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 |
| AWU55_1211 | AWU55_1212 | AWU55_1211 | AWU55_1212 | ADP-ribose diphosphatase; Scaffold_6_3. | Putative hydrolase of the HAD superfamily; Scaffold_6_4. | 0.745 |
| AWU55_1211 | AWU55_1213 | AWU55_1211 | AWU55_1213 | ADP-ribose diphosphatase; Scaffold_6_3. | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 family. | 0.658 |
| AWU55_1211 | hslO | AWU55_1211 | AWU55_1214 | ADP-ribose diphosphatase; Scaffold_6_3. | 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. | 0.573 |
| AWU55_1212 | AWU55_1211 | AWU55_1212 | AWU55_1211 | Putative hydrolase of the HAD superfamily; Scaffold_6_4. | ADP-ribose diphosphatase; Scaffold_6_3. | 0.745 |
| AWU55_1212 | AWU55_1213 | AWU55_1212 | AWU55_1213 | Putative hydrolase of the HAD superfamily; Scaffold_6_4. | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 family. | 0.932 |
| AWU55_1212 | hslO | AWU55_1212 | AWU55_1214 | Putative hydrolase of the HAD superfamily; Scaffold_6_4. | 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. | 0.734 |
| AWU55_1213 | AWU55_1211 | AWU55_1213 | AWU55_1211 | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 family. | ADP-ribose diphosphatase; Scaffold_6_3. | 0.658 |
| AWU55_1213 | AWU55_1212 | AWU55_1213 | AWU55_1212 | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 family. | Putative hydrolase of the HAD superfamily; Scaffold_6_4. | 0.932 |
| AWU55_1213 | dnaJ | AWU55_1213 | AWU55_2568 | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 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, [...] | 0.662 |
| AWU55_1213 | grpE | AWU55_1213 | AWU55_2570 | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 family. | 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 [...] | 0.687 |
| AWU55_1213 | hslO | AWU55_1213 | AWU55_1214 | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 family. | 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. | 0.961 |
| AWU55_1213 | hslU | AWU55_1213 | AWU55_37 | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 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. | 0.682 |
| AWU55_1213 | hslV | AWU55_1213 | AWU55_36 | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 family. | ATP-dependent HslUV protease, peptidase subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.805 |
| AWU55_1213 | htpG | AWU55_1213 | AWU55_2041 | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.520 |
| coaX | hslO | AWU55_368 | AWU55_1214 | Type III pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | 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. | 0.535 |
| dnaJ | AWU55_1213 | AWU55_2568 | AWU55_1213 | 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, [...] | Ribosome-associated heat shock protein Hsp15; Scaffold_6_5; Belongs to the HSP15 family. | 0.662 |
| dnaJ | groL | AWU55_2568 | AWU55_2430 | 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, [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.968 |
| dnaJ | grpE | AWU55_2568 | AWU55_2570 | 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, [...] | 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 [...] | 0.991 |
| dnaJ | hslO | AWU55_2568 | AWU55_1214 | 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, [...] | 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. | 0.672 |
| dnaJ | hslU | AWU55_2568 | AWU55_37 | 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 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. | 0.945 |
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