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 |
ABCC8 | CRYBB1 | ENSP00000374467 | ENSP00000215939 | ATP-binding cassette, sub-family C (CFTR/MRP), member 8; Putative subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive K(+) channels and insulin release | crystallin, beta B1; Crystallins are the dominant structural components of the vertebrate eye lens | 0.576 |
CRYBA1 | CRYBB1 | ENSP00000225387 | ENSP00000215939 | crystallin, beta A1; 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 | 0.947 |
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 |
CRYBA4 | CRYBB1 | ENSP00000346805 | ENSP00000215939 | crystallin, beta A4; 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 | 0.629 |
CRYBB1 | ABCC8 | ENSP00000215939 | ENSP00000374467 | crystallin, beta B1; Crystallins are the dominant structural components of the vertebrate eye lens | ATP-binding cassette, sub-family C (CFTR/MRP), member 8; Putative subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive K(+) channels and insulin release | 0.576 |
CRYBB1 | CRYBA1 | ENSP00000215939 | ENSP00000225387 | crystallin, beta B1; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta A1; Crystallins are the dominant structural components of the vertebrate eye lens | 0.947 |
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 |
CRYBB1 | CRYBA4 | ENSP00000215939 | ENSP00000346805 | crystallin, beta B1; Crystallins are the dominant structural components of the vertebrate eye lens | crystallin, beta A4; Crystallins are the dominant structural components of the vertebrate eye lens | 0.629 |
TERF1 | TERF2IP | ENSP00000276603 | ENSP00000300086 | telomeric repeat binding factor (NIMA-interacting) 1; Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double- stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair [...] | telomeric repeat binding factor 2, interacting protein; Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR [...] | 0.989 |
TERF2IP | TERF1 | ENSP00000300086 | ENSP00000276603 | telomeric repeat binding factor 2, interacting protein; Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR [...] | telomeric repeat binding factor (NIMA-interacting) 1; Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double- stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair [...] | 0.989 |