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 | ENSP00000263168 | ENSP00000401010 | 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. Plays a role in the regulation of cell morphology and cytoskeletal organization. | 0.999 |
| CAPZA1 | PLEKHO2 | ENSP00000263168 | ENSP00000326706 | 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. | Pleckstrin homology domain containing O2. | 0.735 |
| CAPZB | CAPZA1 | ENSP00000401010 | ENSP00000263168 | 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. | 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 | PLEKHO2 | ENSP00000401010 | ENSP00000326706 | 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. | Pleckstrin homology domain containing O2. | 0.778 |
| CYTH4 | MYO1F | ENSP00000248901 | ENSP00000494550 | Cytohesin-4; Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP. | Unconventional myosin-If; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family. | 0.628 |
| CYTH4 | PLEKHO2 | ENSP00000248901 | ENSP00000326706 | Cytohesin-4; Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP. | Pleckstrin homology domain containing O2. | 0.453 |
| FAM184A | PLEKHO2 | ENSP00000342604 | ENSP00000326706 | Protein FAM184A; Family with sequence similarity 184 member A. | Pleckstrin homology domain containing O2. | 0.469 |
| FLAD1 | PLEKHO2 | ENSP00000292180 | ENSP00000326706 | Molybdenum cofactor biosynthesis protein-like region; Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily. | Pleckstrin homology domain containing O2. | 0.420 |
| IL10RB | PLEKHO2 | ENSP00000290200 | ENSP00000326706 | Interleukin-10 receptor subunit beta; Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. | Pleckstrin homology domain containing O2. | 0.528 |
| MAP3K6 | PLEKHO2 | ENSP00000350195 | ENSP00000326706 | Mitogen-activated protein kinase kinase kinase 6; Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways. | Pleckstrin homology domain containing O2. | 0.444 |
| MYO1F | CYTH4 | ENSP00000494550 | ENSP00000248901 | Unconventional myosin-If; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family. | Cytohesin-4; Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP. | 0.628 |
| MYO1F | PLEKHO2 | ENSP00000494550 | ENSP00000326706 | Unconventional myosin-If; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family. | Pleckstrin homology domain containing O2. | 0.411 |
| MYO1F | THEMIS2 | ENSP00000494550 | ENSP00000363031 | Unconventional myosin-If; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family. | Protein THEMIS2; May constitute a control point in macrophage inflammatory response, promoting LPS-induced TNF production. | 0.443 |
| PLEKHO2 | CAPZA1 | ENSP00000326706 | ENSP00000263168 | Pleckstrin homology domain containing O2. | 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. | 0.735 |
| PLEKHO2 | CAPZB | ENSP00000326706 | ENSP00000401010 | Pleckstrin homology domain containing O2. | 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. | 0.778 |
| PLEKHO2 | CYTH4 | ENSP00000326706 | ENSP00000248901 | Pleckstrin homology domain containing O2. | Cytohesin-4; Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP. | 0.453 |
| PLEKHO2 | FAM184A | ENSP00000326706 | ENSP00000342604 | Pleckstrin homology domain containing O2. | Protein FAM184A; Family with sequence similarity 184 member A. | 0.469 |
| PLEKHO2 | FLAD1 | ENSP00000326706 | ENSP00000292180 | Pleckstrin homology domain containing O2. | Molybdenum cofactor biosynthesis protein-like region; Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily. | 0.420 |
| PLEKHO2 | IL10RB | ENSP00000326706 | ENSP00000290200 | Pleckstrin homology domain containing O2. | Interleukin-10 receptor subunit beta; Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. | 0.528 |
| PLEKHO2 | MAP3K6 | ENSP00000326706 | ENSP00000350195 | Pleckstrin homology domain containing O2. | Mitogen-activated protein kinase kinase kinase 6; Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways. | 0.444 |
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