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 |
| ADD67359.1 | ADD67781.1 | Dacet_0561 | Dacet_1005 | Glutaredoxin 2; KEGG: ppd:Ppro_0197 glutaredoxin 2. | Cytochrome c oxidase, subunit II; 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). | 0.750 |
| ADD67359.1 | ADD67785.1 | Dacet_0561 | Dacet_1009 | Glutaredoxin 2; KEGG: ppd:Ppro_0197 glutaredoxin 2. | KEGG: dde:Dde_1822 uncharacterized protein SCO1/SenC/PrrC. | 0.767 |
| ADD67780.1 | ADD67781.1 | Dacet_1004 | Dacet_1005 | PFAM: UbiA prenyltransferase; KEGG: dde:Dde_1827 protoheme IX farnesyltransferase, putative. | Cytochrome c oxidase, subunit II; 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 |
| ADD67780.1 | ADD67782.1 | Dacet_1004 | Dacet_1006 | PFAM: UbiA prenyltransferase; KEGG: dde:Dde_1827 protoheme IX farnesyltransferase, putative. | TIGRFAM: caa(3)-type oxidase, subunit IV; KEGG: dde:Dde_1825 Caa(3)-type oxidase, subunit IV. | 0.993 |
| ADD67780.1 | ADD67783.1 | Dacet_1004 | Dacet_1007 | PFAM: UbiA prenyltransferase; KEGG: dde:Dde_1827 protoheme IX farnesyltransferase, putative. | PFAM: cytochrome c oxidase subunit III; KEGG: dde:Dde_1824 cytochrome c oxidase, subunit III. | 0.999 |
| ADD67780.1 | ADD67784.1 | Dacet_1004 | Dacet_1008 | PFAM: UbiA prenyltransferase; KEGG: dde:Dde_1827 protoheme IX farnesyltransferase, putative. | Cytochrome c 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 |
| ADD67780.1 | ADD67785.1 | Dacet_1004 | Dacet_1009 | PFAM: UbiA prenyltransferase; KEGG: dde:Dde_1827 protoheme IX farnesyltransferase, putative. | KEGG: dde:Dde_1822 uncharacterized protein SCO1/SenC/PrrC. | 0.966 |
| ADD67780.1 | ADD67786.1 | Dacet_1004 | Dacet_1010 | PFAM: UbiA prenyltransferase; KEGG: dde:Dde_1827 protoheme IX farnesyltransferase, putative. | PFAM: cytochrome c class I; KEGG: dvm:DvMF_0538 cytochrome c class I. | 0.757 |
| ADD67781.1 | ADD67359.1 | Dacet_1005 | Dacet_0561 | Cytochrome c oxidase, subunit II; 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). | Glutaredoxin 2; KEGG: ppd:Ppro_0197 glutaredoxin 2. | 0.750 |
| ADD67781.1 | ADD67780.1 | Dacet_1005 | Dacet_1004 | Cytochrome c oxidase, subunit II; 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). | PFAM: UbiA prenyltransferase; KEGG: dde:Dde_1827 protoheme IX farnesyltransferase, putative. | 0.999 |
| ADD67781.1 | ADD67782.1 | Dacet_1005 | Dacet_1006 | Cytochrome c oxidase, subunit II; 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). | TIGRFAM: caa(3)-type oxidase, subunit IV; KEGG: dde:Dde_1825 Caa(3)-type oxidase, subunit IV. | 0.999 |
| ADD67781.1 | ADD67783.1 | Dacet_1005 | Dacet_1007 | Cytochrome c oxidase, subunit II; 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). | PFAM: cytochrome c oxidase subunit III; KEGG: dde:Dde_1824 cytochrome c oxidase, subunit III. | 0.999 |
| ADD67781.1 | ADD67784.1 | Dacet_1005 | Dacet_1008 | Cytochrome c oxidase, subunit II; 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 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 |
| ADD67781.1 | ADD67785.1 | Dacet_1005 | Dacet_1009 | Cytochrome c oxidase, subunit II; 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). | KEGG: dde:Dde_1822 uncharacterized protein SCO1/SenC/PrrC. | 0.997 |
| ADD67781.1 | ADD67786.1 | Dacet_1005 | Dacet_1010 | Cytochrome c oxidase, subunit II; 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). | PFAM: cytochrome c class I; KEGG: dvm:DvMF_0538 cytochrome c class I. | 0.879 |
| ADD67781.1 | ADD68496.1 | Dacet_1005 | Dacet_1732 | Cytochrome c oxidase, subunit II; 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). | PFAM: Thioredoxin domain; KEGG: gsu:GSU2957 thioredoxin family protein. | 0.750 |
| ADD67781.1 | ADD69022.1 | Dacet_1005 | Dacet_2260 | Cytochrome c oxidase, subunit II; 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). | TIGRFAM: redox-active disulfide protein 2; KEGG: ppd:Ppro_0856 redox-active disulfide protein 2. | 0.698 |
| ADD67781.1 | ADD69208.1 | Dacet_1005 | Dacet_2447 | Cytochrome c oxidase, subunit II; 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). | PFAM: Redoxin domain protein; alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; Thioredoxin domain; KEGG: dds:Ddes_1441 redoxin domain protein. | 0.750 |
| ADD67782.1 | ADD67780.1 | Dacet_1006 | Dacet_1004 | TIGRFAM: caa(3)-type oxidase, subunit IV; KEGG: dde:Dde_1825 Caa(3)-type oxidase, subunit IV. | PFAM: UbiA prenyltransferase; KEGG: dde:Dde_1827 protoheme IX farnesyltransferase, putative. | 0.993 |
| ADD67782.1 | ADD67781.1 | Dacet_1006 | Dacet_1005 | TIGRFAM: caa(3)-type oxidase, subunit IV; KEGG: dde:Dde_1825 Caa(3)-type oxidase, subunit IV. | Cytochrome c oxidase, subunit II; 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 |
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