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 |
| Cgl0094 | clpB | cg0123 | cg3079 | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | 0.600 |
| Cgl0094 | dnaJ | cg0123 | cg3098 | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | CHAPERONE WITH DNAK, HEAT SHOCK PROTEIN (DNAJ PROTEIN); 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-depend [...] | 0.942 |
| Cgl0094 | dnaK | cg0123 | cg3100 | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.976 |
| Cgl0094 | groEL | cg0123 | cg0691 | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | 60 KDA CHAPERONIN (PROTEIN CPN60) (HSP60)-N-terminal fragment. | 0.695 |
| Cgl0094 | groEL-2 | cg0123 | cg0693 | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | 60 KDA CHAPERONIN (PROTEIN CPN60) (GROEL PROTEIN) C-terminal fragment; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.696 |
| Cgl0094 | groEL-3 | cg0123 | cg3011 | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | Chaperonin cpn60 (60Kd subunit); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.694 |
| Cgl0094 | groES | cg0123 | cg0690 | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | Chaperonin 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.891 |
| Cgl0094 | grpE | cg0123 | cg3099 | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | Molecular chaperone GrpE (heat shock 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. [...] | 0.766 |
| Cgl0094 | hscA | cg0123 | cg2611 | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | Molecular chaperone, HSP70 family. | 0.973 |
| clpB | Cgl0094 | cg3079 | cg0123 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | 0.600 |
| clpB | dnaJ | cg3079 | cg3098 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | CHAPERONE WITH DNAK, HEAT SHOCK PROTEIN (DNAJ PROTEIN); 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-depend [...] | 0.993 |
| clpB | dnaK | cg3079 | cg3100 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| clpB | groEL | cg3079 | cg0691 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | 60 KDA CHAPERONIN (PROTEIN CPN60) (HSP60)-N-terminal fragment. | 0.819 |
| clpB | groEL-2 | cg3079 | cg0693 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | 60 KDA CHAPERONIN (PROTEIN CPN60) (GROEL PROTEIN) C-terminal fragment; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.878 |
| clpB | groEL-3 | cg3079 | cg3011 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | Chaperonin cpn60 (60Kd subunit); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.877 |
| clpB | groES | cg3079 | cg0690 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | Chaperonin 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.907 |
| clpB | grpE | cg3079 | cg3099 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | Molecular chaperone GrpE (heat shock 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. [...] | 0.999 |
| clpB | hrcA | cg3079 | cg2516 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | Transcriptional regulator of heat shock genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.835 |
| clpB | hscA | cg3079 | cg2611 | PROBABLE ATP-DEPENDENT PROTEASE (HEAT SHOCK PROTEIN); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Necessary [...] | Molecular chaperone, HSP70 family. | 0.818 |
| dnaJ | Cgl0094 | cg3098 | cg0123 | CHAPERONE WITH DNAK, HEAT SHOCK PROTEIN (DNAJ PROTEIN); 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-depend [...] | PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). | 0.942 |
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