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 |
| clpB | dnaJ | ECIAI1_2715 | ECIAI1_0015 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 0.968 |
| clpB | dnaK | ECIAI1_2715 | ECIAI1_0014 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Chaperone Hsp70, co-chaperone with DnaJ; Function experimentally demonstrated in the studied species; factor. | 0.999 |
| clpB | groL | ECIAI1_2715 | ECIAI1_4376 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.963 |
| clpB | groS | ECIAI1_2715 | ECIAI1_4375 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.925 |
| clpB | grpE | ECIAI1_2715 | ECIAI1_2735 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | 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. Several rounds of ATP-depen [...] | 0.975 |
| clpB | hscA | ECIAI1_2715 | ECIAI1_2578 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | DnaK-like molecular chaperone specific for IscU; Function experimentally demonstrated in the studied species; factor. | 0.732 |
| clpB | hscC | ECIAI1_2715 | ECIAI1_0634 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Hsp70 family chaperone Hsc62, binds to RpoD and inhibits transcription; Function experimentally demonstrated in the studied species; factor. | 0.824 |
| clpB | htpG | ECIAI1_2715 | ECIAI1_0476 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity. | 0.980 |
| clpB | rpoH | ECIAI1_2715 | ECIAI1_3607 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | RNA polymerase, sigma 32 (sigma H) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.415 |
| dnaJ | clpB | ECIAI1_0015 | ECIAI1_2715 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | 0.968 |
| dnaJ | dnaK | ECIAI1_0015 | ECIAI1_0014 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Chaperone Hsp70, co-chaperone with DnaJ; Function experimentally demonstrated in the studied species; factor. | 0.999 |
| dnaJ | groL | ECIAI1_0015 | ECIAI1_4376 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.966 |
| dnaJ | groS | ECIAI1_0015 | ECIAI1_4375 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.959 |
| dnaJ | grpE | ECIAI1_0015 | ECIAI1_2735 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | 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. Several rounds of ATP-depen [...] | 0.999 |
| dnaJ | hscA | ECIAI1_0015 | ECIAI1_2578 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | DnaK-like molecular chaperone specific for IscU; Function experimentally demonstrated in the studied species; factor. | 0.976 |
| dnaJ | hscC | ECIAI1_0015 | ECIAI1_0634 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Hsp70 family chaperone Hsc62, binds to RpoD and inhibits transcription; Function experimentally demonstrated in the studied species; factor. | 0.967 |
| dnaJ | htpG | ECIAI1_0015 | ECIAI1_0476 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity. | 0.980 |
| dnaJ | rpoH | ECIAI1_0015 | ECIAI1_3607 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | RNA polymerase, sigma 32 (sigma H) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.918 |
| dnaJ | ydbK | ECIAI1_0015 | ECIAI1_1377 | Chaperone Hsp40, co-chaperone with DnaK; 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 interaction [...] | Putative 2-oxoacid-flavodoxin fused oxidoreductase:conserved protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.915 |
| dnaK | clpB | ECIAI1_0014 | ECIAI1_2715 | Chaperone Hsp70, co-chaperone with DnaJ; Function experimentally demonstrated in the studied species; factor. | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | 0.999 |
page 1 of 5