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 |
| BPUM_0043 | clpQ | BPUM_0043 | BPUM_1513 | Hypothetical protein. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | 0.731 |
| BPUM_0043 | clpY | BPUM_0043 | BPUM_1514 | Hypothetical protein. | Clp protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.638 |
| BPUM_0043 | dnaJ | BPUM_0043 | BPUM_2279 | Hypothetical protein. | 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, [...] | 0.429 |
| BPUM_0043 | grpE | BPUM_0043 | BPUM_2281 | Hypothetical protein. | 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 [...] | 0.584 |
| BPUM_2560 | clpQ | BPUM_2560 | BPUM_1513 | Exlusion protein FxsA. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | 0.730 |
| BPUM_2560 | clpY | BPUM_2560 | BPUM_1514 | Exlusion protein FxsA. | Clp protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.558 |
| clpQ | BPUM_0043 | BPUM_1513 | BPUM_0043 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | Hypothetical protein. | 0.731 |
| clpQ | BPUM_2560 | BPUM_1513 | BPUM_2560 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | Exlusion protein FxsA. | 0.730 |
| clpQ | clpY | BPUM_1513 | BPUM_1514 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | Clp protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.999 |
| clpQ | dnaJ | BPUM_1513 | BPUM_2279 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | 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, [...] | 0.743 |
| clpQ | groEL | BPUM_1513 | BPUM_0535 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.840 |
| clpQ | groS | BPUM_1513 | BPUM_0534 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | Hypothetical protein; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.816 |
| clpQ | grpE | BPUM_1513 | BPUM_2281 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | 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 [...] | 0.833 |
| clpQ | lon | BPUM_1513 | BPUM_2461 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | Peptidase; 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. | 0.789 |
| clpQ | xerC | BPUM_1513 | BPUM_1512 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | Recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.940 |
| clpQ | xerD | BPUM_1513 | BPUM_2082 | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | Recombinase XerD; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.736 |
| clpY | BPUM_0043 | BPUM_1514 | BPUM_0043 | Clp protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Hypothetical protein. | 0.638 |
| clpY | BPUM_2560 | BPUM_1514 | BPUM_2560 | Clp protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Exlusion protein FxsA. | 0.558 |
| clpY | clpQ | BPUM_1514 | BPUM_1513 | Clp protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex. | 0.999 |
| clpY | dnaJ | BPUM_1514 | BPUM_2279 | Clp protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 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, [...] | 0.832 |
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