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 |
| clpQ | clpY | BL01278 | BL01277 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.999 |
| clpQ | codY | BL01278 | BL01276 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Transcriptional regulator; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | 0.732 |
| clpQ | dnaJ | BL01278 | BL02098 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Heat-shock 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 [...] | 0.665 |
| clpQ | dnaK | BL01278 | BL02097 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Class I heat-shock protein (molecular chaperone); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.706 |
| clpQ | groEL | BL01278 | BL03283 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.861 |
| clpQ | groES | BL01278 | BL03284 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.843 |
| clpQ | grpE | BL01278 | BL02095 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | 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 rounds of ATP-depen [...] | 0.857 |
| clpQ | htpG | BL01278 | BL00247 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.870 |
| clpQ | lonA | BL01278 | BL00621 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Class III heat-shock ATP-dependent Lon 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. | 0.849 |
| clpQ | xerC | BL01278 | BL01279 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | Site-specific integrase/recombinase; 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. | 0.946 |
| clpY | clpQ | BL01277 | BL01278 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. | 0.999 |
| clpY | codY | BL01277 | BL01276 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Transcriptional regulator; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | 0.785 |
| clpY | dnaJ | BL01277 | BL02098 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Heat-shock 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 [...] | 0.772 |
| clpY | dnaK | BL01277 | BL02097 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class I heat-shock protein (molecular chaperone); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.757 |
| clpY | groEL | BL01277 | BL03283 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.853 |
| clpY | groES | BL01277 | BL03284 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.851 |
| clpY | grpE | BL01277 | BL02095 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 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 rounds of ATP-depen [...] | 0.867 |
| clpY | htpG | BL01277 | BL00247 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.868 |
| clpY | lonA | BL01277 | BL00621 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class III heat-shock ATP-dependent Lon 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. | 0.869 |
| clpY | xerC | BL01277 | BL01279 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Site-specific integrase/recombinase; 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. | 0.837 |
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