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 |
| dnaJ | fdx | DR97_2104 | DR97_4060 | 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 are require [...] | Ferredoxin, 2fe-2s type, isc system; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions | 0.504 |
| dnaJ | groL | DR97_2104 | DR97_1563 | 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 are require [...] | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 0.981 |
| dnaJ | grpE | DR97_2104 | DR97_2106 | 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 are require [...] | 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 interactions be [...] | 0.997 |
| dnaJ | hscA | DR97_2104 | DR97_4059 | 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 are require [...] | Fe-s protein assembly chaperone hsca; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (By similarity) | 0.978 |
| dnaJ | hscB | DR97_2104 | DR97_4058 | 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 are require [...] | Fe-s protein assembly co-chaperone hscb; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA | 0.628 |
| dnaJ | nifU | DR97_2104 | DR97_4056 | 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 are require [...] | Nitrogen fixation protein nifu and related proteins; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters | 0.560 |
| fdx | dnaJ | DR97_4060 | DR97_2104 | Ferredoxin, 2fe-2s type, isc system; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions | 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 are require [...] | 0.504 |
| fdx | hscA | DR97_4060 | DR97_4059 | Ferredoxin, 2fe-2s type, isc system; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions | Fe-s protein assembly chaperone hsca; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (By similarity) | 0.999 |
| fdx | hscB | DR97_4060 | DR97_4058 | Ferredoxin, 2fe-2s type, isc system; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions | Fe-s protein assembly co-chaperone hscb; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA | 0.998 |
| fdx | iscA | DR97_4060 | DR97_4057 | Ferredoxin, 2fe-2s type, isc system; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions | Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system | 0.948 |
| fdx | iscR | DR97_4060 | DR97_4054 | Ferredoxin, 2fe-2s type, isc system; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions | Rrf2 family transcriptional regulator, iron-sulfur cluster assembly transcription factor; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins | 0.967 |
| fdx | iscS | DR97_4060 | DR97_4055 | Ferredoxin, 2fe-2s type, isc system; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions | Cysteine desulfurase iscs; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins | 0.991 |
| fdx | iscX | DR97_4060 | DR97_4061 | Ferredoxin, 2fe-2s type, isc system; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions | Fes assembly protein iscx; To E.coli YfhJ | 0.999 |
| fdx | nifU | DR97_4060 | DR97_4056 | Ferredoxin, 2fe-2s type, isc system; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions | Nitrogen fixation protein nifu and related proteins; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters | 0.997 |
| groL | dnaJ | DR97_1563 | DR97_2104 | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 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 are require [...] | 0.981 |
| groL | grpE | DR97_1563 | DR97_2106 | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 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 interactions be [...] | 0.996 |
| groL | hscA | DR97_1563 | DR97_4059 | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | Fe-s protein assembly chaperone hsca; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (By similarity) | 0.963 |
| groL | hscB | DR97_1563 | DR97_4058 | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | Fe-s protein assembly co-chaperone hscb; Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA | 0.692 |
| grpE | dnaJ | DR97_2106 | DR97_2104 | 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 interactions be [...] | 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 are require [...] | 0.997 |
| grpE | groL | DR97_2106 | DR97_1563 | 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 interactions be [...] | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 0.996 |
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