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 |
| 4933400A11Rik | Actr1a | ENSRNOP00000004893 | ENSRNOP00000026792 | 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. | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | 0.756 |
| 4933400A11Rik | Capza1 | ENSRNOP00000004893 | ENSRNOP00000052868 | 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 alpha-1; 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. May play a role in the formation of epithelial cell junctions. | 0.546 |
| 4933400A11Rik | Capza2 | ENSRNOP00000004893 | ENSRNOP00000072041 | 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 alpha-2; 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 (By similarity). | 0.680 |
| 4933400A11Rik | Capza3 | ENSRNOP00000004893 | ENSRNOP00000011555 | 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 alpha-3; 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. May play a role in the morphogenesis of spermatid. | 0.714 |
| 4933400A11Rik | Capzb | ENSRNOP00000004893 | ENSRNOP00000070586 | 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. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). | 0.952 |
| 4933400A11Rik | Dctn1 | ENSRNOP00000004893 | ENSRNOP00000059076 | 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. | Dynactin subunit 1; Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. C [...] | 0.791 |
| 4933400A11Rik | Dctn2 | ENSRNOP00000004893 | ENSRNOP00000069048 | 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. | Dynactin subunit 2; Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development (By similarity). | 0.801 |
| 4933400A11Rik | Dctn4 | ENSRNOP00000004893 | ENSRNOP00000026394 | 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. | Dynactin subunit 4; Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton. | 0.766 |
| 4933400A11Rik | Dctn6 | ENSRNOP00000004893 | ENSRNOP00000017756 | 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. | Dynactin 6 (Predicted), isoform CRA_b. | 0.710 |
| 4933400A11Rik | Mtpn | ENSRNOP00000004893 | ENSRNOP00000015808 | 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. | Myotrophin; Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer (By similarity). Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. | 0.830 |
| Actr1a | 4933400A11Rik | ENSRNOP00000026792 | ENSRNOP00000004893 | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | 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. | 0.756 |
| Actr1a | Capza1 | ENSRNOP00000026792 | ENSRNOP00000052868 | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | F-actin-capping protein subunit alpha-1; 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. May play a role in the formation of epithelial cell junctions. | 0.878 |
| Actr1a | Capza2 | ENSRNOP00000026792 | ENSRNOP00000072041 | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | F-actin-capping protein subunit alpha-2; 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 (By similarity). | 0.842 |
| Actr1a | Capza3 | ENSRNOP00000026792 | ENSRNOP00000011555 | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | F-actin-capping protein subunit alpha-3; 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. May play a role in the morphogenesis of spermatid. | 0.754 |
| Actr1a | Capzb | ENSRNOP00000026792 | ENSRNOP00000070586 | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | 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. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). | 0.932 |
| Actr1a | Dctn1 | ENSRNOP00000026792 | ENSRNOP00000059076 | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | Dynactin subunit 1; Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. C [...] | 0.992 |
| Actr1a | Dctn2 | ENSRNOP00000026792 | ENSRNOP00000069048 | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | Dynactin subunit 2; Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development (By similarity). | 0.999 |
| Actr1a | Dctn4 | ENSRNOP00000026792 | ENSRNOP00000026394 | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | Dynactin subunit 4; Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton. | 0.991 |
| Actr1a | Dctn6 | ENSRNOP00000026792 | ENSRNOP00000017756 | Alpha-centractin; Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome (By similarity). | Dynactin 6 (Predicted), isoform CRA_b. | 0.997 |
| Capza1 | 4933400A11Rik | ENSRNOP00000052868 | ENSRNOP00000004893 | F-actin-capping protein subunit alpha-1; 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. May play a role in the formation of epithelial cell junctions. | 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. | 0.546 |
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