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 |
| ALP39978.1 | ALP40210.1 | WL1483_559 | WL1483_4468 | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome C. | 0.554 |
| ALP39978.1 | ALP41147.1 | WL1483_559 | WL1483_1728 | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c-552. | 0.539 |
| ALP39978.1 | ALP43722.1 | WL1483_559 | WL1483_4303 | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Heme A synthase. | 0.895 |
| ALP39978.1 | cc4 | WL1483_559 | WL1483_4241 | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome C. | 0.610 |
| ALP39978.1 | nuoI | WL1483_559 | WL1483_3555 | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | NADH dehydrogenase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | 0.785 |
| ALP39978.1 | petA | WL1483_559 | WL1483_1843 | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Ubiquinol-cytochrome c reductase, iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.998 |
| ALP39978.1 | petC | WL1483_559 | WL1483_1363 | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Ubiquinol--cytochrome c reductase, cytochrome c1. | 0.978 |
| ALP39978.1 | yfhL | WL1483_559 | WL1483_517 | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Ferredoxin. | 0.785 |
| ALP40210.1 | ALP39978.1 | WL1483_4468 | WL1483_559 | Cytochrome C. | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.554 |
| ALP40210.1 | ALP41147.1 | WL1483_4468 | WL1483_1728 | Cytochrome C. | Cytochrome c-552. | 0.565 |
| ALP40210.1 | ALP42245.1 | WL1483_4468 | WL1483_2826 | Cytochrome C. | Putative transcriptional regulator. | 0.694 |
| ALP40210.1 | ALP43722.1 | WL1483_4468 | WL1483_4303 | Cytochrome C. | Heme A synthase. | 0.705 |
| ALP40210.1 | cc4 | WL1483_4468 | WL1483_4241 | Cytochrome C. | Cytochrome C. | 0.818 |
| ALP40210.1 | nuoI | WL1483_4468 | WL1483_3555 | Cytochrome C. | NADH dehydrogenase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | 0.621 |
| ALP40210.1 | petA | WL1483_4468 | WL1483_1843 | Cytochrome C. | Ubiquinol-cytochrome c reductase, iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | 0.619 |
| ALP40210.1 | petC | WL1483_4468 | WL1483_1363 | Cytochrome C. | Ubiquinol--cytochrome c reductase, cytochrome c1. | 0.790 |
| ALP40210.1 | pmp3 | WL1483_4468 | WL1483_4773 | Cytochrome C. | Membrane protein. | 0.694 |
| ALP40210.1 | yfhL | WL1483_4468 | WL1483_517 | Cytochrome C. | Ferredoxin. | 0.621 |
| ALP41147.1 | ALP39978.1 | WL1483_1728 | WL1483_559 | Cytochrome c-552. | Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.539 |
| ALP41147.1 | ALP40210.1 | WL1483_1728 | WL1483_4468 | Cytochrome c-552. | Cytochrome C. | 0.565 |
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