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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpB | dnaJ2 | PFREUD_17920 | PFREUD_04650 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); 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; Belongs to the ClpA/ClpB family. | Chaperone protein dnaJ 2 (DnaJ2 protein) (Heat shock protein 40 2); 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 o [...] | 0.750 |
| clpB | dnaK1 | PFREUD_17920 | PFREUD_17840 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); 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; Belongs to the ClpA/ClpB family. | Chaperone protein dnaK 1 (Heat shock protein 70 1) (Heat shock 70 kDa protein 1) (HSP70 1); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.959 |
| clpB | dnaK2 | PFREUD_17920 | PFREUD_04630 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); 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; Belongs to the ClpA/ClpB family. | Chaperone protein dnaK 2 (Heat shock protein 70 2) (Heat shock 70 kDa protein 2) (HSP70 2); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.960 |
| clpB | groL1 | PFREUD_17920 | PFREUD_06470 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); 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; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin 1 (Protein Cpn60 1) (groEL protein 1) (Heat shock protein 60 1); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.845 |
| clpB | groL2 | PFREUD_17920 | PFREUD_18470 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); 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; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin 2 (Protein Cpn60 2) (groEL protein 2) (Heat shock protein 60 2); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.844 |
| clpB | groS1(groES1) | PFREUD_17920 | PFREUD_06460 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); 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; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin 1 (Protein Cpn10 1) (groES protein 1) (Heat shock 10 1); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.733 |
| clpB | grpE1 | PFREUD_17920 | PFREUD_17830 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); 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; Belongs to the ClpA/ClpB family. | Protein GrpE 1 (HSP-70 cofactor 1) (Co-chaperone protein GrpE1); 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 th [...] | 0.907 |
| clpB | grpE2 | PFREUD_17920 | PFREUD_04640 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); 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; Belongs to the ClpA/ClpB family. | Protein GrpE 2 (HSP-70 cofactor 2) (Co-chaperone protein GrpE2); 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 th [...] | 0.905 |
| clpB-2 | dnaJ2 | PFREUD_19250 | PFREUD_04650 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); 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). | Chaperone protein dnaJ 2 (DnaJ2 protein) (Heat shock protein 40 2); 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 o [...] | 0.750 |
| clpB-2 | dnaK1 | PFREUD_19250 | PFREUD_17840 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); 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). | Chaperone protein dnaK 1 (Heat shock protein 70 1) (Heat shock 70 kDa protein 1) (HSP70 1); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.959 |
| clpB-2 | dnaK2 | PFREUD_19250 | PFREUD_04630 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); 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). | Chaperone protein dnaK 2 (Heat shock protein 70 2) (Heat shock 70 kDa protein 2) (HSP70 2); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.959 |
| clpB-2 | groL1 | PFREUD_19250 | PFREUD_06470 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); 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). | 60 kDa chaperonin 1 (Protein Cpn60 1) (groEL protein 1) (Heat shock protein 60 1); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.844 |
| clpB-2 | groL2 | PFREUD_19250 | PFREUD_18470 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); 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). | 60 kDa chaperonin 2 (Protein Cpn60 2) (groEL protein 2) (Heat shock protein 60 2); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.843 |
| clpB-2 | groS1(groES1) | PFREUD_19250 | PFREUD_06460 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); 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). | 10 kDa chaperonin 1 (Protein Cpn10 1) (groES protein 1) (Heat shock 10 1); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.733 |
| clpB-2 | grpE1 | PFREUD_19250 | PFREUD_17830 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); 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). | Protein GrpE 1 (HSP-70 cofactor 1) (Co-chaperone protein GrpE1); 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 th [...] | 0.906 |
| clpB-2 | grpE2 | PFREUD_19250 | PFREUD_04640 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); 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). | Protein GrpE 2 (HSP-70 cofactor 2) (Co-chaperone protein GrpE2); 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 th [...] | 0.891 |
| dnaJ2 | clpB | PFREUD_04650 | PFREUD_17920 | Chaperone protein dnaJ 2 (DnaJ2 protein) (Heat shock protein 40 2); 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 o [...] | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); 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; Belongs to the ClpA/ClpB family. | 0.750 |
| dnaJ2 | clpB-2 | PFREUD_04650 | PFREUD_19250 | Chaperone protein dnaJ 2 (DnaJ2 protein) (Heat shock protein 40 2); 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 o [...] | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); 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). | 0.750 |
| dnaJ2 | dnaK1 | PFREUD_04650 | PFREUD_17840 | Chaperone protein dnaJ 2 (DnaJ2 protein) (Heat shock protein 40 2); 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 o [...] | Chaperone protein dnaK 1 (Heat shock protein 70 1) (Heat shock 70 kDa protein 1) (HSP70 1); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.985 |
| dnaJ2 | dnaK2 | PFREUD_04650 | PFREUD_04630 | Chaperone protein dnaJ 2 (DnaJ2 protein) (Heat shock protein 40 2); 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 o [...] | Chaperone protein dnaK 2 (Heat shock protein 70 2) (Heat shock 70 kDa protein 2) (HSP70 2); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.990 |
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