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 |
| FAES_1507 | dnaJ | FAES_1507 | FAES_3094 | Cysteine desulfurase. | 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 [...] | 0.566 |
| FAES_1507 | hslU | FAES_1507 | FAES_4766 | Cysteine desulfurase. | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.607 |
| FAES_1507 | hslV | FAES_1507 | FAES_2089 | Cysteine desulfurase. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.497 |
| FAES_1873 | FAES_2819 | FAES_1873 | FAES_2819 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Chaperonin Cpn10. | 0.798 |
| FAES_1873 | FAES_5292 | FAES_1873 | FAES_5292 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Chaperone DnaJ domain protein. | 0.971 |
| FAES_1873 | dnaJ | FAES_1873 | FAES_3094 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 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 [...] | 0.971 |
| FAES_1873 | groL | FAES_1873 | FAES_2231 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.952 |
| FAES_1873 | groS | FAES_1873 | FAES_2230 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.800 |
| FAES_1873 | grpE | FAES_1873 | FAES_3095 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | GrpE 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-dependent i [...] | 0.850 |
| FAES_1873 | hslU | FAES_1873 | FAES_4766 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.862 |
| FAES_1873 | hslV | FAES_1873 | FAES_2089 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.880 |
| FAES_1873 | lon | FAES_1873 | FAES_5413 | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 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. | 0.807 |
| FAES_2819 | FAES_1873 | FAES_2819 | FAES_1873 | Chaperonin Cpn10. | ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity. | 0.798 |
| FAES_2819 | FAES_5292 | FAES_2819 | FAES_5292 | Chaperonin Cpn10. | Chaperone DnaJ domain protein. | 0.599 |
| FAES_2819 | dnaJ | FAES_2819 | FAES_3094 | Chaperonin Cpn10. | 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 [...] | 0.599 |
| FAES_2819 | groL | FAES_2819 | FAES_2231 | Chaperonin Cpn10. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.981 |
| FAES_2819 | grpE | FAES_2819 | FAES_3095 | Chaperonin Cpn10. | GrpE 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-dependent i [...] | 0.858 |
| FAES_2819 | hslU | FAES_2819 | FAES_4766 | Chaperonin Cpn10. | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.784 |
| FAES_2819 | hslV | FAES_2819 | FAES_2089 | Chaperonin Cpn10. | 20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.770 |
| FAES_2819 | lon | FAES_2819 | FAES_5413 | Chaperonin Cpn10. | 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. | 0.431 |
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