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 |
| AMQ41191.1 | dnaJ | AMS64_01655 | AMS64_16495 | Chaperone; 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, [...] | 0.919 |
| AMQ41191.1 | groEL | AMS64_01655 | AMS64_19780 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.933 |
| AMQ41191.1 | groES | AMS64_01655 | AMS64_19785 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.871 |
| AMQ41191.1 | grpE | AMS64_01655 | AMS64_16505 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone 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 of ATP [...] | 0.957 |
| AMQ41191.1 | htpG | AMS64_01655 | AMS64_07940 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.962 |
| AMQ41191.1 | hycE | AMS64_01655 | AMS64_10260 | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hydrogenase 3 large subunit; Formate hydrogenlyase subunit 5; HycBCDEFG is part of the formate hydrogenlyase system which is involved in the cleaving of formate to dihydrogen and carbon dioxide; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.444 |
| AMQ42087.1 | dnaJ | AMS64_06685 | AMS64_16495 | Molecular chaperone HscC; 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, [...] | 0.987 |
| AMQ42087.1 | groEL | AMS64_06685 | AMS64_19780 | Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.940 |
| AMQ42087.1 | groES | AMS64_06685 | AMS64_19785 | Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.864 |
| AMQ42087.1 | grpE | AMS64_06685 | AMS64_16505 | Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone 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 of ATP [...] | 0.969 |
| AMQ42087.1 | htpG | AMS64_06685 | AMS64_07940 | Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.966 |
| AMQ42087.1 | hycE | AMS64_06685 | AMS64_10260 | Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hydrogenase 3 large subunit; Formate hydrogenlyase subunit 5; HycBCDEFG is part of the formate hydrogenlyase system which is involved in the cleaving of formate to dihydrogen and carbon dioxide; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.444 |
| AMQ45065.1 | dnaJ | AMS64_13430 | AMS64_16495 | StbA family protein; 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, [...] | 0.882 |
| AMQ45065.1 | groEL | AMS64_13430 | AMS64_19780 | StbA family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.918 |
| AMQ45065.1 | groES | AMS64_13430 | AMS64_19785 | StbA family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.843 |
| AMQ45065.1 | grpE | AMS64_13430 | AMS64_16505 | StbA family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone 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 of ATP [...] | 0.941 |
| AMQ45065.1 | htpG | AMS64_13430 | AMS64_07940 | StbA family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.958 |
| AMQ45065.1 | hycE | AMS64_13430 | AMS64_10260 | StbA family protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hydrogenase 3 large subunit; Formate hydrogenlyase subunit 5; HycBCDEFG is part of the formate hydrogenlyase system which is involved in the cleaving of formate to dihydrogen and carbon dioxide; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.444 |
| dnaJ | AMQ41191.1 | AMS64_16495 | AMS64_01655 | 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, [...] | Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.919 |
| dnaJ | AMQ42087.1 | AMS64_16495 | AMS64_06685 | 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 HscC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.987 |
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