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 | ENSMUSP00000096899 | ENSMUSP00000116249 | 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. | 0.847 |
| Bfsp1 | Cryaa | ENSMUSP00000096899 | ENSMUSP00000019192 | 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 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). | 0.834 |
| Bfsp1 | Cryab | ENSMUSP00000096899 | ENSMUSP00000149803 | 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. | 0.703 |
| Bfsp1 | Cryba1 | ENSMUSP00000096899 | ENSMUSP00000077693 | 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). | Beta-crystallin A1; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.810 |
| Bfsp1 | Cryba2 | ENSMUSP00000096899 | ENSMUSP00000006721 | 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). | Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.806 |
| Bfsp1 | Cryba4 | ENSMUSP00000096899 | ENSMUSP00000108004 | 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). | Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.747 |
| Bfsp1 | Crybb1 | ENSMUSP00000096899 | ENSMUSP00000031286 | 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). | Beta-crystallin B1B; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.776 |
| Bfsp1 | Crybb2 | ENSMUSP00000096899 | ENSMUSP00000107955 | 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). | Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.747 |
| Bfsp1 | Crybb3 | ENSMUSP00000096899 | ENSMUSP00000112618 | 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). | Beta-crystallin B3, N-terminally processed; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.769 |
| Bfsp1 | Cryga | ENSMUSP00000096899 | ENSMUSP00000058548 | 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; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.648 |
| Bfsp1 | Crygb | ENSMUSP00000096899 | ENSMUSP00000027090 | 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. | 0.662 |
| Bfsp1 | Crygc | ENSMUSP00000096899 | ENSMUSP00000109698 | 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 C; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.674 |
| Bfsp1 | Crygd | ENSMUSP00000096899 | ENSMUSP00000045327 | 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 D; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. | 0.764 |
| Bfsp1 | Cryge | ENSMUSP00000096899 | ENSMUSP00000084617 | 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 E; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.530 |
| Bfsp1 | Crygf | ENSMUSP00000096899 | ENSMUSP00000027082 | 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; Belongs to the beta/gamma-crystallin family. | 0.593 |
| Bfsp1 | Crygn | ENSMUSP00000096899 | ENSMUSP00000035860 | 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 N; Crystallins are the dominant structural components of the vertebrate eye lens (Probable). Plays also an important role for integrity and function of auditory nuclei. Belongs to the beta/gamma-crystallin family. | 0.535 |
| Bfsp1 | Crygs | ENSMUSP00000096899 | ENSMUSP00000043588 | 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 S; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.794 |
| Bfsp1 | Lim2 | ENSMUSP00000096899 | ENSMUSP00000004732 | 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). | Lens fiber membrane intrinsic protein; Present in the thicker 16-17 nm junctions of mammalian lens fiber cells, where it may contribute to cell junctional organization. Acts as a receptor for calmodulin. May play an important role in both lens development and cataractogenesis; Belongs to the PMP-22/EMP/MP20 family. | 0.605 |
| Bfsp1 | Mip | ENSMUSP00000096899 | ENSMUSP00000026455 | 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). | Lens fiber major intrinsic protein; Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.887 |
| Bfsp2 | Bfsp1 | ENSMUSP00000116249 | ENSMUSP00000096899 | 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). | 0.847 |
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