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 |
| CA_C0648 | clpB | CA_C0648 | CA_C0959 | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | 0.710 |
| CA_C0648 | clpC | CA_C0648 | CA_C3189 | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | ATPases with chaperone activity clpC, two ATP-binding domain; Belongs to the ClpA/ClpB family. | 0.710 |
| CA_C0648 | dnaK-3 | CA_C0648 | CA_C1282 | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | Molecular chaperone DnaK, HSP70 family; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.954 |
| CA_C0648 | groEL | CA_C0648 | CA_C2703 | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | Chaperonin GroEL, HSP60 family; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.787 |
| CA_C0648 | groES | CA_C0648 | CA_C2704 | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | Co-chaperonin GroES, HSP10 family; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.717 |
| CA_C0648 | grpE | CA_C0648 | CA_C1281 | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | Molecular chaperone GrpE; 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 [...] | 0.889 |
| CA_C0648 | hrcA | CA_C0648 | CA_C1280 | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | Transcriptional regulator of heat shock genes, HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons; Belongs to the HrcA family. | 0.773 |
| CA_C0648 | hsp18 | CA_C0648 | CA_C3714 | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | Molecular chaperone (small heat shock protein), HSP18; Probable chaperone; Belongs to the small heat shock protein (HSP20) family. | 0.590 |
| CA_C0648 | htpG | CA_C0648 | CA_C3315 | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | Molecular chaperone, HSP90 family; Molecular chaperone. Has ATPase activity. | 0.938 |
| clpB | CA_C0648 | CA_C0959 | CA_C0648 | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | 0.710 |
| clpB | dnaJ | CA_C0959 | CA_C1283 | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | Molecular chaperones DnaJ (HSP40 family); 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 interactio [...] | 0.859 |
| clpB | dnaK-3 | CA_C0959 | CA_C1282 | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | Molecular chaperone DnaK, HSP70 family; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.960 |
| clpB | groEL | CA_C0959 | CA_C2703 | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | Chaperonin GroEL, HSP60 family; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.862 |
| clpB | groES | CA_C0959 | CA_C2704 | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | Co-chaperonin GroES, HSP10 family; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.810 |
| clpB | grpE | CA_C0959 | CA_C1281 | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | Molecular chaperone GrpE; 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 [...] | 0.869 |
| clpB | hrcA | CA_C0959 | CA_C1280 | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | Transcriptional regulator of heat shock genes, HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons; Belongs to the HrcA family. | 0.683 |
| clpB | hsp18 | CA_C0959 | CA_C3714 | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | Molecular chaperone (small heat shock protein), HSP18; Probable chaperone; Belongs to the small heat shock protein (HSP20) family. | 0.780 |
| clpB | htpG | CA_C0959 | CA_C3315 | ATPase with chaperone activity, two ATP-binding domains; 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). Belongs [...] | Molecular chaperone, HSP90 family; Molecular chaperone. Has ATPase activity. | 0.917 |
| clpC | CA_C0648 | CA_C3189 | CA_C0648 | ATPases with chaperone activity clpC, two ATP-binding domain; Belongs to the ClpA/ClpB family. | Molecular chaperone, DnaJ family (contain C-term. Zn finger domain). | 0.710 |
| clpC | dnaJ | CA_C3189 | CA_C1283 | ATPases with chaperone activity clpC, two ATP-binding domain; Belongs to the ClpA/ClpB family. | Molecular chaperones DnaJ (HSP40 family); 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 interactio [...] | 0.864 |
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