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 |
| CAPZA1 | CAPZB | ENSBTAP00000056906 | ENSBTAP00000059505 | 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 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. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization. | 0.999 |
| CAPZA1 | FAM21A | ENSBTAP00000056906 | ENSBTAP00000025173 | 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. | CAP-ZIP_m domain-containing protein. | 0.694 |
| CAPZA1 | SNX27 | ENSBTAP00000056906 | ENSBTAP00000033754 | 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. | Sorting nexin-27; Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C- terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing e [...] | 0.402 |
| CAPZA1 | WASHC1 | ENSBTAP00000056906 | ENSBTAP00000059564 | 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. | WASH complex subunit 1; Acts as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Its assembly in the WASH core complex seems to inhibit its NPF activity and via WASHC2 is required for its membrane targeting. Involved in endocytic trafficking of EGF. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and invo [...] | 0.764 |
| CAPZA1 | WASHC3 | ENSBTAP00000056906 | ENSBTAP00000000022 | 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. | WASH complex subunit 3; Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting. | 0.761 |
| CAPZA1 | WASHC4 | ENSBTAP00000056906 | ENSBTAP00000069188 | 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. | WASH complex subunit 4. | 0.687 |
| CAPZA1 | WASHC5 | ENSBTAP00000056906 | ENSBTAP00000013591 | 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. | WASH complex subunit 5. | 0.728 |
| CAPZB | CAPZA1 | ENSBTAP00000059505 | ENSBTAP00000056906 | 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. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization. | 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. | 0.999 |
| CAPZB | FAM21A | ENSBTAP00000059505 | ENSBTAP00000025173 | 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. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization. | CAP-ZIP_m domain-containing protein. | 0.716 |
| CAPZB | SNX27 | ENSBTAP00000059505 | ENSBTAP00000033754 | 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. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization. | Sorting nexin-27; Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C- terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing e [...] | 0.402 |
| CAPZB | WASHC1 | ENSBTAP00000059505 | ENSBTAP00000059564 | 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. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization. | WASH complex subunit 1; Acts as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Its assembly in the WASH core complex seems to inhibit its NPF activity and via WASHC2 is required for its membrane targeting. Involved in endocytic trafficking of EGF. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and invo [...] | 0.796 |
| CAPZB | WASHC3 | ENSBTAP00000059505 | ENSBTAP00000000022 | 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. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization. | WASH complex subunit 3; Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting. | 0.826 |
| CAPZB | WASHC4 | ENSBTAP00000059505 | ENSBTAP00000069188 | 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. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization. | WASH complex subunit 4. | 0.679 |
| CAPZB | WASHC5 | ENSBTAP00000059505 | ENSBTAP00000013591 | 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. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization. | WASH complex subunit 5. | 0.775 |
| CCDC22 | SNX27 | ENSBTAP00000066233 | ENSBTAP00000033754 | Coiled-coil domain-containing protein 22; Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. Component of the CCC complex, which is inv [...] | Sorting nexin-27; Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C- terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing e [...] | 0.736 |
| CCDC22 | VPS29 | ENSBTAP00000066233 | ENSBTAP00000011076 | Coiled-coil domain-containing protein 22; Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. Component of the CCC complex, which is inv [...] | Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans- Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for carg [...] | 0.865 |
| CCDC22 | VPS35 | ENSBTAP00000066233 | ENSBTAP00000003239 | Coiled-coil domain-containing protein 22; Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. Component of the CCC complex, which is inv [...] | Vacuolar protein sorting-associated protein 35; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may [...] | 0.643 |
| CCDC22 | WASHC1 | ENSBTAP00000066233 | ENSBTAP00000059564 | Coiled-coil domain-containing protein 22; Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. Component of the CCC complex, which is inv [...] | WASH complex subunit 1; Acts as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Its assembly in the WASH core complex seems to inhibit its NPF activity and via WASHC2 is required for its membrane targeting. Involved in endocytic trafficking of EGF. Involved in transferrin receptor recycling. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and invo [...] | 0.716 |
| CCDC22 | WASHC3 | ENSBTAP00000066233 | ENSBTAP00000000022 | Coiled-coil domain-containing protein 22; Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. Component of the CCC complex, which is inv [...] | WASH complex subunit 3; Acts at least in part as component of the WASH core complex whose assembly at the surface of endosomes seems to inhibit WASH nucleation-promoting factor (NPF) activity in recruiting and activating the Arp2/3 complex to induce actin polymerization, and which is involved in regulation of the fission of tubules that serve as transport intermediates during endosome sorting. | 0.736 |
| CCDC22 | WASHC4 | ENSBTAP00000066233 | ENSBTAP00000069188 | Coiled-coil domain-containing protein 22; Involved in regulation of NF-kappa-B signaling. Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10. Component of the CCC complex, which is inv [...] | WASH complex subunit 4. | 0.474 |
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