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 |
| atpB | atpE | wcw_1122 | wcw_1123 | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Putative F-type ATP synthase, 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. | 0.999 |
| atpB | fni | wcw_1122 | wcw_1116 | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Isopentenyl-diphosphate delta-isomerase; Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). | 0.703 |
| atpB | mvaA | wcw_1122 | wcw_1117 | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Hydroxymethylglutaryl-CoA reductase; Belongs to the HMG-CoA reductase family. | 0.682 |
| atpB | mvaK2 | wcw_1122 | wcw_1119 | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Putative phosphomevalonate kinase; Galactokinase. | 0.682 |
| atpB | wcw_1115 | wcw_1122 | wcw_1115 | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Putative hydroxymethylglutaryl-CoA synthase; 3-oxoacyl-[acyl-carrier-protein] synthase III. | 0.682 |
| atpB | wcw_1118 | wcw_1122 | wcw_1118 | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Putative diphosphomevalonate decarboxylase; Mevalonate pyrophosphate decarboxylase. | 0.682 |
| atpB | wcw_1120 | wcw_1122 | wcw_1120 | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Mevalonate kinase. | 0.682 |
| atpB | wcw_1121 | wcw_1122 | wcw_1121 | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Putative membrane protein. | 0.832 |
| atpE | atpB | wcw_1123 | wcw_1122 | Putative F-type ATP synthase, 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. | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 0.999 |
| atpE | fni | wcw_1123 | wcw_1116 | Putative F-type ATP synthase, 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. | Isopentenyl-diphosphate delta-isomerase; Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). | 0.672 |
| atpE | mvaA | wcw_1123 | wcw_1117 | Putative F-type ATP synthase, 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. | Hydroxymethylglutaryl-CoA reductase; Belongs to the HMG-CoA reductase family. | 0.672 |
| atpE | mvaK2 | wcw_1123 | wcw_1119 | Putative F-type ATP synthase, 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. | Putative phosphomevalonate kinase; Galactokinase. | 0.672 |
| atpE | wcw_1115 | wcw_1123 | wcw_1115 | Putative F-type ATP synthase, 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. | Putative hydroxymethylglutaryl-CoA synthase; 3-oxoacyl-[acyl-carrier-protein] synthase III. | 0.687 |
| atpE | wcw_1118 | wcw_1123 | wcw_1118 | Putative F-type ATP synthase, 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. | Putative diphosphomevalonate decarboxylase; Mevalonate pyrophosphate decarboxylase. | 0.695 |
| atpE | wcw_1120 | wcw_1123 | wcw_1120 | Putative F-type ATP synthase, 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. | Mevalonate kinase. | 0.672 |
| atpE | wcw_1121 | wcw_1123 | wcw_1121 | Putative F-type ATP synthase, 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. | Putative membrane protein. | 0.803 |
| crtE | fni | wcw_1169 | wcw_1116 | Farnesyltranstransferase; Geranylgeranyl pyrophosphate synthase; Belongs to the FPP/GGPP synthase family. | Isopentenyl-diphosphate delta-isomerase; Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). | 0.916 |
| crtE | ispA | wcw_1169 | wcw_0012 | Farnesyltranstransferase; Geranylgeranyl pyrophosphate synthase; Belongs to the FPP/GGPP synthase family. | Putative geranyltranstransferase; Geranylgeranyl pyrophosphate synthase; Belongs to the FPP/GGPP synthase family. | 0.924 |
| crtE | wcw_1118 | wcw_1169 | wcw_1118 | Farnesyltranstransferase; Geranylgeranyl pyrophosphate synthase; Belongs to the FPP/GGPP synthase family. | Putative diphosphomevalonate decarboxylase; Mevalonate pyrophosphate decarboxylase. | 0.934 |
| fni | atpB | wcw_1116 | wcw_1122 | Isopentenyl-diphosphate delta-isomerase; Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). | F-type ATP synthase, subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | 0.703 |
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