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 |
| ABI61528.1 | dnaK | GbCGDNIH1_0630 | GbCGDNIH1_0022 | Molecular chaperones (DnaJ family). | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.970 |
| ABI61528.1 | groL | GbCGDNIH1_0630 | GbCGDNIH1_2180 | Molecular chaperones (DnaJ family). | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.649 |
| ABI61528.1 | htpG | GbCGDNIH1_0630 | GbCGDNIH1_0315 | Molecular chaperones (DnaJ family). | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.891 |
| ABI62359.1 | dnaK | GbCGDNIH1_1461 | GbCGDNIH1_0022 | Curved DNA-binding protein. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.995 |
| ABI62359.1 | groL | GbCGDNIH1_1461 | GbCGDNIH1_2180 | Curved DNA-binding protein. | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.797 |
| ABI62359.1 | htpG | GbCGDNIH1_1461 | GbCGDNIH1_0315 | Curved DNA-binding protein. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.891 |
| ABI63167.1 | dnaJ | GbCGDNIH1_2269 | GbCGDNIH1_0021 | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 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 [...] | 0.489 |
| ABI63167.1 | dnaK | GbCGDNIH1_2269 | GbCGDNIH1_0022 | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.415 |
| ABI63167.1 | groL | GbCGDNIH1_2269 | GbCGDNIH1_2180 | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.451 |
| ABI63167.1 | htpG | GbCGDNIH1_2269 | GbCGDNIH1_0315 | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.482 |
| clpX | dnaK | GbCGDNIH1_1306 | GbCGDNIH1_0022 | ATP-dependent endopeptidase clp 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. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.415 |
| clpX | groL | GbCGDNIH1_1306 | GbCGDNIH1_2180 | ATP-dependent endopeptidase clp 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. | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.488 |
| clpX | htpG | GbCGDNIH1_1306 | GbCGDNIH1_0315 | ATP-dependent endopeptidase clp 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. | Chaperone protein htpG; Molecular chaperone. Has ATPase activity. | 0.417 |
| dnaJ | ABI63167.1 | GbCGDNIH1_0021 | GbCGDNIH1_2269 | 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 [...] | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.489 |
| dnaJ | dnaK | GbCGDNIH1_0021 | GbCGDNIH1_0022 | 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. | 0.999 |
| dnaJ | groL | GbCGDNIH1_0021 | GbCGDNIH1_2180 | 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 [...] | 60 kDa chaperonin GROEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.910 |
| dnaJ | htpG | GbCGDNIH1_0021 | GbCGDNIH1_0315 | 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 htpG; Molecular chaperone. Has ATPase activity. | 0.960 |
| dnaK | ABI61528.1 | GbCGDNIH1_0022 | GbCGDNIH1_0630 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Molecular chaperones (DnaJ family). | 0.970 |
| dnaK | ABI62359.1 | GbCGDNIH1_0022 | GbCGDNIH1_1461 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Curved DNA-binding protein. | 0.995 |
| dnaK | ABI63167.1 | GbCGDNIH1_0022 | GbCGDNIH1_2269 | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. | 0.415 |
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