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 |
| F933_02024 | F933_02025 | GCA_000931715_00896 | GCA_000931715_00895 | Unannotated protein; Belongs to the LOG family. | Unannotated protein. | 0.650 |
| F933_02024 | F933_02026 | GCA_000931715_00896 | GCA_000931715_00894 | Unannotated protein; Belongs to the LOG family. | Unannotated protein. | 0.600 |
| F933_02025 | F933_02024 | GCA_000931715_00895 | GCA_000931715_00896 | Unannotated protein. | Unannotated protein; Belongs to the LOG family. | 0.650 |
| F933_02025 | F933_02026 | GCA_000931715_00895 | GCA_000931715_00894 | Unannotated protein. | Unannotated protein. | 0.738 |
| F933_02025 | F933_02027 | GCA_000931715_00895 | GCA_000931715_00893 | Unannotated protein. | Unannotated protein. | 0.434 |
| F933_02026 | F933_02024 | GCA_000931715_00894 | GCA_000931715_00896 | Unannotated protein. | Unannotated protein; Belongs to the LOG family. | 0.600 |
| F933_02026 | F933_02025 | GCA_000931715_00894 | GCA_000931715_00895 | Unannotated protein. | Unannotated protein. | 0.738 |
| F933_02026 | F933_02027 | GCA_000931715_00894 | GCA_000931715_00893 | Unannotated protein. | Unannotated protein. | 0.625 |
| F933_02026 | F933_02028 | GCA_000931715_00894 | GCA_000931715_00892 | Unannotated protein. | Unannotated protein. | 0.541 |
| F933_02026 | ffh | GCA_000931715_00894 | GCA_000931715_01858 | Unannotated protein. | Unannotated protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components; Belongs to t [...] | 0.436 |
| F933_02026 | secY | GCA_000931715_00894 | GCA_000931715_00613 | Unannotated protein. | Unannotated protein; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.493 |
| F933_02027 | F933_02025 | GCA_000931715_00893 | GCA_000931715_00895 | Unannotated protein. | Unannotated protein. | 0.434 |
| F933_02027 | F933_02026 | GCA_000931715_00893 | GCA_000931715_00894 | Unannotated protein. | Unannotated protein. | 0.625 |
| F933_02027 | F933_02028 | GCA_000931715_00893 | GCA_000931715_00892 | Unannotated protein. | Unannotated protein. | 0.678 |
| F933_02028 | F933_02026 | GCA_000931715_00892 | GCA_000931715_00894 | Unannotated protein. | Unannotated protein. | 0.541 |
| F933_02028 | F933_02027 | GCA_000931715_00892 | GCA_000931715_00893 | Unannotated protein. | Unannotated protein. | 0.678 |
| ffh | F933_02026 | GCA_000931715_01858 | GCA_000931715_00894 | Unannotated protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components; Belongs to t [...] | Unannotated protein. | 0.436 |
| ffh | secY | GCA_000931715_01858 | GCA_000931715_00613 | Unannotated protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components; Belongs to t [...] | Unannotated protein; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | 0.977 |
| secY | F933_02026 | GCA_000931715_00613 | GCA_000931715_00894 | Unannotated protein; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | Unannotated protein. | 0.493 |
| secY | ffh | GCA_000931715_00613 | GCA_000931715_01858 | Unannotated protein; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. | Unannotated protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components; Belongs to t [...] | 0.977 |
