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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| HIP | Hsc70Cb | FBpp0070575 | FBpp0292999 | Chaperone binding; protein dimerization activity; heat shock protein binding; Hsp70 protein binding. It is involved in the biological process described with: protein-containing complex assembly; chaperone cofactor-dependent protein refolding; chaperone-mediated 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. | 0.406 |
| HIP | Hsp83 | FBpp0070575 | FBpp0305095 | Chaperone binding; protein dimerization activity; heat shock protein binding; Hsp70 protein binding. It is involved in the biological process described with: protein-containing complex assembly; chaperone cofactor-dependent protein refolding; chaperone-mediated 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 [...] | 0.511 |
| HIP | p23 | FBpp0070575 | FBpp0081560 | Chaperone binding; protein dimerization activity; heat shock protein binding; Hsp70 protein binding. It is involved in the biological process described with: protein-containing complex assembly; chaperone cofactor-dependent protein refolding; chaperone-mediated 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. | 0.509 |
| Hsc70Cb | HIP | FBpp0292999 | FBpp0070575 | 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. | Chaperone binding; protein dimerization activity; heat shock protein binding; Hsp70 protein binding. It is involved in the biological process described with: protein-containing complex assembly; chaperone cofactor-dependent protein refolding; chaperone-mediated protein folding. | 0.406 |
| Hsc70Cb | Hsp83 | FBpp0292999 | FBpp0305095 | 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. | 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 [...] | 0.973 |
| Hsc70Cb | p23 | FBpp0292999 | FBpp0081560 | 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. | 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. | 0.705 |
| Hsp83 | HIP | FBpp0305095 | FBpp0070575 | 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 [...] | Chaperone binding; protein dimerization activity; heat shock protein binding; Hsp70 protein binding. It is involved in the biological process described with: protein-containing complex assembly; chaperone cofactor-dependent protein refolding; chaperone-mediated protein folding. | 0.511 |
| Hsp83 | Hsc70Cb | FBpp0305095 | FBpp0292999 | 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 [...] | 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. | 0.973 |
| Hsp83 | p23 | FBpp0305095 | FBpp0081560 | 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 [...] | 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. | 0.998 |
| p23 | HIP | FBpp0081560 | FBpp0070575 | 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. | Chaperone binding; protein dimerization activity; heat shock protein binding; Hsp70 protein binding. It is involved in the biological process described with: protein-containing complex assembly; chaperone cofactor-dependent protein refolding; chaperone-mediated protein folding. | 0.509 |
| p23 | Hsc70Cb | FBpp0081560 | FBpp0292999 | 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. | 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. | 0.705 |
| p23 | Hsp83 | FBpp0081560 | FBpp0305095 | 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. | 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 [...] | 0.998 |