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 |
| CCH85517.1 | CCH85518.1 | MODMU_0045 | MODMU_0046 | Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain; Function of strongly homologous gene; regulator. | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.928 |
| CCH85518.1 | CCH85517.1 | MODMU_0046 | MODMU_0045 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain; Function of strongly homologous gene; regulator. | 0.928 |
| CCH85518.1 | CCH86202.1 | MODMU_0046 | MODMU_0749 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | ATP-dependent Clp protease ATP-binding subunit; Function of strongly homologous gene; enzyme; Belongs to the ClpA/ClpB family. | 0.889 |
| CCH85518.1 | CCH86657.1 | MODMU_0046 | MODMU_1207 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Putative ATP-dependent Clp protease ATP-binding subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.889 |
| CCH85518.1 | CCH87155.1 | MODMU_0046 | MODMU_1716 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Clp domain protein; Function of strongly homologous gene; enzyme. | 0.889 |
| CCH85518.1 | clpB | MODMU_0046 | MODMU_5158 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Protein disaggregation chaperone; 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; Belongs to the ClpA/ClpB family. | 0.889 |
| CCH85518.1 | clpC | MODMU_0046 | MODMU_3615 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Negative regulator of genetic competence ClpC/MecB; Function of strongly homologous gene; regulator; Belongs to the ClpA/ClpB family. | 0.889 |
| CCH85518.1 | dnaJ | MODMU_0046 | MODMU_1760 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.987 |
| CCH85518.1 | dnaJ-2 | MODMU_0046 | MODMU_5177 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | Chaperone protein dnaJ, heat shock protein (Hsp40), co-chaperone with dnaK; 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 [...] | 0.986 |
| CCH85518.1 | grpE | MODMU_0046 | MODMU_5178 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 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. [...] | 0.990 |
| CCH85518.1 | hrcA | MODMU_0046 | MODMU_1759 | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 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. | 0.889 |
| CCH86202.1 | CCH85518.1 | MODMU_0749 | MODMU_0046 | ATP-dependent Clp protease ATP-binding subunit; Function of strongly homologous gene; enzyme; Belongs to the ClpA/ClpB family. | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.889 |
| CCH86202.1 | dnaJ | MODMU_0749 | MODMU_1760 | ATP-dependent Clp protease ATP-binding subunit; Function of strongly homologous gene; enzyme; Belongs to the ClpA/ClpB family. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.599 |
| CCH86202.1 | dnaJ-2 | MODMU_0749 | MODMU_5177 | ATP-dependent Clp protease ATP-binding subunit; Function of strongly homologous gene; enzyme; Belongs to the ClpA/ClpB family. | Chaperone protein dnaJ, heat shock protein (Hsp40), co-chaperone with dnaK; 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 [...] | 0.599 |
| CCH86202.1 | grpE | MODMU_0749 | MODMU_5178 | ATP-dependent Clp protease ATP-binding subunit; Function of strongly homologous gene; enzyme; 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. [...] | 0.852 |
| CCH86202.1 | hrcA | MODMU_0749 | MODMU_1759 | ATP-dependent Clp protease ATP-binding subunit; Function of strongly homologous gene; enzyme; 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. | 0.597 |
| CCH86657.1 | CCH85518.1 | MODMU_1207 | MODMU_0046 | Putative ATP-dependent Clp protease ATP-binding subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Putative heat shock protein Hsp70; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. | 0.889 |
| CCH86657.1 | dnaJ | MODMU_1207 | MODMU_1760 | Putative ATP-dependent Clp protease ATP-binding subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.599 |
| CCH86657.1 | dnaJ-2 | MODMU_1207 | MODMU_5177 | Putative ATP-dependent Clp protease ATP-binding subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Chaperone protein dnaJ, heat shock protein (Hsp40), co-chaperone with dnaK; 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 [...] | 0.599 |
| CCH86657.1 | grpE | MODMU_1207 | MODMU_5178 | Putative ATP-dependent Clp protease ATP-binding subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 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. [...] | 0.821 |
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