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 |
| azo2278 | azo2279 | azo2278 | azo2279 | Conserved hypothetical protein. Homology to pa3943 of P. aeruginosa (TREMBL:Q9HX73). no domians predicted. weak evidence for signal peptide. no TMHs. | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | 0.873 |
| azo2278 | azo2280 | azo2278 | azo2280 | Conserved hypothetical protein. Homology to pa3943 of P. aeruginosa (TREMBL:Q9HX73). no domians predicted. weak evidence for signal peptide. no TMHs. | Hypothetical protein 25% Identity to TrEMBL;Q7U749. No domains, repeats, motifs or features present. | 0.633 |
| azo2278 | nifF2 | azo2278 | azo2281 | Conserved hypothetical protein. Homology to pa3943 of P. aeruginosa (TREMBL:Q9HX73). no domians predicted. weak evidence for signal peptide. no TMHs. | Probable flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. | 0.556 |
| azo2279 | azo2278 | azo2279 | azo2278 | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | Conserved hypothetical protein. Homology to pa3943 of P. aeruginosa (TREMBL:Q9HX73). no domians predicted. weak evidence for signal peptide. no TMHs. | 0.873 |
| azo2279 | azo2280 | azo2279 | azo2280 | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | Hypothetical protein 25% Identity to TrEMBL;Q7U749. No domains, repeats, motifs or features present. | 0.773 |
| azo2279 | nifF2 | azo2279 | azo2281 | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | Probable flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. | 0.590 |
| azo2280 | azo2278 | azo2280 | azo2278 | Hypothetical protein 25% Identity to TrEMBL;Q7U749. No domains, repeats, motifs or features present. | Conserved hypothetical protein. Homology to pa3943 of P. aeruginosa (TREMBL:Q9HX73). no domians predicted. weak evidence for signal peptide. no TMHs. | 0.633 |
| azo2280 | azo2279 | azo2280 | azo2279 | Hypothetical protein 25% Identity to TrEMBL;Q7U749. No domains, repeats, motifs or features present. | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | 0.773 |
| azo2280 | nifF2 | azo2280 | azo2281 | Hypothetical protein 25% Identity to TrEMBL;Q7U749. No domains, repeats, motifs or features present. | Probable flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. | 0.539 |
| nifF2 | azo2278 | azo2281 | azo2278 | Probable flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. | Conserved hypothetical protein. Homology to pa3943 of P. aeruginosa (TREMBL:Q9HX73). no domians predicted. weak evidence for signal peptide. no TMHs. | 0.556 |
| nifF2 | azo2279 | azo2281 | azo2279 | Probable flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. | Conserved hypothetical protein. Homology to Avin02000067 of Azotobacter vinelandii of 50% (gi|23105742|ref|ZP_00092196.1|(NBCI ENTREZ)). InterPro: Ankyrin-repeat. The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly repeated modules of about 33 amino acids.The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [...] | 0.590 |
| nifF2 | azo2280 | azo2281 | azo2280 | Probable flavodoxin; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. | Hypothetical protein 25% Identity to TrEMBL;Q7U749. No domains, repeats, motifs or features present. | 0.539 |