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 |
| Swoo_0124 | Swoo_1797 | Swoo_0124 | Swoo_1797 | PFAM: peptidase M3A and M3B thimet/oligopeptidase F; KEGG: sse:Ssed_0145 oligopeptidase A. | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 0.526 |
| Swoo_0124 | dnaJ | Swoo_0124 | Swoo_3582 | PFAM: peptidase M3A and M3B thimet/oligopeptidase F; KEGG: sse:Ssed_0145 oligopeptidase A. | 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 [...] | 0.483 |
| Swoo_0124 | hslV | Swoo_0124 | Swoo_4429 | PFAM: peptidase M3A and M3B thimet/oligopeptidase F; KEGG: sse:Ssed_0145 oligopeptidase A. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.453 |
| Swoo_0124 | htpG | Swoo_0124 | Swoo_1796 | PFAM: peptidase M3A and M3B thimet/oligopeptidase F; KEGG: sse:Ssed_0145 oligopeptidase A. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.498 |
| Swoo_1797 | Swoo_0124 | Swoo_1797 | Swoo_0124 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | PFAM: peptidase M3A and M3B thimet/oligopeptidase F; KEGG: sse:Ssed_0145 oligopeptidase A. | 0.526 |
| Swoo_1797 | dnaJ | Swoo_1797 | Swoo_3582 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain 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 [...] | 0.680 |
| Swoo_1797 | hslV | Swoo_1797 | Swoo_4429 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.897 |
| Swoo_1797 | htpG | Swoo_1797 | Swoo_1796 | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.905 |
| dnaJ | Swoo_0124 | Swoo_3582 | Swoo_0124 | 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 [...] | PFAM: peptidase M3A and M3B thimet/oligopeptidase F; KEGG: sse:Ssed_0145 oligopeptidase A. | 0.483 |
| dnaJ | Swoo_1797 | Swoo_3582 | Swoo_1797 | 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 [...] | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 0.680 |
| dnaJ | hslV | Swoo_3582 | Swoo_4429 | 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 [...] | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.868 |
| dnaJ | htpG | Swoo_3582 | Swoo_1796 | 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 [...] | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.963 |
| hslV | Swoo_0124 | Swoo_4429 | Swoo_0124 | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | PFAM: peptidase M3A and M3B thimet/oligopeptidase F; KEGG: sse:Ssed_0145 oligopeptidase A. | 0.453 |
| hslV | Swoo_1797 | Swoo_4429 | Swoo_1797 | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 0.897 |
| hslV | dnaJ | Swoo_4429 | Swoo_3582 | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 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 [...] | 0.868 |
| hslV | htpG | Swoo_4429 | Swoo_1796 | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.887 |
| htpG | Swoo_0124 | Swoo_1796 | Swoo_0124 | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | PFAM: peptidase M3A and M3B thimet/oligopeptidase F; KEGG: sse:Ssed_0145 oligopeptidase A. | 0.498 |
| htpG | Swoo_1797 | Swoo_1796 | Swoo_1797 | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | PFAM: Thioredoxin domain; KEGG: sse:Ssed_2848 thioredoxin domain protein. | 0.905 |
| htpG | dnaJ | Swoo_1796 | Swoo_3582 | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 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 [...] | 0.963 |
| htpG | hslV | Swoo_1796 | Swoo_4429 | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.887 |