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 |
| Bfsp1 | Bfsp2 | ENSRNOP00000007727 | ENSRNOP00000029527 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA. | 0.952 |
| Bfsp1 | Cryaa | ENSRNOP00000007727 | ENSRNOP00000065714 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Alpha-crystallin A(1-151); 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). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. Belongs to the small heat shock protein (HSP20) family. | 0.791 |
| Bfsp1 | Cryab | ENSRNOP00000007727 | ENSRNOP00000055901 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (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; Belongs to the small heat shock protein (HSP20) family. | 0.712 |
| Bfsp1 | Cryga-2 | ENSRNOP00000007727 | ENSRNOP00000074559 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Gamma-crystallin A. | 0.592 |
| Bfsp1 | Crygb | ENSRNOP00000007727 | ENSRNOP00000043562 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Gamma-crystallin B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.659 |
| Bfsp1 | Crygf | ENSRNOP00000007727 | ENSRNOP00000045818 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Gamma-crystallin F; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.613 |
| Bfsp1 | Grifin | ENSRNOP00000007727 | ENSRNOP00000001686 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Grifin. | 0.598 |
| Bfsp2 | Bfsp1 | ENSRNOP00000029527 | ENSRNOP00000007727 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA. | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | 0.952 |
| Bfsp2 | Cryaa | ENSRNOP00000029527 | ENSRNOP00000065714 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA. | Alpha-crystallin A(1-151); 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). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. Belongs to the small heat shock protein (HSP20) family. | 0.693 |
| Bfsp2 | Cryab | ENSRNOP00000029527 | ENSRNOP00000055901 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA. | 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; Belongs to the small heat shock protein (HSP20) family. | 0.597 |
| Bfsp2 | Cryga-2 | ENSRNOP00000029527 | ENSRNOP00000074559 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA. | Gamma-crystallin A. | 0.653 |
| Bfsp2 | Crygb | ENSRNOP00000029527 | ENSRNOP00000043562 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA. | Gamma-crystallin B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.612 |
| Bfsp2 | Crygf | ENSRNOP00000029527 | ENSRNOP00000045818 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA. | Gamma-crystallin F; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.612 |
| Bfsp2 | Grifin | ENSRNOP00000029527 | ENSRNOP00000001686 | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA. | Grifin. | 0.590 |
| Cryaa | Bfsp1 | ENSRNOP00000065714 | ENSRNOP00000007727 | Alpha-crystallin A(1-151); 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). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. Belongs to the small heat shock protein (HSP20) family. | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | 0.791 |
| Cryaa | Bfsp2 | ENSRNOP00000065714 | ENSRNOP00000029527 | Alpha-crystallin A(1-151); 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). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. Belongs to the small heat shock protein (HSP20) family. | Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2, AND CRYAA. | 0.693 |
| Cryaa | Cryab | ENSRNOP00000065714 | ENSRNOP00000055901 | Alpha-crystallin A(1-151); 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). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. 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; Belongs to the small heat shock protein (HSP20) family. | 0.991 |
| Cryaa | Cryga-2 | ENSRNOP00000065714 | ENSRNOP00000074559 | Alpha-crystallin A(1-151); 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). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. Belongs to the small heat shock protein (HSP20) family. | Gamma-crystallin A. | 0.673 |
| Cryaa | Crygb | ENSRNOP00000065714 | ENSRNOP00000043562 | Alpha-crystallin A(1-151); 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). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. Belongs to the small heat shock protein (HSP20) family. | Gamma-crystallin B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.880 |
| Cryaa | Crygf | ENSRNOP00000065714 | ENSRNOP00000045818 | Alpha-crystallin A(1-151); 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). C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity. Belongs to the small heat shock protein (HSP20) family. | Gamma-crystallin F; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.692 |
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