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 |
| KZL38752.1 | KZL41059.1 | TY91_11740 | TY91_07340 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.623 |
| KZL38752.1 | KZL41561.1 | TY91_11740 | TY91_06030 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.698 |
| KZL38752.1 | dnaJ | TY91_11740 | TY91_04065 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaJ; 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, [...] | 0.606 |
| KZL38752.1 | dnaK | TY91_11740 | TY91_04060 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.652 |
| KZL38752.1 | groEL | TY91_11740 | TY91_06025 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.768 |
| KZL38752.1 | grpE | TY91_11740 | TY91_04055 | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 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- [...] | 0.717 |
| KZL41059.1 | KZL38752.1 | TY91_07340 | TY91_11740 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.623 |
| KZL41059.1 | KZL41561.1 | TY91_07340 | TY91_06030 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.836 |
| KZL41059.1 | clpP | TY91_07340 | TY91_05840 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Clp protease; 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. | 0.766 |
| KZL41059.1 | dnaJ | TY91_07340 | TY91_04065 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Molecular chaperone DnaJ; 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, [...] | 0.652 |
| KZL41059.1 | dnaK | TY91_07340 | TY91_04060 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.633 |
| KZL41059.1 | groEL | TY91_07340 | TY91_06025 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.904 |
| KZL41059.1 | grpE | TY91_07340 | TY91_04055 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Heat shock protein 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- [...] | 0.859 |
| KZL41059.1 | hslO | TY91_07340 | TY91_14040 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Molecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.753 |
| KZL41059.1 | hslU | TY91_07340 | TY91_07345 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent protease; 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. | 0.999 |
| KZL41059.1 | xerC | TY91_07340 | TY91_07335 | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Recombinase XerC; 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. | 0.911 |
| KZL41561.1 | KZL38752.1 | TY91_06030 | TY91_11740 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.698 |
| KZL41561.1 | KZL41059.1 | TY91_06030 | TY91_07340 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.836 |
| KZL41561.1 | clpP | TY91_06030 | TY91_05840 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Clp protease; 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. | 0.890 |
| KZL41561.1 | dnaJ | TY91_06030 | TY91_04065 | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Molecular chaperone DnaJ; 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, [...] | 0.875 |
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