Export your current network:
... as a bitmap image:
file format is 'PNG': portable network graphic
... as a high-resolution bitmap:
same PNG format, but at higher resolution
... 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 |
DsdA | GCA_001952955_03745 | GCA_001952955_04233 | GCA_001952955_03745 | Unannotated protein. | Unannotated protein. | 0.800 |
DsdA | gloA_1 | GCA_001952955_04233 | GCA_001952955_01969 | Unannotated protein. | Unannotated protein. | 0.800 |
DsdA | ilvA | GCA_001952955_04233 | GCA_001952955_02802 | Unannotated protein. | Unannotated protein; 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. | 0.919 |
DsdA | sdaA | GCA_001952955_04233 | GCA_001952955_01318 | Unannotated protein. | Unannotated protein; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.920 |
DsdA | sdaB | GCA_001952955_04233 | GCA_001952955_01859 | Unannotated protein. | Unannotated protein; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.920 |
GCA_001952955_03745 | DsdA | GCA_001952955_03745 | GCA_001952955_04233 | Unannotated protein. | Unannotated protein. | 0.800 |
GCA_001952955_03745 | gloA_1 | GCA_001952955_03745 | GCA_001952955_01969 | Unannotated protein. | Unannotated protein. | 0.906 |
GCA_001952955_03745 | ilvA | GCA_001952955_03745 | GCA_001952955_02802 | Unannotated protein. | Unannotated protein; 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. | 0.829 |
GCA_001952955_03745 | sdaA | GCA_001952955_03745 | GCA_001952955_01318 | Unannotated protein. | Unannotated protein; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.810 |
GCA_001952955_03745 | sdaB | GCA_001952955_03745 | GCA_001952955_01859 | Unannotated protein. | Unannotated protein; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.810 |
GCA_001952955_03745 | trpA | GCA_001952955_03745 | GCA_001952955_01706 | Unannotated protein. | Unannotated protein; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.809 |
GCA_001952955_03745 | trpB | GCA_001952955_03745 | GCA_001952955_01705 | Unannotated protein. | Unannotated protein; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.809 |
VFL11327_02789 | gloA_1 | GCA_001952955_01295 | GCA_001952955_01969 | Unannotated protein. | Unannotated protein. | 0.933 |
VFL11327_02789 | gloB_1 | GCA_001952955_01295 | GCA_001952955_00605 | Unannotated protein. | Unannotated protein; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.917 |
gloA_1 | DsdA | GCA_001952955_01969 | GCA_001952955_04233 | Unannotated protein. | Unannotated protein. | 0.800 |
gloA_1 | GCA_001952955_03745 | GCA_001952955_01969 | GCA_001952955_03745 | Unannotated protein. | Unannotated protein. | 0.906 |
gloA_1 | VFL11327_02789 | GCA_001952955_01969 | GCA_001952955_01295 | Unannotated protein. | Unannotated protein. | 0.933 |
gloA_1 | gloB_1 | GCA_001952955_01969 | GCA_001952955_00605 | Unannotated protein. | Unannotated protein; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.975 |
gloA_1 | ilvA | GCA_001952955_01969 | GCA_001952955_02802 | Unannotated protein. | Unannotated protein; 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. | 0.815 |
gloA_1 | nth | GCA_001952955_01969 | GCA_001952955_01968 | Unannotated protein. | Unannotated protein; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. | 0.793 |
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