Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... 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 annotated functions of the network proteins
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ABF64812.1 | ABF64813.1 | TM1040_2080 | TM1040_2081 | annotation not available | annotation not available | 0.676 |
| ABF64812.1 | ABF65663.1 | TM1040_2080 | TM1040_2931 | annotation not available | annotation not available | 0.574 |
| ABF64813.1 | ABF64812.1 | TM1040_2081 | TM1040_2080 | annotation not available | annotation not available | 0.676 |
| ABF64813.1 | ABF64814.1 | TM1040_2081 | TM1040_2082 | annotation not available | annotation not available | 0.641 |
| ABF64813.1 | ABF65346.1 | TM1040_2081 | TM1040_2614 | annotation not available | annotation not available | 0.609 |
| ABF64813.1 | ABF65663.1 | TM1040_2081 | TM1040_2931 | annotation not available | annotation not available | 0.776 |
| ABF64813.1 | dnaJ | TM1040_2081 | TM1040_0009 | annotation not available | 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 [...] | 0.457 |
| ABF64814.1 | ABF64813.1 | TM1040_2082 | TM1040_2081 | annotation not available | annotation not available | 0.641 |
| ABF65346.1 | ABF64813.1 | TM1040_2614 | TM1040_2081 | annotation not available | annotation not available | 0.609 |
| ABF65346.1 | dnaJ | TM1040_2614 | TM1040_0009 | annotation not available | 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 [...] | 0.457 |
| ABF65663.1 | ABF64812.1 | TM1040_2931 | TM1040_2080 | annotation not available | annotation not available | 0.574 |
| ABF65663.1 | ABF64813.1 | TM1040_2931 | TM1040_2081 | annotation not available | annotation not available | 0.776 |
| ABF65663.1 | dnaJ | TM1040_2931 | TM1040_0009 | annotation not available | 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 [...] | 0.457 |
| dnaJ | ABF64813.1 | TM1040_0009 | TM1040_2081 | 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 [...] | annotation not available | 0.457 |
| dnaJ | ABF65346.1 | TM1040_0009 | TM1040_2614 | 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 [...] | annotation not available | 0.457 |
| dnaJ | ABF65663.1 | TM1040_0009 | TM1040_2931 | 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 [...] | annotation not available | 0.457 |
