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 |
| eutB | eutC | STM2458 | STM2457 | Ethanolamine ammonia-lyase, heavy chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. | Ethanolamine ammonia-lyase, light chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. | 0.999 |
| eutB | eutH | STM2458 | STM2460 | Ethanolamine ammonia-lyase, heavy chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. | Putative transport protein; Possibly involved in the transport of ethanolamine from the periplasm to the cytoplasm. | 0.997 |
| eutC | eutB | STM2457 | STM2458 | Ethanolamine ammonia-lyase, light chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. | Ethanolamine ammonia-lyase, heavy chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. | 0.999 |
| eutC | eutH | STM2457 | STM2460 | Ethanolamine ammonia-lyase, light chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. | Putative transport protein; Possibly involved in the transport of ethanolamine from the periplasm to the cytoplasm. | 0.998 |
| eutH | eutB | STM2460 | STM2458 | Putative transport protein; Possibly involved in the transport of ethanolamine from the periplasm to the cytoplasm. | Ethanolamine ammonia-lyase, heavy chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. | 0.997 |
| eutH | eutC | STM2460 | STM2457 | Putative transport protein; Possibly involved in the transport of ethanolamine from the periplasm to the cytoplasm. | Ethanolamine ammonia-lyase, light chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. | 0.998 |
| grpE | htpG | STM2681 | STM0487 | Molecular chaparone; 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-depe [...] | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | 0.927 |
| grpE | trxA | STM2681 | STM3915 | Molecular chaparone; 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-depe [...] | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family. | 0.592 |
| grpE | trxB | STM2681 | STM0958 | Molecular chaparone; 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-depe [...] | Similar to E. coli thioredoxin reductase (AAC73974.1); Blastp hit to AAC73974.1 (321 aa), 96% identity in aa 1 - 320. | 0.405 |
| grpE | trxC | STM2681 | STM2649 | Molecular chaparone; 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-depe [...] | Similar to E. coli putative thioredoxin-like protein (AAC75635.1); Blastp hit to AAC75635.1 (139 aa), 94% identity in aa 1 - 139; Belongs to the thioredoxin family. | 0.529 |
| grpE | yrfI | STM2681 | STM3498 | Molecular chaparone; 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-depe [...] | Heat shock protein 33; 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. | 0.790 |
| htpG | grpE | STM0487 | STM2681 | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | Molecular chaparone; 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-depe [...] | 0.927 |
| htpG | trxA | STM0487 | STM3915 | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family. | 0.553 |
| htpG | trxC | STM0487 | STM2649 | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | Similar to E. coli putative thioredoxin-like protein (AAC75635.1); Blastp hit to AAC75635.1 (139 aa), 94% identity in aa 1 - 139; Belongs to the thioredoxin family. | 0.534 |
| htpG | yrfI | STM0487 | STM3498 | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | Heat shock protein 33; 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. | 0.704 |
| trxA | grpE | STM3915 | STM2681 | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family. | Molecular chaparone; 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-depe [...] | 0.592 |
| trxA | htpG | STM3915 | STM0487 | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family. | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | 0.553 |
| trxA | trxB | STM3915 | STM0958 | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family. | Similar to E. coli thioredoxin reductase (AAC73974.1); Blastp hit to AAC73974.1 (321 aa), 96% identity in aa 1 - 320. | 0.999 |
| trxB | grpE | STM0958 | STM2681 | Similar to E. coli thioredoxin reductase (AAC73974.1); Blastp hit to AAC73974.1 (321 aa), 96% identity in aa 1 - 320. | Molecular chaparone; 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-depe [...] | 0.405 |
| trxB | trxA | STM0958 | STM3915 | Similar to E. coli thioredoxin reductase (AAC73974.1); Blastp hit to AAC73974.1 (321 aa), 96% identity in aa 1 - 320. | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family. | 0.999 |
page 1 of 2