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 |
| AJR22646.1 | AJR25505.1 | TZ53_01435 | TZ53_18970 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.844 |
| AJR22646.1 | dnaJ | TZ53_01435 | TZ53_13580 | Thioredoxin; 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, [...] | 0.774 |
| AJR22646.1 | dnaK | TZ53_01435 | TZ53_13575 | Thioredoxin; 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. | 0.639 |
| AJR22646.1 | ftsH | TZ53_01435 | TZ53_00280 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cell division protein FtsH; 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. | 0.423 |
| AJR22646.1 | grpE | TZ53_01435 | TZ53_22145 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular 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 [...] | 0.828 |
| AJR22646.1 | htpG | TZ53_01435 | TZ53_00145 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.792 |
| AJR22646.1 | htpX | TZ53_01435 | TZ53_10780 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protease HtpX; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.550 |
| AJR22646.1 | lon | TZ53_01435 | TZ53_17255 | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | DNA-binding protein; 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. | 0.560 |
| AJR22802.1 | ftsH | TZ53_02470 | TZ53_00280 | Flagellar motor switch protein FliM; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cell division protein FtsH; 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. | 0.422 |
| AJR22802.1 | htpX | TZ53_02470 | TZ53_10780 | Flagellar motor switch protein FliM; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protease HtpX; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.513 |
| AJR25505.1 | AJR22646.1 | TZ53_18970 | TZ53_01435 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.844 |
| AJR25505.1 | dnaJ | TZ53_18970 | TZ53_13580 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 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, [...] | 0.925 |
| AJR25505.1 | dnaK | TZ53_18970 | TZ53_13575 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.840 |
| AJR25505.1 | ftsH | TZ53_18970 | TZ53_00280 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Cell division protein FtsH; 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. | 0.543 |
| AJR25505.1 | grpE | TZ53_18970 | TZ53_22145 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Molecular 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 [...] | 0.920 |
| AJR25505.1 | htpG | TZ53_18970 | TZ53_00145 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Heat shock protein 90; Molecular chaperone. Has ATPase activity. | 0.881 |
| AJR25505.1 | htpX | TZ53_18970 | TZ53_10780 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Protease HtpX; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M48B family. | 0.508 |
| AJR25505.1 | lon | TZ53_18970 | TZ53_17255 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | DNA-binding protein; 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. | 0.850 |
| dnaJ | AJR22646.1 | TZ53_13580 | TZ53_01435 | 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, [...] | Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.774 |
| dnaJ | AJR25505.1 | TZ53_13580 | TZ53_18970 | 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, [...] | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.925 |
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