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 |
| Daro_2058 | Daro_3428 | Daro_2058 | Daro_3428 | Heat shock protein DnaJ, N-terminal. | Molecular chaperone-like protein. | 0.926 |
| Daro_2058 | Daro_3636 | Daro_2058 | Daro_3636 | Heat shock protein DnaJ, N-terminal. | Heat shock protein DnaJ, N-terminal. | 0.772 |
| Daro_2058 | dnaJ-2 | Daro_2058 | Daro_2467 | Heat shock protein DnaJ, N-terminal. | DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] | 0.769 |
| Daro_2058 | htpG | Daro_2058 | Daro_1127 | Heat shock protein DnaJ, N-terminal. | Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. | 0.728 |
| Daro_3428 | Daro_2058 | Daro_3428 | Daro_2058 | Molecular chaperone-like protein. | Heat shock protein DnaJ, N-terminal. | 0.926 |
| Daro_3428 | Daro_3636 | Daro_3428 | Daro_3636 | Molecular chaperone-like protein. | Heat shock protein DnaJ, N-terminal. | 0.947 |
| Daro_3428 | dnaJ-2 | Daro_3428 | Daro_2467 | Molecular chaperone-like protein. | DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] | 0.950 |
| Daro_3428 | htpG | Daro_3428 | Daro_1127 | Molecular chaperone-like protein. | Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. | 0.952 |
| Daro_3636 | Daro_2058 | Daro_3636 | Daro_2058 | Heat shock protein DnaJ, N-terminal. | Heat shock protein DnaJ, N-terminal. | 0.772 |
| Daro_3636 | Daro_3428 | Daro_3636 | Daro_3428 | Heat shock protein DnaJ, N-terminal. | Molecular chaperone-like protein. | 0.947 |
| Daro_3636 | dnaJ-2 | Daro_3636 | Daro_2467 | Heat shock protein DnaJ, N-terminal. | DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] | 0.773 |
| Daro_3636 | htpG | Daro_3636 | Daro_1127 | Heat shock protein DnaJ, N-terminal. | Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. | 0.909 |
| dnaJ-2 | Daro_2058 | Daro_2467 | Daro_2058 | DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] | Heat shock protein DnaJ, N-terminal. | 0.769 |
| dnaJ-2 | Daro_3428 | Daro_2467 | Daro_3428 | DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] | Molecular chaperone-like protein. | 0.950 |
| dnaJ-2 | Daro_3636 | Daro_2467 | Daro_3636 | DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] | Heat shock protein DnaJ, N-terminal. | 0.773 |
| dnaJ-2 | htpG | Daro_2467 | Daro_1127 | DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] | Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. | 0.897 |
| htpG | Daro_2058 | Daro_1127 | Daro_2058 | Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. | Heat shock protein DnaJ, N-terminal. | 0.728 |
| htpG | Daro_3428 | Daro_1127 | Daro_3428 | Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. | Molecular chaperone-like protein. | 0.952 |
| htpG | Daro_3636 | Daro_1127 | Daro_3636 | Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. | Heat shock protein DnaJ, N-terminal. | 0.909 |
| htpG | dnaJ-2 | Daro_1127 | Daro_2467 | Heat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. | DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. [...] | 0.897 |