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 |
| ECA1220 | dnaJ | ECA1220 | ECA3881 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | 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 [...] | 0.669 |
| ECA1220 | dnaK | ECA1220 | ECA3882 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.484 |
| ECA1220 | groL | ECA1220 | ECA0625 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.603 |
| ECA1220 | groS | ECA1220 | ECA0624 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.504 |
| ECA1220 | grpE | ECA1220 | ECA0842 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | 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 [...] | 0.743 |
| ECA1220 | hslO | ECA1220 | ECA4105 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | Heat shock protein (33 kDa chaperonin); Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.488 |
| ECA1220 | hslU | ECA1220 | ECA4262 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | ATP-dependent Hsl protease ATP-binding subunit (heat shock protein); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.823 |
| ECA1220 | hslV | ECA1220 | ECA4261 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | ATP-dependent protease (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.824 |
| ECA1220 | htpG | ECA1220 | ECA1179 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | Chaperone protein; Molecular chaperone. Has ATPase activity. | 0.688 |
| ECA1220 | lon | ECA1220 | ECA1150 | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | ATP-dependent protease la; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.569 |
| dnaJ | ECA1220 | ECA3881 | ECA1220 | 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 [...] | Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa. | 0.669 |
| dnaJ | dnaK | ECA3881 | ECA3882 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groL | ECA3881 | ECA0625 | 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 [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.949 |
| dnaJ | groS | ECA3881 | ECA0624 | 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 [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.763 |
| dnaJ | grpE | ECA3881 | ECA0842 | 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; 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 [...] | 0.991 |
| dnaJ | hslO | ECA3881 | ECA4105 | 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 (33 kDa chaperonin); Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.659 |
| dnaJ | hslU | ECA3881 | ECA4262 | 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 [...] | ATP-dependent Hsl protease ATP-binding subunit (heat shock protein); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.873 |
| dnaJ | hslV | ECA3881 | ECA4261 | 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 [...] | ATP-dependent protease (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.859 |
| dnaJ | htpG | ECA3881 | ECA1179 | 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 [...] | Chaperone protein; Molecular chaperone. Has ATPase activity. | 0.984 |
| dnaJ | lon | ECA3881 | ECA1150 | 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 [...] | ATP-dependent protease la; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.870 |
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