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 |
| Swol_1654 | clpP | Swol_1654 | Swol_1656 | Endopeptidase La; KEGG: mta:Moth_0530 AAA ATPase. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.534 |
| Swol_1654 | clpX | Swol_1654 | Swol_1655 | Endopeptidase La; KEGG: mta:Moth_0530 AAA ATPase. | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.570 |
| Swol_1654 | engB | Swol_1654 | Swol_1652 | Endopeptidase La; KEGG: mta:Moth_0530 AAA ATPase. | GTP-binding protein; Necessary for normal cell division and for the maintenance of normal septation; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family. | 0.433 |
| Swol_1654 | lon | Swol_1654 | Swol_1653 | Endopeptidase La; KEGG: mta:Moth_0530 AAA ATPase. | Lon-A peptidase. Serine peptidase. MEROPS family S16; 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. | 0.626 |
| Swol_2367 | clpP | Swol_2367 | Swol_1656 | KEGG: mta:Moth_0162 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.910 |
| Swol_2367 | clpX | Swol_2367 | Swol_1655 | KEGG: mta:Moth_0162 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.473 |
| Swol_2367 | groL | Swol_2367 | Swol_1855 | KEGG: mta:Moth_0162 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Conserved hypothetical protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.716 |
| Swol_2367 | grpE | Swol_2367 | Swol_1579 | KEGG: mta:Moth_0162 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | GrpE 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-dependent i [...] | 0.829 |
| Swol_2367 | hslU | Swol_2367 | Swol_0844 | KEGG: mta:Moth_0162 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Heat shock protein HslVU, ATPase 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. | 0.570 |
| Swol_2367 | hslV | Swol_2367 | Swol_0843 | KEGG: mta:Moth_0162 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | CodW component of CodWX peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.432 |
| Swol_2367 | lon | Swol_2367 | Swol_1653 | KEGG: mta:Moth_0162 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Lon-A peptidase. Serine peptidase. MEROPS family S16; 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. | 0.689 |
| clpB | clpP | Swol_0493 | Swol_1656 | Putative ATPase with chaperone activity, two ATP-binding domains; 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. | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | 0.896 |
| clpB | clpX | Swol_0493 | Swol_1655 | Putative ATPase with chaperone activity, two ATP-binding domains; 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. | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.473 |
| clpB | groL | Swol_0493 | Swol_1855 | Putative ATPase with chaperone activity, two ATP-binding domains; 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. | Conserved hypothetical protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.716 |
| clpB | grpE | Swol_0493 | Swol_1579 | Putative ATPase with chaperone activity, two ATP-binding domains; 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. | GrpE 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-dependent i [...] | 0.829 |
| clpB | hslU | Swol_0493 | Swol_0844 | Putative ATPase with chaperone activity, two ATP-binding domains; 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. | Heat shock protein HslVU, ATPase 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. | 0.570 |
| clpB | hslV | Swol_0493 | Swol_0843 | Putative ATPase with chaperone activity, two ATP-binding domains; 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. | CodW component of CodWX peptidase. Threonine peptidase. MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.432 |
| clpB | lon | Swol_0493 | Swol_1653 | Putative ATPase with chaperone activity, two ATP-binding domains; 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. | Lon-A peptidase. Serine peptidase. MEROPS family S16; 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. | 0.689 |
| clpP | Swol_1654 | Swol_1656 | Swol_1654 | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | Endopeptidase La; KEGG: mta:Moth_0530 AAA ATPase. | 0.534 |
| clpP | Swol_2367 | Swol_1656 | Swol_2367 | ATP-dependent Clp protease proteolytic subunit ClpP; 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. | KEGG: mta:Moth_0162 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | 0.910 |
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