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 |
| AEA66738.1 | AEA66739.1 | PSEBR_a590 | PSEBR_a591 | Putative chaperone. | Curved DNA-binding protein. | 0.932 |
| AEA66738.1 | dnaJ | PSEBR_a590 | PSEBR_a765 | Putative chaperone. | Chaperone protein; 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, DnaK a [...] | 0.909 |
| AEA66738.1 | groL | PSEBR_a590 | PSEBR_a4374 | Putative chaperone. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.900 |
| AEA66738.1 | groS | PSEBR_a590 | PSEBR_a4375 | Putative chaperone. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.856 |
| AEA66738.1 | grpE | PSEBR_a590 | PSEBR_a763 | Putative chaperone. | Chaperone protein (heat shock 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 [...] | 0.924 |
| AEA66738.1 | hslU | PSEBR_a590 | PSEBR_a412 | Putative chaperone. | ATP-dependent protease, ATP-binding 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. | 0.503 |
| AEA66738.1 | htpG | PSEBR_a590 | PSEBR_a4129 | Putative chaperone. | Chaperone protein (heat shock protein); Molecular chaperone. Has ATPase activity. | 0.935 |
| AEA66739.1 | AEA66738.1 | PSEBR_a591 | PSEBR_a590 | Curved DNA-binding protein. | Putative chaperone. | 0.932 |
| AEA66739.1 | AEA68534.1 | PSEBR_a591 | PSEBR_a2257 | Curved DNA-binding protein. | Chaperone; Belongs to the heat shock protein 70 family. | 0.956 |
| AEA66739.1 | dnaK | PSEBR_a591 | PSEBR_a764 | Curved DNA-binding protein. | Chaperone protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.962 |
| AEA66739.1 | groL | PSEBR_a591 | PSEBR_a4374 | Curved DNA-binding protein. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.889 |
| AEA66739.1 | groS | PSEBR_a591 | PSEBR_a4375 | Curved DNA-binding protein. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.714 |
| AEA66739.1 | grpE | PSEBR_a591 | PSEBR_a763 | Curved DNA-binding protein. | Chaperone protein (heat shock 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 [...] | 0.963 |
| AEA66739.1 | hscA | PSEBR_a591 | PSEBR_a929 | Curved DNA-binding protein. | Putative chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.930 |
| AEA66739.1 | hslU | PSEBR_a591 | PSEBR_a412 | Curved DNA-binding protein. | ATP-dependent protease, ATP-binding 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. | 0.775 |
| AEA66739.1 | htpG | PSEBR_a591 | PSEBR_a4129 | Curved DNA-binding protein. | Chaperone protein (heat shock protein); Molecular chaperone. Has ATPase activity. | 0.965 |
| AEA68534.1 | AEA66739.1 | PSEBR_a2257 | PSEBR_a591 | Chaperone; Belongs to the heat shock protein 70 family. | Curved DNA-binding protein. | 0.956 |
| AEA68534.1 | dnaJ | PSEBR_a2257 | PSEBR_a765 | Chaperone; Belongs to the heat shock protein 70 family. | Chaperone protein; 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, DnaK a [...] | 0.981 |
| AEA68534.1 | groL | PSEBR_a2257 | PSEBR_a4374 | 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. | 0.897 |
| AEA68534.1 | groS | PSEBR_a2257 | PSEBR_a4375 | 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. | 0.832 |
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