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 |
| grpE-1 | hslO | sync_0022 | sync_1272 | Co-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-depend [...] | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | 0.543 |
| grpE-1 | htpG | sync_0022 | sync_1398 | Co-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-depend [...] | Chaperone protein HtpG; Identified by similarity to SP:Q9S3Q2; match to protein family HMM PF00183; match to protein family HMM PF02518. | 0.833 |
| grpE-1 | trxB | sync_0022 | sync_0910 | Co-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-depend [...] | Thioredoxin-disulfide reductase; Identified by match to protein family HMM PF00070; match to protein family HMM PF07992; match to protein family HMM TIGR01292. | 0.632 |
| hslO | grpE-1 | sync_1272 | sync_0022 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | Co-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-depend [...] | 0.543 |
| hslO | htpG | sync_1272 | sync_1398 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | Chaperone protein HtpG; Identified by similarity to SP:Q9S3Q2; match to protein family HMM PF00183; match to protein family HMM PF02518. | 0.464 |
| hslO | sync_1273 | sync_1272 | sync_1273 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | ABC transporter, ATP-binding protein; Identified by match to protein family HMM PF00005. | 0.801 |
| hslO | sync_1274 | sync_1272 | sync_1274 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | Uncharacterized protein. | 0.587 |
| hslO | sync_2152 | sync_1272 | sync_2152 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | Identified by match to protein family HMM PF05670; match to protein family HMM PF05833. | 0.593 |
| hslO | sync_2509 | sync_1272 | sync_2509 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | Transcriptional activator, putative, Baf family protein; Identified by match to protein family HMM TIGR00671. | 0.441 |
| hslO | sync_2707 | sync_1272 | sync_2707 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | GTPase family protein; Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity; Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily. | 0.453 |
| hslO | trxB | sync_1272 | sync_0910 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | Thioredoxin-disulfide reductase; Identified by match to protein family HMM PF00070; match to protein family HMM PF07992; match to protein family HMM TIGR01292. | 0.424 |
| hslO | tsf | sync_1272 | sync_1276 | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | Translation elongation factor Ts; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family. | 0.405 |
| htpG | grpE-1 | sync_1398 | sync_0022 | Chaperone protein HtpG; Identified by similarity to SP:Q9S3Q2; match to protein family HMM PF00183; match to protein family HMM PF02518. | Co-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-depend [...] | 0.833 |
| htpG | hslO | sync_1398 | sync_1272 | Chaperone protein HtpG; Identified by similarity to SP:Q9S3Q2; match to protein family HMM PF00183; match to protein family HMM PF02518. | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | 0.464 |
| htpG | trxB | sync_1398 | sync_0910 | Chaperone protein HtpG; Identified by similarity to SP:Q9S3Q2; match to protein family HMM PF00183; match to protein family HMM PF02518. | Thioredoxin-disulfide reductase; Identified by match to protein family HMM PF00070; match to protein family HMM PF07992; match to protein family HMM TIGR01292. | 0.560 |
| sync_1273 | hslO | sync_1273 | sync_1272 | ABC transporter, ATP-binding protein; Identified by match to protein family HMM PF00005. | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | 0.801 |
| sync_1273 | sync_1274 | sync_1273 | sync_1274 | ABC transporter, ATP-binding protein; Identified by match to protein family HMM PF00005. | Uncharacterized protein. | 0.729 |
| sync_1274 | hslO | sync_1274 | sync_1272 | Uncharacterized protein. | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | 0.587 |
| sync_1274 | sync_1273 | sync_1274 | sync_1273 | Uncharacterized protein. | ABC transporter, ATP-binding protein; Identified by match to protein family HMM PF00005. | 0.729 |
| sync_2152 | hslO | sync_2152 | sync_1272 | Identified by match to protein family HMM PF05670; match to protein family HMM PF05833. | 33 kDa chaperonin (Heat shock protein 33 homolog) (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. | 0.593 |
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