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 |
purB | secG | Msp_1247 | Msp_0229 | PurB; Adenylosuccinate lyase; COG0015, pfam00206; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. | SecG; Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. | 0.429 |
secE | secG | Msp_1268 | Msp_0229 | Partially conserved hypothetical membrane-spanning protein; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. | SecG; Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. | 0.413 |
secE | secY | Msp_1268 | Msp_0885 | Partially conserved hypothetical membrane-spanning protein; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. | SecY; 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. | 0.934 |
secG | purB | Msp_0229 | Msp_1247 | SecG; Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. | PurB; Adenylosuccinate lyase; COG0015, pfam00206; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. | 0.429 |
secG | secE | Msp_0229 | Msp_1268 | SecG; Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. | Partially conserved hypothetical membrane-spanning protein; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. | 0.413 |
secG | secY | Msp_0229 | Msp_0885 | SecG; Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. | SecY; 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. | 0.413 |
secG | thiC1 | Msp_0229 | Msp_0228 | SecG; Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. | ThiC1; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family. | 0.423 |
secY | secE | Msp_0885 | Msp_1268 | SecY; 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. | Partially conserved hypothetical membrane-spanning protein; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. | 0.934 |
secY | secG | Msp_0885 | Msp_0229 | SecY; 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. | SecG; Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. | 0.413 |
thiC1 | secG | Msp_0228 | Msp_0229 | ThiC1; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family. | SecG; Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. | 0.423 |