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 |
| hslO | hslU | GCA_001266615_00412 | GCA_001266615_01838 | Unannotated protein; 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. | Unannotated protein; 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 |
| hslO | htpG | GCA_001266615_00412 | GCA_001266615_01410 | Unannotated protein; 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. | Unannotated protein; Molecular chaperone. Has ATPase activity. | 0.603 |
| hslO | prlC | GCA_001266615_00412 | GCA_001266615_00499 | Unannotated protein; 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. | Unannotated protein. | 0.444 |
| hslO | ybbN | GCA_001266615_00412 | GCA_001266615_01395 | Unannotated protein; 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. | Unannotated protein. | 0.535 |
| hslU | hslO | GCA_001266615_01838 | GCA_001266615_00412 | Unannotated protein; 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. | Unannotated protein; 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. | 0.862 |
| hslU | htpG | GCA_001266615_01838 | GCA_001266615_01410 | Unannotated protein; 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. | Unannotated protein; Molecular chaperone. Has ATPase activity. | 0.910 |
| hslU | prlC | GCA_001266615_01838 | GCA_001266615_00499 | Unannotated protein; 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. | Unannotated protein. | 0.410 |
| hslU | ybbN | GCA_001266615_01838 | GCA_001266615_01395 | Unannotated protein; 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. | Unannotated protein. | 0.905 |
| htpG | hslO | GCA_001266615_01410 | GCA_001266615_00412 | Unannotated protein; Molecular chaperone. Has ATPase activity. | Unannotated protein; 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. | 0.603 |
| htpG | hslU | GCA_001266615_01410 | GCA_001266615_01838 | Unannotated protein; Molecular chaperone. Has ATPase activity. | Unannotated protein; 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. | 0.910 |
| htpG | prlC | GCA_001266615_01410 | GCA_001266615_00499 | Unannotated protein; Molecular chaperone. Has ATPase activity. | Unannotated protein. | 0.408 |
| htpG | ybbN | GCA_001266615_01410 | GCA_001266615_01395 | Unannotated protein; Molecular chaperone. Has ATPase activity. | Unannotated protein. | 0.900 |
| leuE_1 | prlC | GCA_001266615_00500 | GCA_001266615_00499 | Unannotated protein. | Unannotated protein. | 0.548 |
| leuE_1 | rsmJ | GCA_001266615_00500 | GCA_001266615_00498 | Unannotated protein. | Unannotated protein; Specifically methylates the guanosine in position 1516 of 16S rRNA. | 0.504 |
| prlC | hslO | GCA_001266615_00499 | GCA_001266615_00412 | Unannotated protein. | Unannotated protein; 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. | 0.444 |
| prlC | hslU | GCA_001266615_00499 | GCA_001266615_01838 | Unannotated protein. | Unannotated protein; 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. | 0.410 |
| prlC | htpG | GCA_001266615_00499 | GCA_001266615_01410 | Unannotated protein. | Unannotated protein; Molecular chaperone. Has ATPase activity. | 0.408 |
| prlC | leuE_1 | GCA_001266615_00499 | GCA_001266615_00500 | Unannotated protein. | Unannotated protein. | 0.548 |
| prlC | rsmJ | GCA_001266615_00499 | GCA_001266615_00498 | Unannotated protein. | Unannotated protein; Specifically methylates the guanosine in position 1516 of 16S rRNA. | 0.816 |
| prlC | ybbN | GCA_001266615_00499 | GCA_001266615_01395 | Unannotated protein. | Unannotated protein. | 0.418 |
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