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 |
| ANP64709.1 | ANP64710.1 | BAU10_06800 | BAU10_06805 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 0.707 |
| ANP64709.1 | dnaJ | BAU10_06800 | BAU10_02310 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone 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, [...] | 0.947 |
| ANP64709.1 | groEL | BAU10_06800 | BAU10_14150 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.758 |
| ANP64709.1 | groEL-2 | BAU10_06800 | BAU10_16875 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.758 |
| ANP64709.1 | grpE | BAU10_06800 | BAU10_02295 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Nucleotide exchange factor GrpE; 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 [...] | 0.934 |
| ANP64709.1 | hslU | BAU10_06800 | BAU10_00280 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase ATPase subunit; 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. | 0.660 |
| ANP64709.1 | hslV | BAU10_06800 | BAU10_00285 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.633 |
| ANP64709.1 | htpG | BAU10_06800 | BAU10_03165 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.952 |
| ANP64710.1 | ANP64709.1 | BAU10_06805 | BAU10_06800 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.707 |
| ANP64710.1 | dnaJ | BAU10_06805 | BAU10_02310 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Molecular chaperone 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, [...] | 0.947 |
| ANP64710.1 | groEL | BAU10_06805 | BAU10_14150 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.758 |
| ANP64710.1 | groEL-2 | BAU10_06805 | BAU10_16875 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.758 |
| ANP64710.1 | grpE | BAU10_06805 | BAU10_02295 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Nucleotide exchange factor GrpE; 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 [...] | 0.934 |
| ANP64710.1 | hslU | BAU10_06805 | BAU10_00280 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | HslU--HslV peptidase ATPase subunit; 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. | 0.660 |
| ANP64710.1 | hslV | BAU10_06805 | BAU10_00285 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.633 |
| ANP64710.1 | htpG | BAU10_06805 | BAU10_03165 | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.952 |
| dnaJ | ANP64709.1 | BAU10_02310 | BAU10_06800 | Molecular chaperone 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, [...] | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.947 |
| dnaJ | ANP64710.1 | BAU10_02310 | BAU10_06805 | Molecular chaperone 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, [...] | Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. | 0.947 |
| dnaJ | dnaK | BAU10_02310 | BAU10_02305 | Molecular chaperone 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, [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groEL | BAU10_02310 | BAU10_14150 | Molecular chaperone 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, [...] | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.961 |
page 1 of 5