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 |
| ClpA | Lon | DR97_3426 | DR97_77 | Atp-dependent clp protease atp-binding subunit clpc; Belongs to the ClpA/ClpB family | 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 | 0.775 |
| ClpA | clpP2 | DR97_3426 | DR97_4601 | Atp-dependent clp protease atp-binding subunit clpc; Belongs to the ClpA/ClpB family | Atp-dependent clp protease proteolytic subunit; 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 | 0.911 |
| ClpA | clpX | DR97_3426 | DR97_78 | Atp-dependent clp protease atp-binding subunit clpc; 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 | 0.895 |
| ClpA | dnaK | DR97_3426 | DR97_2105 | Atp-dependent clp protease atp-binding subunit clpc; Belongs to the ClpA/ClpB family | Molecular chaperone dnak; Acts as a chaperone | 0.825 |
| ClpA | groL | DR97_3426 | DR97_1563 | Atp-dependent clp protease atp-binding subunit clpc; Belongs to the ClpA/ClpB family | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 0.655 |
| ClpA | hslU | DR97_3426 | DR97_2409 | Atp-dependent clp protease atp-binding subunit clpc; Belongs to the ClpA/ClpB family | Atp-dependent hsluv protease atp-binding 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 | 0.618 |
| ClpA | hslV | DR97_3426 | DR97_2408 | Atp-dependent clp protease atp-binding subunit clpc; Belongs to the ClpA/ClpB family | Atp-dependent hsluv protease, peptidase subunit hslv; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery | 0.454 |
| ClpA | lon | DR97_3426 | DR97_1204 | Atp-dependent clp protease atp-binding subunit clpc; Belongs to the ClpA/ClpB family | Putative atp-dependent 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 | 0.800 |
| Lon | ClpA | DR97_77 | DR97_3426 | 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 | Atp-dependent clp protease atp-binding subunit clpc; Belongs to the ClpA/ClpB family | 0.775 |
| Lon | clpA | DR97_77 | DR97_5342 | 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 | Atp-dependent clp protease atp-binding subunit clpa; Belongs to the ClpA/ClpB family | 0.830 |
| Lon | clpB | DR97_77 | DR97_1845 | 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 | Atp-dependent clp protease atp-binding subunit 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity) | 0.853 |
| Lon | clpP2 | DR97_77 | DR97_4601 | 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 | Atp-dependent clp protease proteolytic subunit; 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 | 0.922 |
| Lon | clpX | DR97_77 | DR97_78 | 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 | 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 | 0.993 |
| Lon | dnaK | DR97_77 | DR97_2105 | 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 | Molecular chaperone dnak; Acts as a chaperone | 0.898 |
| Lon | groL | DR97_77 | DR97_1563 | 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 | Chaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions | 0.586 |
| Lon | hslU | DR97_77 | DR97_2409 | 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 | Atp-dependent hsluv protease atp-binding 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 | 0.862 |
| Lon | hslV | DR97_77 | DR97_2408 | 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 | Atp-dependent hsluv protease, peptidase subunit hslv; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery | 0.839 |
| clpA | Lon | DR97_5342 | DR97_77 | Atp-dependent clp protease atp-binding subunit clpa; Belongs to the ClpA/ClpB family | 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 | 0.830 |
| clpA | clpP2 | DR97_5342 | DR97_4601 | Atp-dependent clp protease atp-binding subunit clpa; Belongs to the ClpA/ClpB family | Atp-dependent clp protease proteolytic subunit; 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 | 0.959 |
| clpA | clpX | DR97_5342 | DR97_78 | Atp-dependent clp protease atp-binding subunit clpa; 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 | 0.962 |
page 1 of 6
