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 |
| cadD | hslO | llmg_2203 | llmg_2204 | Cadmium resistance transporter family protein. | Heat shock protein, 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.516 |
| cadD | llmg_2205 | llmg_2203 | llmg_2205 | Cadmium resistance transporter family protein. | Conserved hypothetical protein; Bacterial bifunctional deaminase-reductase, C-terminal. | 0.414 |
| clpE | dnaJ | llmg_0528 | llmg_2502 | ATP-dependent Clp protease ATP-binding subunit clpE; Along with ClpP could be necessary for degrading proteins generated by certain types of stress. | Chaperone protein dnaJ; 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 interactions between DnaJ, D [...] | 0.869 |
| clpE | dnaK | llmg_0528 | llmg_1574 | ATP-dependent Clp protease ATP-binding subunit clpE; Along with ClpP could be necessary for degrading proteins generated by certain types of stress. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.968 |
| clpE | groEL2 | llmg_0528 | llmg_0411 | ATP-dependent Clp protease ATP-binding subunit clpE; Along with ClpP could be necessary for degrading proteins generated by certain types of stress. | Heat shock protein groEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.942 |
| clpE | grpE | llmg_0528 | llmg_1575 | ATP-dependent Clp protease ATP-binding subunit clpE; Along with ClpP could be necessary for degrading proteins generated by certain types of stress. | GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 i [...] | 0.906 |
| clpE | hslO | llmg_0528 | llmg_2204 | ATP-dependent Clp protease ATP-binding subunit clpE; Along with ClpP could be necessary for degrading proteins generated by certain types of stress. | Heat shock protein, 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.564 |
| dnaJ | clpE | llmg_2502 | llmg_0528 | Chaperone protein dnaJ; 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 interactions between DnaJ, D [...] | ATP-dependent Clp protease ATP-binding subunit clpE; Along with ClpP could be necessary for degrading proteins generated by certain types of stress. | 0.869 |
| dnaJ | dnaK | llmg_2502 | llmg_1574 | Chaperone protein dnaJ; 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 interactions between DnaJ, D [...] | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groEL2 | llmg_2502 | llmg_0411 | Chaperone protein dnaJ; 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 interactions between DnaJ, D [...] | Heat shock protein groEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.983 |
| dnaJ | grpE | llmg_2502 | llmg_1575 | Chaperone protein dnaJ; 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 interactions between DnaJ, D [...] | GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 i [...] | 0.999 |
| dnaJ | hslO | llmg_2502 | llmg_2204 | Chaperone protein dnaJ; 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 interactions between DnaJ, D [...] | Heat shock protein, 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.699 |
| dnaK | clpE | llmg_1574 | llmg_0528 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent Clp protease ATP-binding subunit clpE; Along with ClpP could be necessary for degrading proteins generated by certain types of stress. | 0.968 |
| dnaK | dnaJ | llmg_1574 | llmg_2502 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperone protein dnaJ; 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 interactions between DnaJ, D [...] | 0.999 |
| dnaK | groEL2 | llmg_1574 | llmg_0411 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein groEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.997 |
| dnaK | grpE | llmg_1574 | llmg_1575 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 i [...] | 0.999 |
| dnaK | hslO | llmg_1574 | llmg_2204 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein, 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.517 |
| groEL2 | clpE | llmg_0411 | llmg_0528 | Heat shock protein groEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | ATP-dependent Clp protease ATP-binding subunit clpE; Along with ClpP could be necessary for degrading proteins generated by certain types of stress. | 0.942 |
| groEL2 | dnaJ | llmg_0411 | llmg_2502 | Heat shock protein groEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperone protein dnaJ; 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 interactions between DnaJ, D [...] | 0.983 |
| groEL2 | dnaK | llmg_0411 | llmg_1574 | Heat shock protein groEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
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