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 |
| CCT1 | CCT8 | FBpp0083684 | FBpp0087764 | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: protein folding. | 0.999 |
| CCT1 | CG11267 | FBpp0083684 | FBpp0075609 | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | RH34413p; Metal ion binding; unfolded protein binding; chaperone binding. It is involved in the biological process described with: chaperone cofactor-dependent protein refolding; Belongs to the GroES chaperonin family. | 0.838 |
| CCT1 | CG9920 | FBpp0083684 | FBpp0082377 | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | AT30951p; Chaperone binding; unfolded protein binding; metal ion binding. It is involved in the biological process described with: chaperone cofactor-dependent protein refolding; Belongs to the GroES chaperonin family. | 0.780 |
| CCT1 | Gp93 | FBpp0083684 | FBpp0084623 | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | Glycoprotein 93 (Gp93) encodes a heat shock protein Hsp90 family member that is involved in midgut development. | 0.742 |
| CCT1 | Hsc70-5 | FBpp0083684 | FBpp0086694 | T-complex protein 1 subunit alpha; 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 70 kDa protein cognate 5. | 0.769 |
| CCT1 | Hsc70Cb | FBpp0083684 | FBpp0292999 | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 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. | 0.692 |
| CCT1 | Hsp60A | FBpp0083684 | FBpp0073290 | T-complex protein 1 subunit alpha; 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 60A; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.800 |
| CCT1 | Hsp83 | FBpp0083684 | FBpp0305095 | T-complex protein 1 subunit alpha; 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 [...] | 0.886 |
| CCT1 | Pfdn5 | FBpp0083684 | FBpp0290701 | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | Probable prefoldin subunit 5; 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 (By similarity); Belongs to the prefoldin subunit alpha family. | 0.876 |
| CCT1 | Roe1 | FBpp0083684 | FBpp0086795 | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | GrpE protein homolog, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity). | 0.768 |
| CCT8 | CCT1 | FBpp0087764 | FBpp0083684 | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: protein folding. | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 0.999 |
| CCT8 | CG11267 | FBpp0087764 | FBpp0075609 | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: protein folding. | RH34413p; Metal ion binding; unfolded protein binding; chaperone binding. It is involved in the biological process described with: chaperone cofactor-dependent protein refolding; Belongs to the GroES chaperonin family. | 0.716 |
| CCT8 | CG9920 | FBpp0087764 | FBpp0082377 | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: protein folding. | AT30951p; Chaperone binding; unfolded protein binding; metal ion binding. It is involved in the biological process described with: chaperone cofactor-dependent protein refolding; Belongs to the GroES chaperonin family. | 0.659 |
| CCT8 | Gp93 | FBpp0087764 | FBpp0084623 | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: protein folding. | Glycoprotein 93 (Gp93) encodes a heat shock protein Hsp90 family member that is involved in midgut development. | 0.655 |
| CCT8 | Hsc70-5 | FBpp0087764 | FBpp0086694 | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: protein folding. | Heat shock 70 kDa protein cognate 5. | 0.544 |
| CCT8 | Hsc70Cb | FBpp0087764 | FBpp0292999 | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: 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. | 0.917 |
| CCT8 | Hsp60A | FBpp0087764 | FBpp0073290 | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: protein folding. | Heat shock protein 60A; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.853 |
| CCT8 | Hsp83 | FBpp0087764 | FBpp0305095 | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: 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 [...] | 0.867 |
| CCT8 | Pfdn5 | FBpp0087764 | FBpp0290701 | Chaperonin containing TCP1 subunit 8; Unfolded protein binding; ATP binding. It is involved in the biological process described with: protein folding. | Probable prefoldin subunit 5; 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 (By similarity); Belongs to the prefoldin subunit alpha family. | 0.851 |
| CG11267 | CCT1 | FBpp0075609 | FBpp0083684 | RH34413p; Metal ion binding; unfolded protein binding; chaperone binding. It is involved in the biological process described with: chaperone cofactor-dependent protein refolding; Belongs to the GroES chaperonin family. | T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 0.838 |
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