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 |
| PMM1150 | clpB1 | PMM1150 | PMM0580 | Putative thioredoxin reductase; Alternative locus ID: PMED4_13081. | 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 [...] | 0.538 |
| PMM1150 | clpC | PMM1150 | PMM1088 | Putative thioredoxin reductase; Alternative locus ID: PMED4_13081. | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | 0.575 |
| PMM1150 | clpP1 | PMM1150 | PMM0742 | Putative thioredoxin reductase; Alternative locus ID: PMED4_13081. | 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. | 0.568 |
| PMM1150 | clpX | PMM1150 | PMM1657 | Putative thioredoxin reductase; Alternative locus ID: PMED4_13081. | Clp protease ATP-binding subunit, ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.527 |
| PMM1150 | dnaK2 | PMM1150 | PMM1704 | Putative thioredoxin reductase; Alternative locus ID: PMED4_13081. | Molecular chaperone DnaK2, heat shock protein hsp70-2; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.513 |
| PMM1150 | groEL2,cpn60-2 | PMM1150 | PMM0452 | Putative thioredoxin reductase; Alternative locus ID: PMED4_13081. | GroEL2 protein (Chaperonin cpn60 2); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.621 |
| PMM1150 | groES | PMM1150 | PMM1437 | Putative thioredoxin reductase; Alternative locus ID: PMED4_13081. | GroES protein (Chaperonin cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.660 |
| clpB1 | PMM1150 | PMM0580 | PMM1150 | 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 thioredoxin reductase; Alternative locus ID: PMED4_13081. | 0.538 |
| 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 | clpS | PMM0580 | PMM1499 | 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 [...] | Conserved hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.547 |
| 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 | 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 |
| clpC | PMM1150 | PMM1088 | PMM1150 | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | Putative thioredoxin reductase; Alternative locus ID: PMED4_13081. | 0.575 |
| 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 | clpS | PMM1088 | PMM1499 | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | Conserved hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.547 |
| clpC | dnaK2 | PMM1088 | PMM1704 | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | Molecular chaperone DnaK2, heat shock protein hsp70-2; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.653 |
| clpC | groEL2,cpn60-2 | PMM1088 | PMM0452 | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | GroEL2 protein (Chaperonin cpn60 2); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.709 |
| clpC | groES | PMM1088 | PMM1437 | ClpC; Regulatory subunit of ATP-dependent Clp protease; Alternative locus ID: PMED4_12341; Belongs to the ClpA/ClpB family. | GroES protein (Chaperonin cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.516 |
| clpP1 | PMM1150 | PMM0742 | PMM1150 | 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. | Putative thioredoxin reductase; Alternative locus ID: PMED4_13081. | 0.568 |
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