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 |
| act-5 | cap-1 | T25C8.2.2 | D2024.6.2 | ACTin. | F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | 0.549 |
| act-5 | cap-2 | T25C8.2.2 | M106.5.1 | ACTin. | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | 0.704 |
| act-5 | cas-1 | T25C8.2.2 | F41G4.2a.1 | ACTin. | Adenylyl cyclase-associated protein; Belongs to the CAP family. | 0.548 |
| act-5 | cas-2 | T25C8.2.2 | C18E3.6a.2 | ACTin. | Adenylyl cyclase-associated protein; Belongs to the CAP family. | 0.638 |
| act-5 | gsnl-1 | T25C8.2.2 | K06A4.3.1 | ACTin. | Gelsolin-like protein 1; Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). Binds actin but does not nucleate actin polymerization, albeit slows down elongation by blocking the barbed ends. By promoting actin depolymerization, required for the elimination of presynaptic components downstream of the egl-1, ced-4 and ced-3 apoptotic pathway during larval development. Belongs to the villin/gelsolin family. | 0.997 |
| act-5 | pfn-3 | T25C8.2.2 | K03E6.6.1 | ACTin. | Profilin-3; Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Also binds to poly(L-proline) and phosphatidylinositol 4,5-bisphosphate micelles. | 0.999 |
| act-5 | twf-2 | T25C8.2.2 | F38E9.5.2 | ACTin. | TWinFilin actin binding protein homolog. | 0.920 |
| act-5 | unc-60 | T25C8.2.2 | C38C3.5.1 | ACTin. | Actin-depolymerizing factor 2, isoform c; Depolymerizes growing actin filaments in muscle cells; required for the assembly of actin filaments into the functional contractile myofilament lattice of muscle. Belongs to the actin-binding proteins ADF family. | 0.999 |
| cap-1 | act-5 | D2024.6.2 | T25C8.2.2 | F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | ACTin. | 0.549 |
| cap-1 | cap-2 | D2024.6.2 | M106.5.1 | F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | 0.999 |
| cap-1 | cas-1 | D2024.6.2 | F41G4.2a.1 | F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | Adenylyl cyclase-associated protein; Belongs to the CAP family. | 0.414 |
| cap-1 | cas-2 | D2024.6.2 | C18E3.6a.2 | F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | Adenylyl cyclase-associated protein; Belongs to the CAP family. | 0.411 |
| cap-1 | pfn-3 | D2024.6.2 | K03E6.6.1 | F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | Profilin-3; Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Also binds to poly(L-proline) and phosphatidylinositol 4,5-bisphosphate micelles. | 0.507 |
| cap-1 | twf-2 | D2024.6.2 | F38E9.5.2 | F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | TWinFilin actin binding protein homolog. | 0.864 |
| cap-1 | unc-60 | D2024.6.2 | C38C3.5.1 | F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | Actin-depolymerizing factor 2, isoform c; Depolymerizes growing actin filaments in muscle cells; required for the assembly of actin filaments into the functional contractile myofilament lattice of muscle. Belongs to the actin-binding proteins ADF family. | 0.564 |
| cap-2 | act-5 | M106.5.1 | T25C8.2.2 | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | ACTin. | 0.704 |
| cap-2 | cap-1 | M106.5.1 | D2024.6.2 | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | 0.999 |
| cap-2 | cas-1 | M106.5.1 | F41G4.2a.1 | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | Adenylyl cyclase-associated protein; Belongs to the CAP family. | 0.419 |
| cap-2 | cas-2 | M106.5.1 | C18E3.6a.2 | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | Adenylyl cyclase-associated protein; Belongs to the CAP family. | 0.883 |
| cap-2 | gsnl-1 | M106.5.1 | K06A4.3.1 | F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | Gelsolin-like protein 1; Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). Binds actin but does not nucleate actin polymerization, albeit slows down elongation by blocking the barbed ends. By promoting actin depolymerization, required for the elimination of presynaptic components downstream of the egl-1, ced-4 and ced-3 apoptotic pathway during larval development. Belongs to the villin/gelsolin family. | 0.412 |
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