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 |
SDN87383.1 | SDO03319.1 | SAMN04487957_102243 | SAMN04487957_103113 | Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | Heat shock protein HtpX. | 0.416 |
SDN87383.1 | htpX | SAMN04487957_102243 | SAMN04487957_108104 | Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | Heat shock protein. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.416 |
SDN89227.1 | SDO03319.1 | SAMN04487957_102298 | SAMN04487957_103113 | Putative thioredoxin. | Heat shock protein HtpX. | 0.419 |
SDN89227.1 | dnaJ | SAMN04487957_102298 | SAMN04487957_106161 | Putative thioredoxin. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | 0.775 |
SDN89227.1 | ftsH | SAMN04487957_102298 | SAMN04487957_106171 | Putative thioredoxin. | Membrane protease FtsH catalytic subunit; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.440 |
SDN89227.1 | grpE | SAMN04487957_102298 | SAMN04487957_106159 | Putative thioredoxin. | Molecular chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...] | 0.855 |
SDN89227.1 | htpX | SAMN04487957_102298 | SAMN04487957_108104 | Putative thioredoxin. | Heat shock protein. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.419 |
SDN94900.1 | SDO03319.1 | SAMN04487957_102478 | SAMN04487957_103113 | Glycosyl transferase family 2. | Heat shock protein HtpX. | 0.401 |
SDO02563.1 | SDO03319.1 | SAMN04487957_10392 | SAMN04487957_103113 | Protein-S-isoprenylcysteine O-methyltransferase Ste14. | Heat shock protein HtpX. | 0.444 |
SDO02563.1 | htpX | SAMN04487957_10392 | SAMN04487957_108104 | Protein-S-isoprenylcysteine O-methyltransferase Ste14. | Heat shock protein. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.444 |
SDO03319.1 | SDN87383.1 | SAMN04487957_103113 | SAMN04487957_102243 | Heat shock protein HtpX. | Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. | 0.416 |
SDO03319.1 | SDN89227.1 | SAMN04487957_103113 | SAMN04487957_102298 | Heat shock protein HtpX. | Putative thioredoxin. | 0.419 |
SDO03319.1 | SDN94900.1 | SAMN04487957_103113 | SAMN04487957_102478 | Heat shock protein HtpX. | Glycosyl transferase family 2. | 0.401 |
SDO03319.1 | SDO02563.1 | SAMN04487957_103113 | SAMN04487957_10392 | Heat shock protein HtpX. | Protein-S-isoprenylcysteine O-methyltransferase Ste14. | 0.444 |
SDO03319.1 | SDO21610.1 | SAMN04487957_103113 | SAMN04487957_104276 | Heat shock protein HtpX. | LemA protein. | 0.465 |
SDO03319.1 | dnaJ | SAMN04487957_103113 | SAMN04487957_106161 | Heat shock protein HtpX. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | 0.462 |
SDO03319.1 | ftsH | SAMN04487957_103113 | SAMN04487957_106171 | Heat shock protein HtpX. | Membrane protease FtsH catalytic subunit; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.446 |
SDO03319.1 | grpE | SAMN04487957_103113 | SAMN04487957_106159 | Heat shock protein HtpX. | Molecular chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP [...] | 0.410 |
SDO03319.1 | htpX | SAMN04487957_103113 | SAMN04487957_108104 | Heat shock protein HtpX. | Heat shock protein. Metallo peptidase. MEROPS family M48B; Belongs to the peptidase M48B family. | 0.746 |
SDO03319.1 | secY | SAMN04487957_103113 | SAMN04487957_11360 | Heat shock protein HtpX. | Protein translocase subunit secY/sec61 alpha; 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. | 0.428 |
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