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 |
AGOS_AAL008W | AGOS_AEL224W | Q75ET2 | Q758I6 | AAL008Wp. | AEL224Wp. | 0.927 |
AGOS_AAL008W | AGOS_AER187W | Q75ET2 | Q756R7 | AAL008Wp. | AER187Wp; Belongs to the heat shock protein 70 family. | 0.813 |
AGOS_AAL008W | AGOS_AFR114W | Q75ET2 | Q754F6 | AAL008Wp. | AFR114Wp; Belongs to the heat shock protein 70 family. | 0.812 |
AGOS_AAL008W | AGOS_AGL339C | Q75ET2 | Q751R5 | AAL008Wp. | AGL339Cp. | 0.507 |
AGOS_AAL008W | AGOS_AGR352C | Q75ET2 | Q74Z54 | AAL008Wp. | AGR352Cp. | 0.588 |
AGOS_AAL008W | HSP82 | Q75ET2 | Q8J2M3 | AAL008Wp. | Heat shock protein HSP82; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity); Belongs to the heat shock protein 90 family. | 0.810 |
AGOS_AAL008W | KAR2 | Q75ET2 | Q75C78 | AAL008Wp. | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | 0.844 |
AGOS_AAL008W | SSB1 | Q75ET2 | Q75E44 | AAL008Wp. | Ribosome-associated molecular chaperone SSB1; Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation- prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP- [...] | 0.810 |
AGOS_ACL184C | AGOS_AER187W | Q75CV0 | Q756R7 | ACL184Cp. | AER187Wp; Belongs to the heat shock protein 70 family. | 0.443 |
AGOS_ACL184C | AGOS_AFR114W | Q75CV0 | Q754F6 | ACL184Cp. | AFR114Wp; Belongs to the heat shock protein 70 family. | 0.443 |
AGOS_ACL184C | RPL3 | Q75CV0 | Q759R7 | ACL184Cp. | 60S ribosomal protein L3. | 0.999 |
AGOS_ACL184C | SSB1 | Q75CV0 | Q75E44 | ACL184Cp. | Ribosome-associated molecular chaperone SSB1; Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation- prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP- [...] | 0.809 |
AGOS_AEL224W | AGOS_AAL008W | Q758I6 | Q75ET2 | AEL224Wp. | AAL008Wp. | 0.927 |
AGOS_AEL224W | AGOS_AER187W | Q758I6 | Q756R7 | AEL224Wp. | AER187Wp; Belongs to the heat shock protein 70 family. | 0.852 |
AGOS_AEL224W | AGOS_AFR114W | Q758I6 | Q754F6 | AEL224Wp. | AFR114Wp; Belongs to the heat shock protein 70 family. | 0.852 |
AGOS_AEL224W | HSP82 | Q758I6 | Q8J2M3 | AEL224Wp. | Heat shock protein HSP82; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity); Belongs to the heat shock protein 90 family. | 0.966 |
AGOS_AEL224W | KAR2 | Q758I6 | Q75C78 | AEL224Wp. | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | 0.560 |
AGOS_AEL224W | SSB1 | Q758I6 | Q75E44 | AEL224Wp. | Ribosome-associated molecular chaperone SSB1; Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation- prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP- [...] | 0.852 |
AGOS_AER187W | AGOS_AAL008W | Q756R7 | Q75ET2 | AER187Wp; Belongs to the heat shock protein 70 family. | AAL008Wp. | 0.813 |
AGOS_AER187W | AGOS_ACL184C | Q756R7 | Q75CV0 | AER187Wp; Belongs to the heat shock protein 70 family. | ACL184Cp. | 0.443 |
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