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 |
| entD | exbB | STM0584 | STM3159 | Enterochelin synthetase, component D (phoshpantetheinyltransferase); Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PC [...] | Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity). | 0.403 |
| entD | exbD | STM0584 | STM3158 | Enterochelin synthetase, component D (phoshpantetheinyltransferase); Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PC [...] | tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141. | 0.460 |
| exbB | entD | STM3159 | STM0584 | Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity). | Enterochelin synthetase, component D (phoshpantetheinyltransferase); Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PC [...] | 0.403 |
| exbB | exbD | STM3159 | STM3158 | Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity). | tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141. | 0.999 |
| exbB | tonB | STM3159 | STM1737 | Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity). | TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...] | 0.995 |
| exbD | entD | STM3158 | STM0584 | tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141. | Enterochelin synthetase, component D (phoshpantetheinyltransferase); Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PC [...] | 0.460 |
| exbD | exbB | STM3158 | STM3159 | tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141. | Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity). | 0.999 |
| exbD | tonB | STM3158 | STM1737 | tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141. | TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...] | 0.997 |
| tonB | exbB | STM1737 | STM3159 | TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...] | Uptake of enterochelin; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity). | 0.995 |
| tonB | exbD | STM1737 | STM3158 | TonB; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific en [...] | tonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141. | 0.997 |