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 |
| SAM1 | SAM2 | YLR180W | YDR502C | S-adenosylmethionine synthase 1; S-adenosylmethionine synthetase; catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; SAM1 has a paralog, SAM2, that arose from the whole genome duplication. | S-adenosylmethionine synthase 2; S-adenosylmethionine synthetase; catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon. | 0.999 |
| SAM1 | SAM3 | YLR180W | YPL274W | S-adenosylmethionine synthase 1; S-adenosylmethionine synthetase; catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; SAM1 has a paralog, SAM2, that arose from the whole genome duplication. | High-affinity S-adenosylmethionine permease; required for utilization of S-adenosylmethionine as a sulfur source; has similarity to S-methylmethionine permease Mmp1p. | 0.727 |
| SAM2 | SAM1 | YDR502C | YLR180W | S-adenosylmethionine synthase 2; S-adenosylmethionine synthetase; catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon. | S-adenosylmethionine synthase 1; S-adenosylmethionine synthetase; catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; SAM1 has a paralog, SAM2, that arose from the whole genome duplication. | 0.999 |
| SAM2 | SAM3 | YDR502C | YPL274W | S-adenosylmethionine synthase 2; S-adenosylmethionine synthetase; catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon. | High-affinity S-adenosylmethionine permease; required for utilization of S-adenosylmethionine as a sulfur source; has similarity to S-methylmethionine permease Mmp1p. | 0.714 |
| SAM3 | SAM1 | YPL274W | YLR180W | High-affinity S-adenosylmethionine permease; required for utilization of S-adenosylmethionine as a sulfur source; has similarity to S-methylmethionine permease Mmp1p. | S-adenosylmethionine synthase 1; S-adenosylmethionine synthetase; catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; SAM1 has a paralog, SAM2, that arose from the whole genome duplication. | 0.727 |
| SAM3 | SAM2 | YPL274W | YDR502C | High-affinity S-adenosylmethionine permease; required for utilization of S-adenosylmethionine as a sulfur source; has similarity to S-methylmethionine permease Mmp1p. | S-adenosylmethionine synthase 2; S-adenosylmethionine synthetase; catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon. | 0.714 |