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 |
| KWX69362.1 | ktrB1 | AMQ84_30665 | AMQ84_04940 | Ion transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP synthase subunit J; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.709 |
| KWX69362.1 | ktrB3 | AMQ84_30665 | AMQ84_12145 | Ion transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP synthase subunit J; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.709 |
| KWX71657.1 | KWX81187.1 | AMQ84_27480 | AMQ84_00685 | Cation transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Dihydroorotate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.622 |
| KWX71657.1 | cadA | AMQ84_27480 | AMQ84_27490 | Cation transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cadmium transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.413 |
| KWX71657.1 | copA | AMQ84_27480 | AMQ84_27350 | Cation transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase P; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.413 |
| KWX71657.1 | ydbA | AMQ84_27480 | AMQ84_30870 | Cation transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.413 |
| KWX71657.1 | zosA | AMQ84_27480 | AMQ84_11190 | Cation transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.413 |
| KWX71739.1 | KWX76650.1 | AMQ84_27995 | AMQ84_15045 | Cytochrome B; 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.730 |
| KWX71739.1 | KWX76652.1 | AMQ84_27995 | AMQ84_15055 | Cytochrome B; 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 oxidase subunit IV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |
| KWX71739.1 | KWX76653.1 | AMQ84_27995 | AMQ84_15060 | Cytochrome B; 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 B oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KWX71739.1 | KWX76654.1 | AMQ84_27995 | AMQ84_15065 | Cytochrome B; 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| KWX71739.1 | KWX80657.1 | AMQ84_27995 | AMQ84_02885 | Cytochrome B; 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 oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.974 |
| KWX71739.1 | atpA | AMQ84_27995 | AMQ84_22145 | Cytochrome B; 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). | ATP F0F1 synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | 0.624 |
| KWX71739.1 | atpB | AMQ84_27995 | AMQ84_22125 | Cytochrome B; 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). | ATP synthase F0 subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. | 0.836 |
| KWX71739.1 | atpC | AMQ84_27995 | AMQ84_22160 | Cytochrome B; 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). | ATP synthase F1 subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. | 0.606 |
| KWX71739.1 | atpD | AMQ84_27995 | AMQ84_22155 | Cytochrome B; 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). | ATP F0F1 synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.552 |
| KWX71739.1 | atpE | AMQ84_27995 | AMQ84_22130 | Cytochrome B; 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). | ATP synthase F0F1 subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.639 |
| KWX71739.1 | atpG | AMQ84_27995 | AMQ84_22150 | Cytochrome B; 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). | ATP F0F1 synthase subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | 0.816 |
| KWX71739.1 | atpH | AMQ84_27995 | AMQ84_22140 | Cytochrome B; 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). | ATP synthase F0F1 subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.693 |
| KWX71739.1 | ctaD | AMQ84_27995 | AMQ84_28000 | Cytochrome B; 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). | Quinol oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.999 |
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