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 |
| clpP | clpQ | BSU34540 | BSU16150 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | 0.970 |
| clpP | clpY | BSU34540 | BSU16160 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Two-component ATP-dependent protease (ATPase and chaperone); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity; Belongs to the ClpX chaperone family. HslU subfamily. | 0.984 |
| clpP | codY | BSU34540 | BSU16170 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Transcriptional regulator, GTP and BCAA-dependent; 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 and sporulation. 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. | 0.440 |
| clpP | dnaK | BSU34540 | BSU25470 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.982 |
| clpP | groEL | BSU34540 | BSU06030 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.972 |
| clpP | groES | BSU34540 | BSU06020 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Chaperonin small subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.924 |
| clpP | grpE | BSU34540 | BSU25480 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Nucleotide exchange factor for DnaK activity; 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. S [...] | 0.947 |
| clpP | htpG | BSU34540 | BSU39820 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.679 |
| clpP | lonA | BSU34540 | BSU28200 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Class III heat-shock ATP-dependent LonA 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 (By similarity). Has been implicated in preventing sigma(G) activity under non-sporulation conditions. | 0.796 |
| clpQ | clpP | BSU16150 | BSU34540 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | 0.970 |
| clpQ | clpY | BSU16150 | BSU16160 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Two-component ATP-dependent protease (ATPase and chaperone); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity; Belongs to the ClpX chaperone family. HslU subfamily. | 0.999 |
| clpQ | codV | BSU16150 | BSU16140 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Site-specific tyrosine recombinase for chromosome partitioning; 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. | 0.983 |
| clpQ | codY | BSU16150 | BSU16170 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Transcriptional regulator, GTP and BCAA-dependent; 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 and sporulation. 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. | 0.821 |
| clpQ | dnaK | BSU16150 | BSU25470 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.884 |
| clpQ | groEL | BSU16150 | BSU06030 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.904 |
| clpQ | groES | BSU16150 | BSU06020 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Chaperonin small subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.897 |
| clpQ | grpE | BSU16150 | BSU25480 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Nucleotide exchange factor for DnaK activity; 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. S [...] | 0.928 |
| clpQ | htpG | BSU16150 | BSU39820 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.963 |
| clpQ | lonA | BSU16150 | BSU28200 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Class III heat-shock ATP-dependent LonA 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 (By similarity). Has been implicated in preventing sigma(G) activity under non-sporulation conditions. | 0.870 |
| clpY | clpP | BSU16160 | BSU34540 | Two-component ATP-dependent protease (ATPase and chaperone); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity; Belongs to the ClpX chaperone family. HslU subfamily. | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | 0.984 |
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