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 |
| bofA | fin | BSU00230 | BSU00540 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | 0.575 |
| bofA | gerM | BSU00230 | BSU28380 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Germination (cortex hydrolysis) and sporulation (stage II, multiple polar septa) lytic enzyme; Unknown. Affects both sporulation and germination. | 0.554 |
| bofA | spoVID | BSU00230 | BSU28110 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Morphogenetic spore protein (stage VI sporulation); Required for assembly of a normal spore coat. May be a component of the innermost layer of the spore coat that aids in its adherence to the prespore. | 0.809 |
| bofA | yaaC | BSU00230 | BSU00080 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.715 |
| bofA | yabQ | BSU00230 | BSU00610 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Membrane protein of the forespore; Required for sporulation. Plays an important role in cortex and coat formation. | 0.815 |
| bofA | yqfX | BSU00230 | BSU25080 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.763 |
| bofA | yqgE | BSU00230 | BSU25010 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.483 |
| bofA | yrzE | BSU00230 | BSU27690 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Putative transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.711 |
| bofA | ysxE | BSU00230 | BSU28100 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Spore coat protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. | 0.614 |
| bofA | yutH | BSU00230 | BSU32270 | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | Spore coat-associated protein; Involved in sporulation; Belongs to the CotS family. | 0.615 |
| fin | bofA | BSU00540 | BSU00230 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K. | 0.575 |
| fin | gerM | BSU00540 | BSU28380 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Germination (cortex hydrolysis) and sporulation (stage II, multiple polar septa) lytic enzyme; Unknown. Affects both sporulation and germination. | 0.758 |
| fin | spoVID | BSU00540 | BSU28110 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Morphogenetic spore protein (stage VI sporulation); Required for assembly of a normal spore coat. May be a component of the innermost layer of the spore coat that aids in its adherence to the prespore. | 0.782 |
| fin | yaaC | BSU00540 | BSU00080 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.760 |
| fin | yabQ | BSU00540 | BSU00610 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Membrane protein of the forespore; Required for sporulation. Plays an important role in cortex and coat formation. | 0.806 |
| fin | yqfX | BSU00540 | BSU25080 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. | 0.716 |
| fin | yqgE | BSU00540 | BSU25010 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.752 |
| fin | yrzE | BSU00540 | BSU27690 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Putative transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.724 |
| fin | ysxE | BSU00540 | BSU28100 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Spore coat protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. | 0.494 |
| fin | yutH | BSU00540 | BSU32270 | Protein required for the switch from F to G during sporulation (anti sigma F); An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages. Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene. | Spore coat-associated protein; Involved in sporulation; Belongs to the CotS family. | 0.552 |
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