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 |
CVI75185.1 | CVI75579.1 | AWB65_00486 | AWB65_00642 | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c-555 precursor. | 0.884 |
CVI75185.1 | CVI79294.1 | AWB65_00486 | AWB65_02498 | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Di-heme cytochrome c peroxidase. | 0.585 |
CVI75185.1 | CVI81493.1 | AWB65_00486 | AWB65_03582 | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c, class I. | 0.892 |
CVI75185.1 | CVI81633.1 | AWB65_00486 | AWB65_03657 | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Glutamate synthase. | 0.835 |
CVI75185.1 | CVI82435.1 | AWB65_00486 | AWB65_04055 | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Pyochelin synthetase. | 0.820 |
CVI75185.1 | CVI82939.1 | AWB65_00486 | AWB65_04304 | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Class I cytochrome c. | 0.892 |
CVI75185.1 | CVI83434.1 | AWB65_00486 | AWB65_04552 | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c, class I. | 0.898 |
CVI75185.1 | CVI83915.1 | AWB65_00486 | AWB65_04784 | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c, class I. | 0.884 |
CVI75185.1 | CVI85814.1 | AWB65_00486 | AWB65_06100 | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Hypothetical protein. | 0.750 |
CVI75579.1 | CVI75185.1 | AWB65_00642 | AWB65_00486 | Cytochrome c-555 precursor. | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.884 |
CVI75579.1 | CVI81633.1 | AWB65_00642 | AWB65_03657 | Cytochrome c-555 precursor. | Glutamate synthase. | 0.707 |
CVI75579.1 | CVI85814.1 | AWB65_00642 | AWB65_06100 | Cytochrome c-555 precursor. | Hypothetical protein. | 0.714 |
CVI79294.1 | CVI75185.1 | AWB65_02498 | AWB65_00486 | Di-heme cytochrome c peroxidase. | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.585 |
CVI79294.1 | CVI83914.1 | AWB65_02498 | AWB65_04783 | Di-heme cytochrome c peroxidase. | Amine dehydrogenase; Belongs to the aromatic amine dehydrogenase light chain family. | 0.953 |
CVI79294.1 | CVI83915.1 | AWB65_02498 | AWB65_04784 | Di-heme cytochrome c peroxidase. | Cytochrome c, class I. | 0.470 |
CVI79294.1 | CVI85814.1 | AWB65_02498 | AWB65_06100 | Di-heme cytochrome c peroxidase. | Hypothetical protein. | 0.908 |
CVI81493.1 | CVI75185.1 | AWB65_03582 | AWB65_00486 | Cytochrome c, class I. | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.892 |
CVI81493.1 | CVI81633.1 | AWB65_03582 | AWB65_03657 | Cytochrome c, class I. | Glutamate synthase. | 0.707 |
CVI81493.1 | CVI85814.1 | AWB65_03582 | AWB65_06100 | Cytochrome c, class I. | Hypothetical protein. | 0.714 |
CVI81633.1 | CVI75185.1 | AWB65_03657 | AWB65_00486 | Glutamate synthase. | Cytochrome c oxidase; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.835 |
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