Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 | Cdc37 | FBpp0085258 | FBpp0072660 | 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. | Hsp90 co-chaperone Cdc37; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Required for cytokinesis and chromosome segregation in mitosis and male meiosis. Belongs to the CDC37 family. | 0.707 |
| CG1416 | Fkbp59 | FBpp0085258 | FBpp0309663 | 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. | FK506-binding protein 59kD (Fkbp59) encodes a peptidylprolyl isomerase involved in the regulation of calcium transport and phototransduction. | 0.755 |
| CG1416 | Hsc70-3 | FBpp0085258 | FBpp0073447 | 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. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins (By similarity). Acts as a key repressor of the unfolded protein response (UPR) (By similarity). | 0.760 |
| CG1416 | Hsp68 | FBpp0085258 | FBpp0083974 | 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 68 (Hsp68) encodes a protein involved in lifespan determination and response to heat shock and starvation. | 0.569 |
| 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 | PpD3 | FBpp0085258 | FBpp0081606 | 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. | Protein phosphatase D3 (PpD3) encodes a protein required for mitosis. | 0.668 |
| 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 | 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 |
| 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 | Cdc37 | FBpp0076113 | FBpp0072660 | 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. | Hsp90 co-chaperone Cdc37; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Required for cytokinesis and chromosome segregation in mitosis and male meiosis. Belongs to the CDC37 family. | 0.524 |
| CG8336 | Fkbp59 | FBpp0076113 | FBpp0309663 | 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. | FK506-binding protein 59kD (Fkbp59) encodes a peptidylprolyl isomerase involved in the regulation of calcium transport and phototransduction. | 0.580 |
| CG8336 | Hsc70-3 | FBpp0076113 | FBpp0073447 | 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. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins (By similarity). Acts as a key repressor of the unfolded protein response (UPR) (By similarity). | 0.544 |
| 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 | 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 |
| Cdc37 | CG1416 | FBpp0072660 | FBpp0085258 | Hsp90 co-chaperone Cdc37; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Required for cytokinesis and chromosome segregation in mitosis and male meiosis. Belongs to the CDC37 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. | 0.707 |
| Cdc37 | CG8336 | FBpp0072660 | FBpp0076113 | Hsp90 co-chaperone Cdc37; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Required for cytokinesis and chromosome segregation in mitosis and male meiosis. Belongs to the CDC37 family. | 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. | 0.524 |
| Cdc37 | Fkbp59 | FBpp0072660 | FBpp0309663 | Hsp90 co-chaperone Cdc37; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Required for cytokinesis and chromosome segregation in mitosis and male meiosis. Belongs to the CDC37 family. | FK506-binding protein 59kD (Fkbp59) encodes a peptidylprolyl isomerase involved in the regulation of calcium transport and phototransduction. | 0.422 |
| Cdc37 | Hsp83 | FBpp0072660 | FBpp0305095 | Hsp90 co-chaperone Cdc37; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Required for cytokinesis and chromosome segregation in mitosis and male meiosis. Belongs to the CDC37 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 [...] | 0.993 |
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