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 |
| AEA69402.1 | AEA69403.1 | PSEBR_a3095 | PSEBR_a3096 | Putative dehydrogenase. | Conserved hypothetical protein. | 0.668 |
| AEA69402.1 | AEA69405.1 | PSEBR_a3095 | PSEBR_a3098 | Putative dehydrogenase. | Putative ATP-dependent DNA ligase. | 0.546 |
| AEA69402.1 | ilvA-2 | PSEBR_a3095 | PSEBR_a3094 | Putative dehydrogenase. | Threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | 0.401 |
| AEA69402.1 | ku | PSEBR_a3095 | PSEBR_a3097 | Putative dehydrogenase. | Conserved hypothetical protein, KU domain-containing protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | 0.472 |
| AEA69403.1 | AEA69402.1 | PSEBR_a3096 | PSEBR_a3095 | Conserved hypothetical protein. | Putative dehydrogenase. | 0.668 |
| AEA69403.1 | AEA69405.1 | PSEBR_a3096 | PSEBR_a3098 | Conserved hypothetical protein. | Putative ATP-dependent DNA ligase. | 0.513 |
| AEA69403.1 | ku | PSEBR_a3096 | PSEBR_a3097 | Conserved hypothetical protein. | Conserved hypothetical protein, KU domain-containing protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | 0.558 |
| AEA69405.1 | AEA69402.1 | PSEBR_a3098 | PSEBR_a3095 | Putative ATP-dependent DNA ligase. | Putative dehydrogenase. | 0.546 |
| AEA69405.1 | AEA69403.1 | PSEBR_a3098 | PSEBR_a3096 | Putative ATP-dependent DNA ligase. | Conserved hypothetical protein. | 0.513 |
| AEA69405.1 | ku | PSEBR_a3098 | PSEBR_a3097 | Putative ATP-dependent DNA ligase. | Conserved hypothetical protein, KU domain-containing protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | 0.981 |
| ilvA-2 | AEA69402.1 | PSEBR_a3094 | PSEBR_a3095 | Threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. | Putative dehydrogenase. | 0.401 |
| ku | AEA69402.1 | PSEBR_a3097 | PSEBR_a3095 | Conserved hypothetical protein, KU domain-containing protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | Putative dehydrogenase. | 0.472 |
| ku | AEA69403.1 | PSEBR_a3097 | PSEBR_a3096 | Conserved hypothetical protein, KU domain-containing protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | Conserved hypothetical protein. | 0.558 |
| ku | AEA69405.1 | PSEBR_a3097 | PSEBR_a3098 | Conserved hypothetical protein, KU domain-containing protein; With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD. Belongs to the prokaryotic Ku family. | Putative ATP-dependent DNA ligase. | 0.981 |