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 |
| CLPB | GROEL | WS0609 | WS0308 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.650 |
| CLPB | GRPE | WS0609 | WS0495 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | GRPE PROTEIN (HSP-70 COFACTOR); 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 [...] | 0.866 |
| CLPB | WS0496 | WS0609 | WS0496 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | Hypothetical protein. | 0.695 |
| CLPB | WS1253 | WS0609 | WS1253 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | CO-CHAPERONE-CURVED DNA BINDING PROTEIN A CBPA. | 0.714 |
| CLPB | dnaJ | WS0609 | WS0698 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB 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-dependen [...] | 0.789 |
| CLPB | dnaK | WS0609 | WS0494 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | HEAT SHOCK PROTEIN, DNAK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.970 |
| CLPB | groS | WS0609 | WS0309 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | HEAT SHOCK PROTEIN GROES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.756 |
| CLPB | hslU | WS0609 | WS1293 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | CLPY PROTEIN; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.705 |
| CLPB | hslV | WS0609 | WS1294 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | HEAT SHOCK PROTEIN; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.468 |
| CLPB | lon | WS0609 | WS1972 | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | PUTATIVE ATP-DEPENDENT PROTEASE LA PROTEIN; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.680 |
| GROEL | CLPB | WS0308 | WS0609 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | CLP PROTEASE ATP-BINDING SUBUNIT; 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 to the ClpA/ClpB family. | 0.650 |
| GROEL | GRPE | WS0308 | WS0495 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | GRPE PROTEIN (HSP-70 COFACTOR); 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 [...] | 0.979 |
| GROEL | WS0496 | WS0308 | WS0496 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Hypothetical protein. | 0.761 |
| GROEL | WS1253 | WS0308 | WS1253 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | CO-CHAPERONE-CURVED DNA BINDING PROTEIN A CBPA. | 0.760 |
| GROEL | dnaJ | WS0308 | WS0698 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 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-dependen [...] | 0.912 |
| GROEL | dnaK | WS0308 | WS0494 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | HEAT SHOCK PROTEIN, DNAK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.978 |
| GROEL | groS | WS0308 | WS0309 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | HEAT SHOCK PROTEIN GROES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.998 |
| GROEL | hslU | WS0308 | WS1293 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | CLPY PROTEIN; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.870 |
| GROEL | hslV | WS0308 | WS1294 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | HEAT SHOCK PROTEIN; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.830 |
| GROEL | lon | WS0308 | WS1972 | HEAT SHOCK PROTEIN; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | PUTATIVE ATP-DEPENDENT PROTEASE LA PROTEIN; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.843 |
page 1 of 6