Export your current network:
... as a bitmap image:
file format is 'PNG': portable network graphic
... as a high-resolution bitmap:
same PNG format, but at higher resolution
... 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 |
ACO77089.1 | ACO77092.1 | Avin_08440 | Avin_08470 | Conserved hypothetical protein; Belongs to the UPF0250 family. | Hypothetical protein. | 0.752 |
ACO77089.1 | ACO77093.1 | Avin_08440 | Avin_08480 | Conserved hypothetical protein; Belongs to the UPF0250 family. | Thiamine diphosphate-dependent enzyme; Belongs to the TPP enzyme family. | 0.752 |
ACO77089.1 | lipA | Avin_08440 | Avin_08460 | Conserved hypothetical protein; Belongs to the UPF0250 family. | Lipoic acid synthetase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.848 |
ACO77089.1 | lipB | Avin_08440 | Avin_08450 | Conserved hypothetical protein; Belongs to the UPF0250 family. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.887 |
ACO77092.1 | ACO77089.1 | Avin_08470 | Avin_08440 | Hypothetical protein. | Conserved hypothetical protein; Belongs to the UPF0250 family. | 0.752 |
ACO77092.1 | ACO77093.1 | Avin_08470 | Avin_08480 | Hypothetical protein. | Thiamine diphosphate-dependent enzyme; Belongs to the TPP enzyme family. | 0.773 |
ACO77092.1 | lipA | Avin_08470 | Avin_08460 | Hypothetical protein. | Lipoic acid synthetase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.752 |
ACO77092.1 | lipB | Avin_08470 | Avin_08450 | Hypothetical protein. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.752 |
ACO77093.1 | ACO77089.1 | Avin_08480 | Avin_08440 | Thiamine diphosphate-dependent enzyme; Belongs to the TPP enzyme family. | Conserved hypothetical protein; Belongs to the UPF0250 family. | 0.752 |
ACO77093.1 | ACO77092.1 | Avin_08480 | Avin_08470 | Thiamine diphosphate-dependent enzyme; Belongs to the TPP enzyme family. | Hypothetical protein. | 0.773 |
ACO77093.1 | lipA | Avin_08480 | Avin_08460 | Thiamine diphosphate-dependent enzyme; Belongs to the TPP enzyme family. | Lipoic acid synthetase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.752 |
ACO77093.1 | lipB | Avin_08480 | Avin_08450 | Thiamine diphosphate-dependent enzyme; Belongs to the TPP enzyme family. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.752 |
ACO80525.1 | bioH | Avin_44040 | Avin_06000 | FabI-like dehydrogenase/reductase. | Biotin biosynthesis protein BioH. | 0.910 |
ACO80525.1 | fabB | Avin_44040 | Avin_29060 | FabI-like dehydrogenase/reductase. | 3-oxoacyl-(acyl-carrier-protein) synthase, FabB; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. | 0.974 |
ACO80525.1 | fabF | Avin_44040 | Avin_14940 | FabI-like dehydrogenase/reductase. | Beta-ketoacyl-acyl carrier protein synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.981 |
ACO80525.1 | fabI | Avin_44040 | Avin_29690 | FabI-like dehydrogenase/reductase. | NADH-dependent enoyl-ACP reductase. | 0.909 |
ACO80525.1 | lipB | Avin_44040 | Avin_08450 | FabI-like dehydrogenase/reductase. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.800 |
bioH | ACO80525.1 | Avin_06000 | Avin_44040 | Biotin biosynthesis protein BioH. | FabI-like dehydrogenase/reductase. | 0.910 |
bioH | fabI | Avin_06000 | Avin_29690 | Biotin biosynthesis protein BioH. | NADH-dependent enoyl-ACP reductase. | 0.910 |
bioH | lipB | Avin_06000 | Avin_08450 | Biotin biosynthesis protein BioH. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.753 |
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