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 |
| DVU_0915 | DVU_0989 | DVU_0915 | DVU_0989 | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | Periplasmic divalent cation tolerance protein cutA, putative; Identified by similarity to SP:P36654; match to protein family HMM PF03091. | 0.421 |
| DVU_0915 | atpE | DVU_0915 | DVU_0917 | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | ATP synthase F0, C subunit; 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. | 0.461 |
| DVU_0915 | atpI | DVU_0915 | DVU_0920 | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | ATP synthase protein I; Identified by similarity to SP:P15011. | 0.422 |
| DVU_0915 | cobS | DVU_0915 | DVU_0914 | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | Cobalamin-5-phosphate synthase; Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family. | 0.533 |
| DVU_0915 | rex | DVU_0915 | DVU_0916 | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | AT-rich DNA-binding protein; Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | 0.709 |
| DVU_0989 | DVU_0915 | DVU_0989 | DVU_0915 | Periplasmic divalent cation tolerance protein cutA, putative; Identified by similarity to SP:P36654; match to protein family HMM PF03091. | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | 0.421 |
| atpE | DVU_0915 | DVU_0917 | DVU_0915 | ATP synthase F0, C subunit; 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. | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | 0.461 |
| atpE | atpI | DVU_0917 | DVU_0920 | ATP synthase F0, C subunit; 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. | ATP synthase protein I; Identified by similarity to SP:P15011. | 0.685 |
| atpE | rex | DVU_0917 | DVU_0916 | ATP synthase F0, C subunit; 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. | AT-rich DNA-binding protein; Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | 0.713 |
| atpI | DVU_0915 | DVU_0920 | DVU_0915 | ATP synthase protein I; Identified by similarity to SP:P15011. | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | 0.422 |
| atpI | atpE | DVU_0920 | DVU_0917 | ATP synthase protein I; Identified by similarity to SP:P15011. | ATP synthase F0, C subunit; 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. | 0.685 |
| atpI | rex | DVU_0920 | DVU_0916 | ATP synthase protein I; Identified by similarity to SP:P15011. | AT-rich DNA-binding protein; Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | 0.429 |
| cobS | DVU_0915 | DVU_0914 | DVU_0915 | Cobalamin-5-phosphate synthase; Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family. | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | 0.533 |
| rex | DVU_0915 | DVU_0916 | DVU_0915 | AT-rich DNA-binding protein; Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | Conserved hypothetical protein; Identified by similarity to OMNI:CT1550; match to protein family HMM PF01887. | 0.709 |
| rex | atpE | DVU_0916 | DVU_0917 | AT-rich DNA-binding protein; Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | ATP synthase F0, C subunit; 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. | 0.713 |
| rex | atpI | DVU_0916 | DVU_0920 | AT-rich DNA-binding protein; Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | ATP synthase protein I; Identified by similarity to SP:P15011. | 0.429 |