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 |
| EDS74020.1 | clpP | CLOSPI_02446 | CLOSPI_02165 | ATPase family associated with various cellular activities (AAA); KEGG: eru:Erum4660 8.4e-96 clpA; ATP-dependent Clp protease, ATP-binding subunit K03694; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | Endopeptidase Clp; 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. | 0.966 |
| EDS74020.1 | groL | CLOSPI_02446 | CLOSPI_00416 | ATPase family associated with various cellular activities (AAA); KEGG: eru:Erum4660 8.4e-96 clpA; ATP-dependent Clp protease, ATP-binding subunit K03694; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.627 |
| EDS74020.1 | grpE | CLOSPI_02446 | CLOSPI_00866 | ATPase family associated with various cellular activities (AAA); KEGG: eru:Erum4660 8.4e-96 clpA; ATP-dependent Clp protease, ATP-binding subunit K03694; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | Co-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-depend [...] | 0.758 |
| EDS74020.1 | htpG | CLOSPI_02446 | CLOSPI_00715 | ATPase family associated with various cellular activities (AAA); KEGG: eru:Erum4660 8.4e-96 clpA; ATP-dependent Clp protease, ATP-binding subunit K03694; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.677 |
| EDS74020.1 | lon | CLOSPI_02446 | CLOSPI_00899 | ATPase family associated with various cellular activities (AAA); KEGG: eru:Erum4660 8.4e-96 clpA; ATP-dependent Clp protease, ATP-binding subunit K03694; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | Endopeptidase La; 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. | 0.662 |
| EDS76003.1 | clpP | CLOSPI_00116 | CLOSPI_02165 | Trypsin; KEGG: bsu:BG11054 1.1e-70 yyxA, yycK; similar to serine protease Do; COG: COG0265 Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domain. | Endopeptidase Clp; 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. | 0.482 |
| EDS76003.1 | lon | CLOSPI_00116 | CLOSPI_00899 | Trypsin; KEGG: bsu:BG11054 1.1e-70 yyxA, yycK; similar to serine protease Do; COG: COG0265 Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domain. | Endopeptidase La; 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. | 0.653 |
| clpB | clpP | CLOSPI_00570 | CLOSPI_02165 | Putative ATP-dependent chaperone protein ClpB; 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. | Endopeptidase Clp; 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. | 0.956 |
| clpB | groL | CLOSPI_00570 | CLOSPI_00416 | Putative ATP-dependent chaperone protein ClpB; 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. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.627 |
| clpB | grpE | CLOSPI_00570 | CLOSPI_00866 | Putative ATP-dependent chaperone protein ClpB; 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. | Co-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-depend [...] | 0.758 |
| clpB | htpG | CLOSPI_00570 | CLOSPI_00715 | Putative ATP-dependent chaperone protein ClpB; 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. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.677 |
| clpB | lon | CLOSPI_00570 | CLOSPI_00899 | Putative ATP-dependent chaperone protein ClpB; 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. | Endopeptidase La; 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. | 0.662 |
| clpP | EDS74020.1 | CLOSPI_02165 | CLOSPI_02446 | Endopeptidase Clp; 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. | ATPase family associated with various cellular activities (AAA); KEGG: eru:Erum4660 8.4e-96 clpA; ATP-dependent Clp protease, ATP-binding subunit K03694; COG: COG0542 ATPases with chaperone activity, ATP-binding subunit; Psort location: Cytoplasmic, score: 9.98; Belongs to the ClpA/ClpB family. | 0.966 |
| clpP | EDS76003.1 | CLOSPI_02165 | CLOSPI_00116 | Endopeptidase Clp; 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. | Trypsin; KEGG: bsu:BG11054 1.1e-70 yyxA, yycK; similar to serine protease Do; COG: COG0265 Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domain. | 0.482 |
| clpP | clpB | CLOSPI_02165 | CLOSPI_00570 | Endopeptidase Clp; 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. | Putative ATP-dependent chaperone protein ClpB; 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. | 0.956 |
| clpP | groL | CLOSPI_02165 | CLOSPI_00416 | Endopeptidase Clp; 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. | Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.723 |
| clpP | grpE | CLOSPI_02165 | CLOSPI_00866 | Endopeptidase Clp; 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. | Co-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-depend [...] | 0.768 |
| clpP | hflB | CLOSPI_02165 | CLOSPI_02241 | Endopeptidase Clp; 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. | ATP-dependent metallopeptidase HflB; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.400 |
| clpP | htpG | CLOSPI_02165 | CLOSPI_00715 | Endopeptidase Clp; 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. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.422 |
| clpP | lon | CLOSPI_02165 | CLOSPI_00899 | Endopeptidase Clp; 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; 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. | 0.670 |
page 1 of 3