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 |
| SAL13360.1 | SAL43183.1 | AWB69_00481 | AWB69_04365 | Thioredoxin. | ATPase central domain-containing protein. | 0.625 |
| SAL13360.1 | SAL45872.1 | AWB69_00481 | AWB69_04618 | Thioredoxin. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.823 |
| SAL13360.1 | dnaJ | AWB69_00481 | AWB69_08856 | Thioredoxin. | 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 [...] | 0.872 |
| SAL13360.1 | groL | AWB69_00481 | AWB69_00531 | Thioredoxin. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.823 |
| SAL13360.1 | groS | AWB69_00481 | AWB69_00530 | Thioredoxin. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.678 |
| SAL13360.1 | grpE | AWB69_00481 | AWB69_07596 | Thioredoxin. | 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- [...] | 0.908 |
| SAL13360.1 | hslU | AWB69_00481 | AWB69_00801 | Thioredoxin. | ATP-dependent protease ATP-binding subunit HslU; 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. | 0.922 |
| SAL13360.1 | hslV | AWB69_00481 | AWB69_00800 | Thioredoxin. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.915 |
| SAL13360.1 | htpG | AWB69_00481 | AWB69_06742 | Thioredoxin. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.895 |
| SAL43183.1 | SAL13360.1 | AWB69_04365 | AWB69_00481 | ATPase central domain-containing protein. | Thioredoxin. | 0.625 |
| SAL43183.1 | SAL45872.1 | AWB69_04365 | AWB69_04618 | ATPase central domain-containing protein. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.755 |
| SAL43183.1 | clpX | AWB69_04365 | AWB69_08992 | ATPase central domain-containing protein. | ATP-dependent 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. | 0.699 |
| SAL43183.1 | dnaJ | AWB69_04365 | AWB69_08856 | ATPase central domain-containing protein. | 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 [...] | 0.867 |
| SAL43183.1 | groL | AWB69_04365 | AWB69_00531 | ATPase central domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.755 |
| SAL43183.1 | groS | AWB69_04365 | AWB69_00530 | ATPase central domain-containing protein. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.609 |
| SAL43183.1 | grpE | AWB69_04365 | AWB69_07596 | ATPase central domain-containing protein. | 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- [...] | 0.869 |
| SAL43183.1 | hslU | AWB69_04365 | AWB69_00801 | ATPase central domain-containing protein. | ATP-dependent protease ATP-binding subunit HslU; 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. | 0.870 |
| SAL43183.1 | hslV | AWB69_04365 | AWB69_00800 | ATPase central domain-containing protein. | ATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.850 |
| SAL43183.1 | htpG | AWB69_04365 | AWB69_06742 | ATPase central domain-containing protein. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.861 |
| SAL45872.1 | SAL13360.1 | AWB69_04618 | AWB69_00481 | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Thioredoxin. | 0.823 |
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