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 |
| VF_1477 | VF_1517 | VF_1477 | VF_1517 | Tetratricopeptide repeat family protein. | DnaK-related protein; Belongs to the heat shock protein 70 family. | 0.886 |
| VF_1477 | dnaK | VF_1477 | VF_1994 | Tetratricopeptide repeat family protein. | Chaperone Hsp70/DnaK, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.886 |
| VF_1477 | dnaK1 | VF_1477 | VF_1467 | Tetratricopeptide repeat family protein. | Chaperone, DnaK-like protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.886 |
| VF_1477 | groL | VF_1477 | VF_0205 | Tetratricopeptide repeat family protein. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.716 |
| VF_1477 | groS | VF_1477 | VF_0204 | Tetratricopeptide repeat family protein. | Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.583 |
| VF_1477 | hscA | VF_1477 | VF_0621 | Tetratricopeptide repeat family protein. | DnaK-like molecular chaperone specific for Fe-S scaffold IscU; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.886 |
| VF_1477 | hslV | VF_1477 | VF_2277 | Tetratricopeptide repeat family protein. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.511 |
| VF_1477 | htpG | VF_1477 | VF_0792 | Tetratricopeptide repeat family protein. | Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity. | 0.924 |
| VF_1477 | yegD | VF_1477 | VF_1207 | Tetratricopeptide repeat family protein. | Predicted chaperone. | 0.886 |
| VF_1517 | VF_1477 | VF_1517 | VF_1477 | DnaK-related protein; Belongs to the heat shock protein 70 family. | Tetratricopeptide repeat family protein. | 0.886 |
| VF_1517 | dnaJ | VF_1517 | VF_1993 | DnaK-related protein; Belongs to the heat shock protein 70 family. | Chaperone Hsp40/DnaJ, co-chaperone with DnaK; 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. Several rounds of ATP-dependent intera [...] | 0.837 |
| VF_1517 | groL | VF_1517 | VF_0205 | DnaK-related protein; Belongs to the heat shock protein 70 family. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.764 |
| VF_1517 | groS | VF_1517 | VF_0204 | DnaK-related protein; Belongs to the heat shock protein 70 family. | Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.723 |
| VF_1517 | hslV | VF_1517 | VF_2277 | DnaK-related protein; Belongs to the heat shock protein 70 family. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.475 |
| VF_1517 | htpG | VF_1517 | VF_0792 | DnaK-related protein; Belongs to the heat shock protein 70 family. | Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity. | 0.899 |
| dnaJ | VF_1517 | VF_1993 | VF_1517 | Chaperone Hsp40/DnaJ, co-chaperone with DnaK; 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. Several rounds of ATP-dependent intera [...] | DnaK-related protein; Belongs to the heat shock protein 70 family. | 0.837 |
| dnaJ | dnaK | VF_1993 | VF_1994 | Chaperone Hsp40/DnaJ, co-chaperone with DnaK; 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. Several rounds of ATP-dependent intera [...] | Chaperone Hsp70/DnaK, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.991 |
| dnaJ | dnaK1 | VF_1993 | VF_1467 | Chaperone Hsp40/DnaJ, co-chaperone with DnaK; 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. Several rounds of ATP-dependent intera [...] | Chaperone, DnaK-like protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.987 |
| dnaJ | groL | VF_1993 | VF_0205 | Chaperone Hsp40/DnaJ, co-chaperone with DnaK; 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. Several rounds of ATP-dependent intera [...] | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.944 |
| dnaJ | groS | VF_1993 | VF_0204 | Chaperone Hsp40/DnaJ, co-chaperone with DnaK; 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. Several rounds of ATP-dependent intera [...] | Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.861 |
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