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 |
| cysH | trxA | HMPREF0758_0450 | HMPREF0758_1508 | Phosphoadenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. Belongs to the PAPS reductase family. CysH subfamily. | Thioredoxin; COG: COG0526; Pfam: PF00085; InterPro: IPR012335; Belongs to the thioredoxin family. | 0.638 |
| dnaJ | dnaK | HMPREF0758_0580 | HMPREF0758_0581 | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.996 |
| dnaJ | groS | HMPREF0758_0580 | HMPREF0758_0891 | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.796 |
| dnaJ | grpE | HMPREF0758_0580 | HMPREF0758_2441 | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | Co-chaperone 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-depend [...] | 0.962 |
| dnaJ | hslU | HMPREF0758_0580 | HMPREF0758_1169 | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | ATP-dependent protease HslVU, ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.907 |
| dnaJ | trxA | HMPREF0758_0580 | HMPREF0758_1508 | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | Thioredoxin; COG: COG0526; Pfam: PF00085; InterPro: IPR012335; Belongs to the thioredoxin family. | 0.569 |
| dnaJ | trxB | HMPREF0758_0580 | HMPREF0758_4452 | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | Thioredoxin-disulfide reductase; COG: COG0492; Pfam: PF07992,PF00070; InterPro: IPR005982. | 0.443 |
| dnaK | dnaJ | HMPREF0758_0581 | HMPREF0758_0580 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | 0.996 |
| dnaK | groS | HMPREF0758_0581 | HMPREF0758_0891 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.890 |
| dnaK | grpE | HMPREF0758_0581 | HMPREF0758_2441 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Co-chaperone 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-depend [...] | 0.975 |
| dnaK | hslU | HMPREF0758_0581 | HMPREF0758_1169 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent protease HslVU, ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.724 |
| dnaK | trxA | HMPREF0758_0581 | HMPREF0758_1508 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Thioredoxin; COG: COG0526; Pfam: PF00085; InterPro: IPR012335; Belongs to the thioredoxin family. | 0.566 |
| fur | trxA | HMPREF0758_4880 | HMPREF0758_1508 | Transcriptional regulator, Fur family; COG: COG0735; Pfam: PF01475; InterPro: IPR002481; Belongs to the Fur family. | Thioredoxin; COG: COG0526; Pfam: PF00085; InterPro: IPR012335; Belongs to the thioredoxin family. | 0.538 |
| gor | trxA | HMPREF0758_1103 | HMPREF0758_1508 | Glutathione-disulfide reductase; COG: COG1249; Pfam: PF07992,PF00070,PF02852; InterPro: IPR006322. | Thioredoxin; COG: COG0526; Pfam: PF00085; InterPro: IPR012335; Belongs to the thioredoxin family. | 0.565 |
| gor | trxB | HMPREF0758_1103 | HMPREF0758_4452 | Glutathione-disulfide reductase; COG: COG1249; Pfam: PF07992,PF00070,PF02852; InterPro: IPR006322. | Thioredoxin-disulfide reductase; COG: COG0492; Pfam: PF07992,PF00070; InterPro: IPR005982. | 0.512 |
| groS | dnaJ | HMPREF0758_0891 | HMPREF0758_0580 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Chaperone protein DnaJ; 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 interactions between DnaJ, D [...] | 0.796 |
| groS | dnaK | HMPREF0758_0891 | HMPREF0758_0581 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.890 |
| groS | grpE | HMPREF0758_0891 | HMPREF0758_2441 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Co-chaperone 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-depend [...] | 0.961 |
| groS | hslU | HMPREF0758_0891 | HMPREF0758_1169 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | ATP-dependent protease HslVU, ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.852 |
| groS | trxA | HMPREF0758_0891 | HMPREF0758_1508 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | Thioredoxin; COG: COG0526; Pfam: PF00085; InterPro: IPR012335; Belongs to the thioredoxin family. | 0.526 |
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