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 |
| T14G8.3 | T24H7.2 | T14G8.3a.1 | T24H7.2.1 | Uncharacterized protein. | Uncharacterized protein. | 0.919 |
| T14G8.3 | hsp-3 | T14G8.3a.1 | C15H9.6a.5 | Uncharacterized protein. | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.971 |
| T14G8.3 | hsp-4 | T14G8.3a.1 | F43E2.8a.2 | Uncharacterized protein. | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | 0.965 |
| T24H7.2 | T14G8.3 | T24H7.2.1 | T14G8.3a.1 | Uncharacterized protein. | Uncharacterized protein. | 0.919 |
| T24H7.2 | hsp-3 | T24H7.2.1 | C15H9.6a.5 | Uncharacterized protein. | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.950 |
| T24H7.2 | hsp-4 | T24H7.2.1 | F43E2.8a.2 | Uncharacterized protein. | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | 0.946 |
| hsp-3 | T14G8.3 | C15H9.6a.5 | T14G8.3a.1 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | Uncharacterized protein. | 0.971 |
| hsp-3 | T24H7.2 | C15H9.6a.5 | T24H7.2.1 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | Uncharacterized protein. | 0.950 |
| hsp-3 | hsp-4 | C15H9.6a.5 | F43E2.8a.2 | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | 0.913 |
| hsp-4 | T14G8.3 | F43E2.8a.2 | T14G8.3a.1 | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | Uncharacterized protein. | 0.965 |
| hsp-4 | T24H7.2 | F43E2.8a.2 | T24H7.2.1 | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | Uncharacterized protein. | 0.946 |
| hsp-4 | hsp-3 | F43E2.8a.2 | C15H9.6a.5 | Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family. | Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. | 0.913 |