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 |
| SFW11154.1 | SFW18714.1 | SAMN02910447_00103 | SAMN02910447_00633 | Threonine dehydratase; 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. | O-acetylhomoserine (thiol)-lyase. | 0.780 |
| SFW11154.1 | SFW20284.1 | SAMN02910447_00103 | SAMN02910447_00764 | Threonine dehydratase; 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. | O-acetylhomoserine (thiol)-lyase. | 0.833 |
| SFW11154.1 | SFW41699.1 | SAMN02910447_00103 | SAMN02910447_02475 | Threonine dehydratase; 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. | 5-methyltetrahydrofolate--homocysteine methyltransferase. | 0.939 |
| SFW11154.1 | ahcY | SAMN02910447_00103 | SAMN02910447_01367 | Threonine dehydratase; 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. | Adenosylhomocysteinase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. | 0.890 |
| SFW11154.1 | metE | SAMN02910447_00103 | SAMN02910447_00092 | Threonine dehydratase; 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. | Methionine synthase (B12-independent); Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family. | 0.889 |
| SFW18639.1 | SFW18671.1 | SAMN02910447_00628 | SAMN02910447_00629 | Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif. | Thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily. | 0.983 |
| SFW18639.1 | SFW18685.1 | SAMN02910447_00628 | SAMN02910447_00630 | Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif. | Sulfur carrier protein. | 0.991 |
| SFW18639.1 | SFW18694.1 | SAMN02910447_00628 | SAMN02910447_00631 | Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif. | Thioredoxin; Belongs to the thioredoxin family. | 0.757 |
| SFW18639.1 | SFW18701.1 | SAMN02910447_00628 | SAMN02910447_00632 | Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif. | TusA-related sulfurtransferase; Belongs to the sulfur carrier protein TusA family. | 0.945 |
| SFW18639.1 | SFW18714.1 | SAMN02910447_00628 | SAMN02910447_00633 | Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif. | O-acetylhomoserine (thiol)-lyase. | 0.758 |
| SFW18671.1 | SFW18639.1 | SAMN02910447_00629 | SAMN02910447_00628 | Thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily. | Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif. | 0.983 |
| SFW18671.1 | SFW18685.1 | SAMN02910447_00629 | SAMN02910447_00630 | Thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily. | Sulfur carrier protein. | 0.994 |
| SFW18671.1 | SFW18694.1 | SAMN02910447_00629 | SAMN02910447_00631 | Thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily. | Thioredoxin; Belongs to the thioredoxin family. | 0.757 |
| SFW18671.1 | SFW18701.1 | SAMN02910447_00629 | SAMN02910447_00632 | Thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily. | TusA-related sulfurtransferase; Belongs to the sulfur carrier protein TusA family. | 0.928 |
| SFW18671.1 | SFW18714.1 | SAMN02910447_00629 | SAMN02910447_00633 | Thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily. | O-acetylhomoserine (thiol)-lyase. | 0.758 |
| SFW18685.1 | SFW18639.1 | SAMN02910447_00630 | SAMN02910447_00628 | Sulfur carrier protein. | Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN metalloenzyme (JAMM) motif. | 0.991 |
| SFW18685.1 | SFW18671.1 | SAMN02910447_00630 | SAMN02910447_00629 | Sulfur carrier protein. | Thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily. | 0.994 |
| SFW18685.1 | SFW18694.1 | SAMN02910447_00630 | SAMN02910447_00631 | Sulfur carrier protein. | Thioredoxin; Belongs to the thioredoxin family. | 0.754 |
| SFW18685.1 | SFW18701.1 | SAMN02910447_00630 | SAMN02910447_00632 | Sulfur carrier protein. | TusA-related sulfurtransferase; Belongs to the sulfur carrier protein TusA family. | 0.952 |
| SFW18685.1 | SFW18714.1 | SAMN02910447_00630 | SAMN02910447_00633 | Sulfur carrier protein. | O-acetylhomoserine (thiol)-lyase. | 0.793 |
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