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 |
| PMM1432 | clpB1 | PMM1432 | PMM0580 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | 0.639 |
| PMM1432 | clpC | PMM1432 | PMM1088 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | 0.638 |
| PMM1432 | clpP1 | PMM1432 | PMM0742 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | Clp protease subunit; 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. | 0.414 |
| PMM1432 | groEL | PMM1432 | PMM1436 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | GroEL protein (Chaperonin cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.688 |
| PMM1432 | groEL2,cpn60-2 | PMM1432 | PMM0452 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | GroEL2 protein (Chaperonin cpn60 2); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.691 |
| PMM1432 | groES | PMM1432 | PMM1437 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | GroES protein (Chaperonin cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.718 |
| PMM1432 | grpE | PMM1432 | PMM0016 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | Heat shock protein 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- [...] | 0.888 |
| PMM1432 | htpG | PMM1432 | PMM0901 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.897 |
| clpB1 | PMM1432 | PMM0580 | PMM1432 | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | 0.639 |
| clpB1 | clpP1 | PMM0580 | PMM0742 | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | Clp protease subunit; 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. | 0.882 |
| clpB1 | dnaK | PMM0580 | PMM0897 | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | Molecular chaperone DnaK, heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.861 |
| clpB1 | dnaK2 | PMM0580 | PMM1704 | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | Molecular chaperone DnaK2, heat shock protein hsp70-2; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.858 |
| clpB1 | groEL | PMM0580 | PMM1436 | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | GroEL protein (Chaperonin cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.796 |
| clpB1 | groEL2,cpn60-2 | PMM0580 | PMM0452 | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | GroEL2 protein (Chaperonin cpn60 2); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.689 |
| clpB1 | groES | PMM0580 | PMM1437 | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | GroES protein (Chaperonin cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.885 |
| clpB1 | grpE | PMM0580 | PMM0016 | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | Heat shock protein 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- [...] | 0.921 |
| clpB1 | htpG | PMM0580 | PMM0901 | ATP-dependent Clp protease, Hsp 100, ATP-binding subunit ClpB; 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). B [...] | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.791 |
| clpC | PMM1432 | PMM1088 | PMM1432 | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | 0.638 |
| clpC | clpP1 | PMM1088 | PMM0742 | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | Clp protease subunit; 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. | 0.804 |
| clpC | dnaK | PMM1088 | PMM0897 | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaK, heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.739 |
page 1 of 6