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 |
| ECA1820 | dnaJ | ECA1820 | ECA3881 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 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 [...] | 0.955 |
| ECA1820 | groL | ECA1820 | ECA0625 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.817 |
| ECA1820 | groS | ECA1820 | ECA0624 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.768 |
| ECA1820 | hslV | ECA1820 | ECA4261 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | ATP-dependent protease (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.465 |
| ECA1820 | htpG | ECA1820 | ECA1179 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | Chaperone protein; Molecular chaperone. Has ATPase activity. | 0.942 |
| ECA1820 | sseB | ECA1820 | ECA3229 | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | Enhanced serine sensitivity protein; Similar to Escherichia coli, and Shigella flexneri protein SseB or b2522 or sf2569 SWALL:SSEB_ECOLI (SWALL:P31143) (258 aa) fasta scores: E(): 1.6e-51, 55.11% id in 254 aa. | 0.542 |
| dnaJ | ECA1820 | ECA3881 | ECA1820 | 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 [...] | Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa. | 0.955 |
| 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 | hscA | ECA3881 | ECA3233 | 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; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. | 0.984 |
| 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 | ppiA | ECA3881 | ECA4071 | 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 [...] | Peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.735 |
| dnaJ | ppiB | ECA3881 | ECA3154 | 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 [...] | Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.735 |
| dnaJ | sseB | ECA3881 | ECA3229 | 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 [...] | Enhanced serine sensitivity protein; Similar to Escherichia coli, and Shigella flexneri protein SseB or b2522 or sf2569 SWALL:SSEB_ECOLI (SWALL:P31143) (258 aa) fasta scores: E(): 1.6e-51, 55.11% id in 254 aa. | 0.639 |
| dnaK | dnaJ | ECA3882 | ECA3881 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 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 [...] | 0.999 |
| dnaK | groL | ECA3882 | ECA0625 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.973 |
| dnaK | groS | ECA3882 | ECA0624 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.891 |
| dnaK | hscA | ECA3882 | ECA3233 | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. | 0.548 |
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