Export your current network:
... 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 |
| HSP15.7 | HSP90-1 | Q9FHQ3 | P27323 | 15.7 kDa heat shock protein, peroxisomal; Possesses chaperone activity; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein 90-1; Functions as a holding molecular chaperone (holdase) which stabilizes unfolding protein intermediates and rapidly releases them in an active form once stress has abated. Functions as a folding molecular chaperone (foldase) that assists the non-covalent folding of proteins in an ATP-dependent manner. Molecular chaperone involved in R gene-mediated disease resistance. Required for full RPS2- mediated resistance through interaction with RAR1. Possesses probably ATPase activity. | 0.722 |
| HSP90-1 | HSP15.7 | P27323 | Q9FHQ3 | Heat shock protein 90-1; Functions as a holding molecular chaperone (holdase) which stabilizes unfolding protein intermediates and rapidly releases them in an active form once stress has abated. Functions as a folding molecular chaperone (foldase) that assists the non-covalent folding of proteins in an ATP-dependent manner. Molecular chaperone involved in R gene-mediated disease resistance. Required for full RPS2- mediated resistance through interaction with RAR1. Possesses probably ATPase activity. | 15.7 kDa heat shock protein, peroxisomal; Possesses chaperone activity; Belongs to the small heat shock protein (HSP20) family. | 0.722 |