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 |
CALCOCO1 | CRYBA2 | ENSP00000449960 | ENSP00000295728 | calcium binding and coiled-coil domain 1; Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1- mediated transcriptional activation via its inte [...] | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.506 |
CRYBA2 | CALCOCO1 | ENSP00000295728 | ENSP00000449960 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | calcium binding and coiled-coil domain 1; Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1- mediated transcriptional activation via its inte [...] | 0.506 |
CRYBA2 | CRYBB1 | ENSP00000295728 | ENSP00000215939 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta B1; Crystallins are the dominant structural components of the vertebrate eye lens | 0.602 |
CRYBA2 | CRYBB2 | ENSP00000295728 | ENSP00000381273 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.603 |
CRYBA2 | CRYBB3 | ENSP00000295728 | ENSP00000215855 | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta B3; Crystallins are the dominant structural components of the vertebrate eye lens | 0.603 |
CRYBB1 | CRYBA2 | ENSP00000215939 | ENSP00000295728 | crystallin, beta B1; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.602 |
CRYBB2 | CRYBA2 | ENSP00000381273 | ENSP00000295728 | crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.603 |
CRYBB3 | CRYBA2 | ENSP00000215855 | ENSP00000295728 | crystallin, beta B3; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens | 0.603 |