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 |
| AGE26272.1 | AGE28796.1 | H045_11035 | H045_23690 | COG0071 Molecular chaperone (small heat shock protein). | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | 0.504 |
| AGE26272.1 | AGE28797.1 | H045_11035 | H045_23695 | COG0071 Molecular chaperone (small heat shock protein). | Curved DNA-binding protein; COG2214 DnaJ-class molecular chaperone. | 0.505 |
| AGE26272.1 | clpB | H045_11035 | H045_00735 | COG0071 Molecular chaperone (small heat shock protein). | Chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.707 |
| AGE26272.1 | dnaJ | H045_11035 | H045_16895 | COG0071 Molecular chaperone (small heat shock protein). | 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 [...] | 0.634 |
| AGE26272.1 | dnaK | H045_11035 | H045_16900 | COG0071 Molecular chaperone (small heat shock protein). | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.507 |
| AGE26272.1 | groEL | H045_11035 | H045_15770 | COG0071 Molecular chaperone (small heat shock protein). | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.424 |
| AGE26272.1 | groES | H045_11035 | H045_15775 | COG0071 Molecular chaperone (small heat shock protein). | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.511 |
| AGE26272.1 | grpE | H045_11035 | H045_16905 | COG0071 Molecular chaperone (small heat shock protein). | Heat shock protein 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- [...] | 0.683 |
| AGE26272.1 | hslU | H045_11035 | H045_22870 | COG0071 Molecular chaperone (small heat shock protein). | ATP-dependent protease ATP-binding 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. | 0.586 |
| AGE26272.1 | hslV | H045_11035 | H045_22875 | COG0071 Molecular chaperone (small heat shock protein). | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.597 |
| AGE26272.1 | htpG | H045_11035 | H045_05365 | COG0071 Molecular chaperone (small heat shock protein). | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.704 |
| AGE26272.1 | lon | H045_11035 | H045_02290 | COG0071 Molecular chaperone (small heat shock protein). | ATP-dependent protease; 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. | 0.470 |
| AGE26272.1 | lon-2 | H045_11035 | H045_11745 | COG0071 Molecular chaperone (small heat shock protein). | 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. | 0.470 |
| AGE28796.1 | AGE26272.1 | H045_23690 | H045_11035 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | COG0071 Molecular chaperone (small heat shock protein). | 0.504 |
| AGE28796.1 | AGE28797.1 | H045_23690 | H045_23695 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Curved DNA-binding protein; COG2214 DnaJ-class molecular chaperone. | 0.893 |
| AGE28796.1 | clpB | H045_23690 | H045_00735 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 0.657 |
| AGE28796.1 | clpP | H045_23690 | H045_11755 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.481 |
| AGE28796.1 | dnaJ | H045_23690 | H045_16895 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | 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 [...] | 0.841 |
| AGE28796.1 | groEL | H045_23690 | H045_15770 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.813 |
| AGE28796.1 | groES | H045_23690 | H045_15775 | Heat shock protein, Hsp70 family; COG0443 Molecular chaperone. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.766 |
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