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 |
| PEPE_0607 | PEPE_0962 | PEPE_0607 | PEPE_0962 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.456 |
| PEPE_0607 | clpP | PEPE_0607 | PEPE_0455 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.816 |
| PEPE_0607 | dnaJ | PEPE_0607 | PEPE_0897 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.735 |
| PEPE_0607 | dnaK | PEPE_0607 | PEPE_0896 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.862 |
| PEPE_0607 | groL | PEPE_0607 | PEPE_0421 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.633 |
| PEPE_0607 | groS | PEPE_0607 | PEPE_0420 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.648 |
| PEPE_0607 | grpE | PEPE_0607 | PEPE_0895 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB 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. [...] | 0.710 |
| PEPE_0607 | hrcA | PEPE_0607 | PEPE_0894 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.598 |
| PEPE_0962 | PEPE_0607 | PEPE_0962 | PEPE_0607 | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | 0.456 |
| PEPE_0962 | PEPE_0976 | PEPE_0962 | PEPE_0976 | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | 0.456 |
| PEPE_0962 | dnaJ | PEPE_0962 | PEPE_0897 | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.702 |
| PEPE_0962 | dnaK | PEPE_0962 | PEPE_0896 | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.638 |
| PEPE_0962 | groL | PEPE_0962 | PEPE_0421 | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.817 |
| PEPE_0962 | groS | PEPE_0962 | PEPE_0420 | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.777 |
| PEPE_0962 | grpE | PEPE_0962 | PEPE_0895 | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 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. [...] | 0.862 |
| PEPE_0962 | hslV | PEPE_0962 | PEPE_0963 | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP dependent peptidase CodWX, CodW component, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| PEPE_0976 | PEPE_0962 | PEPE_0976 | PEPE_0962 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.456 |
| PEPE_0976 | clpP | PEPE_0976 | PEPE_0455 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.816 |
| PEPE_0976 | dnaJ | PEPE_0976 | PEPE_0897 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.735 |
| PEPE_0976 | dnaK | PEPE_0976 | PEPE_0896 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.862 |
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