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 |
| AMO66794.1 | AMO66795.1 | AZF00_00090 | AZF00_00095 | 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 oxidase subunit I; 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 |
| AMO66794.1 | AMO66796.1 | AZF00_00090 | AZF00_00100 | 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 oxidase assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.991 |
| AMO66794.1 | AMO66797.1 | AZF00_00090 | AZF00_00105 | 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). | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
| AMO66794.1 | AMO66799.1 | AZF00_00090 | AZF00_00115 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.902 |
| AMO66794.1 | AMO66800.1 | AZF00_00090 | AZF00_00120 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.897 |
| AMO66794.1 | AMO66801.1 | AZF00_00090 | AZF00_00125 | 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). | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.913 |
| AMO66794.1 | AMO66803.1 | AZF00_00090 | AZF00_00135 | 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). | Electron transporter SenC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.821 |
| AMO66794.1 | AMO68867.1 | AZF00_00090 | AZF00_11395 | 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 oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.980 |
| AMO66794.1 | AMO69316.1 | AZF00_00090 | AZF00_13815 | 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). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.626 |
| AMO66794.1 | cyoE | AZF00_00090 | AZF00_00130 | 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). | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.982 |
| AMO66795.1 | AMO66794.1 | AZF00_00095 | AZF00_00090 | Cytochrome oxidase subunit I; 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. | 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). | 0.999 |
| AMO66795.1 | AMO66796.1 | AZF00_00095 | AZF00_00100 | Cytochrome oxidase subunit I; 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. | Cytochrome C oxidase assembly protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.946 |
| AMO66795.1 | AMO66797.1 | AZF00_00095 | AZF00_00105 | Cytochrome oxidase subunit I; 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. | MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
| AMO66795.1 | AMO66799.1 | AZF00_00095 | AZF00_00115 | Cytochrome oxidase subunit I; 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.714 |
| AMO66795.1 | AMO66800.1 | AZF00_00095 | AZF00_00120 | Cytochrome oxidase subunit I; 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.567 |
| AMO66795.1 | AMO66801.1 | AZF00_00095 | AZF00_00125 | Cytochrome oxidase subunit I; 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. | Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.807 |
| AMO66795.1 | AMO66803.1 | AZF00_00095 | AZF00_00135 | Cytochrome oxidase subunit I; 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. | Electron transporter SenC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.419 |
| AMO66795.1 | AMO68867.1 | AZF00_00095 | AZF00_11395 | Cytochrome oxidase subunit I; 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. | Cytochrome-c oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| AMO66795.1 | AMO69316.1 | AZF00_00095 | AZF00_13815 | Cytochrome oxidase subunit I; 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.485 |
| AMO66795.1 | cyoE | AZF00_00095 | AZF00_00130 | Cytochrome oxidase subunit I; 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. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.972 |
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