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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Lmod2 | Lmod3 | ENSMUSP00000031694 | ENSMUSP00000093315 | Leiomodin-2; Mediates nucleation of actin filaments and thereby promotes actin polymerization (By similarity). Plays a role in the regulation of actin filament length. Required for normal sarcomere organization in the heart, and for normal heart function. | Leiomodin-3; Essential for the organization of sarcomeric actin thin filaments in skeletal muscle. Increases the rate of actin polymerization (By similarity). Belongs to the tropomodulin family. | 0.590 |
| Lmod3 | Lmod2 | ENSMUSP00000093315 | ENSMUSP00000031694 | Leiomodin-3; Essential for the organization of sarcomeric actin thin filaments in skeletal muscle. Increases the rate of actin polymerization (By similarity). Belongs to the tropomodulin family. | Leiomodin-2; Mediates nucleation of actin filaments and thereby promotes actin polymerization (By similarity). Plays a role in the regulation of actin filament length. Required for normal sarcomere organization in the heart, and for normal heart function. | 0.590 |
| Lmod3 | Tmod4 | ENSMUSP00000093315 | ENSMUSP00000102846 | Leiomodin-3; Essential for the organization of sarcomeric actin thin filaments in skeletal muscle. Increases the rate of actin polymerization (By similarity). Belongs to the tropomodulin family. | Tropomodulin-4; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | 0.460 |
| Tmod1 | Tmod2 | ENSMUSP00000103402 | ENSMUSP00000069956 | Tropomodulin-1; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | Tropomodulin-2; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | 0.525 |
| Tmod1 | Tmod3 | ENSMUSP00000103402 | ENSMUSP00000072087 | Tropomodulin-1; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | Tropomodulin-3; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | 0.521 |
| Tmod1 | Tmod4 | ENSMUSP00000103402 | ENSMUSP00000102846 | Tropomodulin-1; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | Tropomodulin-4; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | 0.536 |
| Tmod2 | Tmod1 | ENSMUSP00000069956 | ENSMUSP00000103402 | Tropomodulin-2; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | Tropomodulin-1; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | 0.525 |
| Tmod2 | Tmod3 | ENSMUSP00000069956 | ENSMUSP00000072087 | Tropomodulin-2; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | Tropomodulin-3; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | 0.513 |
| Tmod2 | Tmod4 | ENSMUSP00000069956 | ENSMUSP00000102846 | Tropomodulin-2; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | Tropomodulin-4; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | 0.522 |
| Tmod3 | Tmod1 | ENSMUSP00000072087 | ENSMUSP00000103402 | Tropomodulin-3; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | Tropomodulin-1; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | 0.521 |
| Tmod3 | Tmod2 | ENSMUSP00000072087 | ENSMUSP00000069956 | Tropomodulin-3; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | Tropomodulin-2; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | 0.513 |
| Tmod3 | Tmod4 | ENSMUSP00000072087 | ENSMUSP00000102846 | Tropomodulin-3; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | Tropomodulin-4; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | 0.523 |
| Tmod4 | Lmod3 | ENSMUSP00000102846 | ENSMUSP00000093315 | Tropomodulin-4; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | Leiomodin-3; Essential for the organization of sarcomeric actin thin filaments in skeletal muscle. Increases the rate of actin polymerization (By similarity). Belongs to the tropomodulin family. | 0.460 |
| Tmod4 | Tmod1 | ENSMUSP00000102846 | ENSMUSP00000103402 | Tropomodulin-4; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | Tropomodulin-1; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | 0.536 |
| Tmod4 | Tmod2 | ENSMUSP00000102846 | ENSMUSP00000069956 | Tropomodulin-4; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | Tropomodulin-2; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | 0.522 |
| Tmod4 | Tmod3 | ENSMUSP00000102846 | ENSMUSP00000072087 | Tropomodulin-4; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). | Tropomodulin-3; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity); Belongs to the tropomodulin family. | 0.523 |