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 |
DES48_101225 | DES48_10419 | GCA_900168775_02092 | GCA_900168775_02210 | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Unannotated protein. | 0.586 |
DES48_101225 | GCA_900168775_03544 | GCA_900168775_02092 | GCA_900168775_03544 | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Unannotated protein. | 0.612 |
DES48_101225 | dnaJ | GCA_900168775_02092 | GCA_900168775_02457 | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Unannotated protein; 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, DnaK [...] | 0.916 |
DES48_101225 | dnaK | GCA_900168775_02092 | GCA_900168775_02456 | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Unannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.660 |
DES48_101225 | htpG | GCA_900168775_02092 | GCA_900168775_01736 | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Unannotated protein; Molecular chaperone. Has ATPase activity. | 0.930 |
DES48_101225 | rplK | GCA_900168775_02092 | GCA_900168775_03226 | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Unannotated protein; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.852 |
DES48_101225 | rplN | GCA_900168775_02092 | GCA_900168775_03199 | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Unannotated protein; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.818 |
DES48_101225 | rplQ | GCA_900168775_02092 | GCA_900168775_03181 | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Unannotated protein. | 0.864 |
DES48_10419 | DES48_101225 | GCA_900168775_02210 | GCA_900168775_02092 | Unannotated protein. | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.586 |
DES48_10419 | GCA_900168775_03544 | GCA_900168775_02210 | GCA_900168775_03544 | Unannotated protein. | Unannotated protein. | 0.689 |
DES48_10419 | dnaJ | GCA_900168775_02210 | GCA_900168775_02457 | Unannotated protein. | Unannotated protein; 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, DnaK [...] | 0.909 |
DES48_10419 | dnaK | GCA_900168775_02210 | GCA_900168775_02456 | Unannotated protein. | Unannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.689 |
DES48_10419 | groL | GCA_900168775_02210 | GCA_900168775_02180 | Unannotated protein. | Unannotated protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.445 |
DES48_10419 | htpG | GCA_900168775_02210 | GCA_900168775_01736 | Unannotated protein. | Unannotated protein; Molecular chaperone. Has ATPase activity. | 0.543 |
DES48_10419 | rplK | GCA_900168775_02210 | GCA_900168775_03226 | Unannotated protein. | Unannotated protein; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.767 |
DES48_10419 | rplN | GCA_900168775_02210 | GCA_900168775_03199 | Unannotated protein. | Unannotated protein; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family. | 0.605 |
GCA_900168775_03544 | DES48_101225 | GCA_900168775_03544 | GCA_900168775_02092 | Unannotated protein. | Unannotated protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.612 |
GCA_900168775_03544 | DES48_10419 | GCA_900168775_03544 | GCA_900168775_02210 | Unannotated protein. | Unannotated protein. | 0.689 |
GCA_900168775_03544 | dnaJ | GCA_900168775_03544 | GCA_900168775_02457 | Unannotated protein. | Unannotated protein; 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, DnaK [...] | 0.980 |
GCA_900168775_03544 | groL | GCA_900168775_03544 | GCA_900168775_02180 | Unannotated protein. | Unannotated protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.927 |
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