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 |
| SDK67354.1 | SDK70945.1 | SAMN05216298_1097 | SAMN05216298_1287 | Clp amino terminal domain-containing protein, pathogenicity island component. | Molecular chaperone HtpG. | 0.766 |
| SDK67354.1 | SDK85177.1 | SAMN05216298_1097 | SAMN05216298_1663 | Clp amino terminal domain-containing protein, pathogenicity island component. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.746 |
| SDK67354.1 | SDK85237.1 | SAMN05216298_1097 | SAMN05216298_1666 | Clp amino terminal domain-containing protein, pathogenicity island component. | DnaJ domain-containing protein. | 0.634 |
| SDK67354.1 | SDL36184.1 | SAMN05216298_1097 | SAMN05216298_3609 | Clp amino terminal domain-containing protein, pathogenicity island component. | Hsp70 protein. | 0.799 |
| SDK67354.1 | dnaJ | SAMN05216298_1097 | SAMN05216298_2662 | Clp amino terminal domain-containing protein, pathogenicity island component. | Molecular chaperone 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, [...] | 0.693 |
| SDK67354.1 | dnaJ-2 | SAMN05216298_1097 | SAMN05216298_4322 | Clp amino terminal domain-containing protein, pathogenicity island component. | Molecular chaperone 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, [...] | 0.693 |
| SDK67354.1 | grpE | SAMN05216298_1097 | SAMN05216298_2663 | Clp amino terminal domain-containing protein, pathogenicity island component. | 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. [...] | 0.882 |
| SDK70945.1 | SDK67354.1 | SAMN05216298_1287 | SAMN05216298_1097 | Molecular chaperone HtpG. | Clp amino terminal domain-containing protein, pathogenicity island component. | 0.766 |
| SDK70945.1 | SDK84596.1 | SAMN05216298_1287 | SAMN05216298_1638 | Molecular chaperone HtpG. | Peptidylprolyl isomerase. | 0.991 |
| SDK70945.1 | SDK85177.1 | SAMN05216298_1287 | SAMN05216298_1663 | Molecular chaperone HtpG. | GrpE 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. Several rounds of ATP-dependent i [...] | 0.800 |
| SDK70945.1 | SDK85237.1 | SAMN05216298_1287 | SAMN05216298_1666 | Molecular chaperone HtpG. | DnaJ domain-containing protein. | 0.939 |
| SDK70945.1 | SDL34556.1 | SAMN05216298_1287 | SAMN05216298_3530 | Molecular chaperone HtpG. | ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family. | 0.766 |
| SDK70945.1 | SDL36184.1 | SAMN05216298_1287 | SAMN05216298_3609 | Molecular chaperone HtpG. | Hsp70 protein. | 0.972 |
| SDK70945.1 | clpB | SAMN05216298_1287 | SAMN05216298_3413 | Molecular chaperone HtpG. | ATP-dependent Clp protease 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; Belongs to the ClpA/ClpB family. | 0.766 |
| SDK70945.1 | dnaJ | SAMN05216298_1287 | SAMN05216298_2662 | Molecular chaperone HtpG. | Molecular chaperone 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, [...] | 0.957 |
| SDK70945.1 | dnaJ-2 | SAMN05216298_1287 | SAMN05216298_4322 | Molecular chaperone HtpG. | Molecular chaperone 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, [...] | 0.957 |
| SDK70945.1 | grpE | SAMN05216298_1287 | SAMN05216298_2663 | Molecular chaperone HtpG. | 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. [...] | 0.824 |
| SDK84596.1 | SDK70945.1 | SAMN05216298_1638 | SAMN05216298_1287 | Peptidylprolyl isomerase. | Molecular chaperone HtpG. | 0.991 |
| SDK84596.1 | SDL36184.1 | SAMN05216298_1638 | SAMN05216298_3609 | Peptidylprolyl isomerase. | Hsp70 protein. | 0.808 |
| SDK85177.1 | SDK67354.1 | SAMN05216298_1663 | SAMN05216298_1097 | GrpE 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. Several rounds of ATP-dependent i [...] | Clp amino terminal domain-containing protein, pathogenicity island component. | 0.746 |
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