. It shows an ATPase activity and is involved in neurodegeneration associated with mitochondrial dysfunction. | 0.818 |
CG8336 | Tsc1 | FBpp0076113 | FBpp0083931 | GH06403p; Peptidyl-prolyl cis-trans isomerase activity; cyclosporin A binding. It is involved in the biological process described with: protein peptidyl-prolyl isomerization; protein folding. | LD23779p; Tsc1 (Tsc1) encodes a tumour suppressor protein that forms a complex with the product of gig. They control cellular growth via antagonizing insulin and TOR signalling pathways. | 0.818 |
CG8336 | p23 | FBpp0076113 | FBpp0081560 | GH06403p; Peptidyl-prolyl cis-trans isomerase activity; cyclosporin A binding. It is involved in the biological process described with: protein peptidyl-prolyl isomerization; protein folding. | Uncharacterized protein CG16817; prostaglandin-E synthase activity; Hsp90 protein binding; chaperone binding. It is involved in the biological process described with: protein folding; positive regulation of small RNA loading onto RISC; chaperone-mediated protein complex assembly; Belongs to the p23/wos2 family. | 0.907 |