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 simple tabular text output:
TSV: tab separated values - can be opened in Excel
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... 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 annotated functions of the network proteins
Browse interactions in tabular form:
node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
DR93_12 | DR93_6 | DR93_12 | DR93_6 | Uncharacterized protein | Conserved hypothetical protein | 0.426 |
DR93_12 | DR93_8 | DR93_12 | DR93_8 | Uncharacterized protein | annotation not available | 0.688 |
DR93_12 | DR93_922 | DR93_12 | DR93_922 | Uncharacterized protein | annotation not available | 0.400 |
DR93_12 | dacA | DR93_12 | DR93_7 | Uncharacterized protein | annotation not available | 0.692 |
DR93_12 | lipB | DR93_12 | DR93_5 | Uncharacterized protein | Octanoyltransferase; 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; Belongs to the LipB family | 0.543 |
DR93_12 | mrdA | DR93_12 | DR93_10 | Uncharacterized protein | pbp2_mrdA: penicillin-binding protein 2 | 0.832 |
DR93_12 | mrdB | DR93_12 | DR93_9 | Uncharacterized protein | rodA_shape: rod shape-determining protein RodA; Belongs to the SEDS family | 0.783 |
DR93_12 | rlmH | DR93_12 | DR93_11 | Uncharacterized protein | Ribosomal RNA large subunit methyltransferase H; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family | 0.963 |
DR93_6 | DR93_12 | DR93_6 | DR93_12 | Conserved hypothetical protein | Uncharacterized protein | 0.426 |
DR93_6 | DR93_8 | DR93_6 | DR93_8 | Conserved hypothetical protein | annotation not available | 0.564 |
DR93_6 | DR93_922 | DR93_6 | DR93_922 | Conserved hypothetical protein | annotation not available | 0.791 |
DR93_6 | dacA | DR93_6 | DR93_7 | Conserved hypothetical protein | annotation not available | 0.912 |
DR93_6 | lipB | DR93_6 | DR93_5 | Conserved hypothetical protein | Octanoyltransferase; 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; Belongs to the LipB family | 0.868 |
DR93_6 | mrdA | DR93_6 | DR93_10 | Conserved hypothetical protein | pbp2_mrdA: penicillin-binding protein 2 | 0.880 |
DR93_6 | mrdB | DR93_6 | DR93_9 | Conserved hypothetical protein | rodA_shape: rod shape-determining protein RodA; Belongs to the SEDS family | 0.871 |
DR93_6 | rlmH | DR93_6 | DR93_11 | Conserved hypothetical protein | Ribosomal RNA large subunit methyltransferase H; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA; Belongs to the RNA methyltransferase RlmH family | 0.476 |
DR93_8 | DR93_12 | DR93_8 | DR93_12 | annotation not available | Uncharacterized protein | 0.688 |
DR93_8 | DR93_6 | DR93_8 | DR93_6 | annotation not available | Conserved hypothetical protein | 0.564 |
DR93_8 | dacA | DR93_8 | DR93_7 | annotation not available | annotation not available | 0.828 |
DR93_8 | lipB | DR93_8 | DR93_5 | annotation not available | Octanoyltransferase; 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; Belongs to the LipB family | 0.644 |
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