Export your current network:
... as a bitmap image:
file format is 'PNG': portable network graphic
... as a high-resolution bitmap:
same PNG format, but resolution at 400 dpi
... 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 |
CUL4A | DCAF15 | ENSP00000364589 | ENSP00000254337 | cullin 4A; Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on [...] | DDB1 and CUL4 associated factor 15; May be involved in ubiquitination and degradation through a DBB1-CUL4 E3 protein-ubiquitin ligase | 0.515 |
DCAF15 | CUL4A | ENSP00000254337 | ENSP00000364589 | DDB1 and CUL4 associated factor 15; May be involved in ubiquitination and degradation through a DBB1-CUL4 E3 protein-ubiquitin ligase | cullin 4A; Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on [...] | 0.515 |