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 |
| Cryaa | Cryab | ENSMUSP00000019192 | ENSMUSP00000149803 | Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | 0.993 |
| Cryab | Cryaa | ENSMUSP00000149803 | ENSMUSP00000019192 | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | 0.993 |
| Cryab | Hspb2 | ENSMUSP00000149803 | ENSMUSP00000042374 | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | Heat shock protein beta-2; May regulate the kinase DMPK; Belongs to the small heat shock protein (HSP20) family. | 0.842 |
| Cryab | Hspb6 | ENSMUSP00000149803 | ENSMUSP00000039172 | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | Heat shock protein beta-6; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. | 0.782 |
| Hspb2 | Cryab | ENSMUSP00000042374 | ENSMUSP00000149803 | Heat shock protein beta-2; May regulate the kinase DMPK; Belongs to the small heat shock protein (HSP20) family. | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | 0.842 |
| Hspb6 | Cryab | ENSMUSP00000039172 | ENSMUSP00000149803 | Heat shock protein beta-6; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | 0.782 |