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 |
| CCT3 | CG1416 | FBpp0082788 | FBpp0085258 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 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. | 0.516 |
| CCT3 | CG8336 | FBpp0082788 | FBpp0076113 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 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. | 0.744 |
| CCT3 | Hsp83 | FBpp0082788 | FBpp0305095 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 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 [...] | 0.933 |
| CCT3 | Nrd1 | FBpp0082788 | FBpp0073438 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | Nardilysin (Nrd1) encodes a protein involved in chaperone-mediated protein folding; Belongs to the peptidase M16 family. | 0.720 |
| CCT3 | Stip1 | FBpp0082788 | FBpp0077790 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | Stress induced phosphoprotein 1; Hsp90 protein binding. | 0.742 |
| CCT3 | Trap1 | FBpp0082788 | FBpp0085482 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 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. | 0.601 |
| CCT3 | Tsc1 | FBpp0082788 | FBpp0083931 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 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. | 0.591 |
| CG1416 | CCT3 | FBpp0085258 | FBpp0082788 | 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. | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 0.516 |
| CG1416 | CG2887 | FBpp0085258 | FBpp0071393 | 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. | AT19485p; Chaperone binding; unfolded protein binding. It is involved in the biological process described with: negative regulation of transcription by RNA polymerase II; chaperone cofactor-dependent protein refolding. | 0.619 |
| 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 | 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 | Sil1 | FBpp0085258 | FBpp0084244 | 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. | Nucleotide exchange factor Sil1; Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for an ER lumenal chaperone of HSP70 family (By similarity). Belongs to the SIL1 family. | 0.695 |
| 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 |
| CG2887 | CG1416 | FBpp0071393 | FBpp0085258 | AT19485p; Chaperone binding; unfolded protein binding. It is involved in the biological process described with: negative regulation of transcription by RNA polymerase II; chaperone cofactor-dependent protein refolding. | 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. | 0.619 |
| CG2887 | CG8336 | FBpp0071393 | FBpp0076113 | AT19485p; Chaperone binding; unfolded protein binding. It is involved in the biological process described with: negative regulation of transcription by RNA polymerase II; chaperone cofactor-dependent protein refolding. | 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. | 0.727 |
| CG2887 | Hsp83 | FBpp0071393 | FBpp0305095 | AT19485p; Chaperone binding; unfolded protein binding. It is involved in the biological process described with: negative regulation of transcription by RNA polymerase II; chaperone cofactor-dependent protein refolding. | 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 [...] | 0.515 |
| CG2887 | Sil1 | FBpp0071393 | FBpp0084244 | AT19485p; Chaperone binding; unfolded protein binding. It is involved in the biological process described with: negative regulation of transcription by RNA polymerase II; chaperone cofactor-dependent protein refolding. | Nucleotide exchange factor Sil1; Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for an ER lumenal chaperone of HSP70 family (By similarity). Belongs to the SIL1 family. | 0.751 |
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