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 |
| EFL41155.1 | dnaJ | SSRG_03959 | SSRG_03024 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 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, DnaK and [...] | 0.630 |
| EFL41155.1 | dnaJ-2 | SSRG_03959 | SSRG_04227 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 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, DnaK and [...] | 0.630 |
| EFL41155.1 | dnaK | SSRG_03959 | SSRG_00795 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.902 |
| EFL41155.1 | dnaK-2 | SSRG_03959 | SSRG_03026 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.902 |
| EFL41155.1 | groL | SSRG_03959 | SSRG_02447 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.990 |
| EFL41155.1 | groL-2 | SSRG_03959 | SSRG_03503 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.990 |
| EFL41155.1 | grpE | SSRG_03959 | SSRG_03025 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | GrpE (HSP-70 cofactor); 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-d [...] | 0.921 |
| EFL41155.1 | htpG | SSRG_03959 | SSRG_05930 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.867 |
| EFL41155.1 | tig | SSRG_03959 | SSRG_04164 | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Trigger factor tig; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.412 |
| dnaJ | EFL41155.1 | SSRG_03024 | SSRG_03959 | 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, DnaK and [...] | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.630 |
| dnaJ | dnaK | SSRG_03024 | SSRG_00795 | 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, DnaK and [...] | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| dnaJ | dnaK-2 | SSRG_03024 | SSRG_03026 | 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, DnaK and [...] | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groL | SSRG_03024 | SSRG_02447 | 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, DnaK and [...] | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.964 |
| dnaJ | groL-2 | SSRG_03024 | SSRG_03503 | 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, DnaK and [...] | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.965 |
| dnaJ | groS | SSRG_03024 | SSRG_02448 | 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, DnaK and [...] | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.865 |
| dnaJ | grpE | SSRG_03024 | SSRG_03025 | 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, DnaK and [...] | GrpE (HSP-70 cofactor); 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-d [...] | 0.999 |
| dnaJ | htpG | SSRG_03024 | SSRG_05930 | 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, DnaK and [...] | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.993 |
| dnaJ | tig | SSRG_03024 | SSRG_04164 | 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, DnaK and [...] | Trigger factor tig; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.594 |
| dnaJ-2 | EFL41155.1 | SSRG_04227 | SSRG_03959 | 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, DnaK and [...] | Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.630 |
| dnaJ-2 | dnaK | SSRG_04227 | SSRG_00795 | 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, DnaK and [...] | Chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
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