node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACTA1 | CAP1 | ENSP00000355645 | ENSP00000361883 | Actin, alpha skeletal muscle, intermediate form; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells; Belongs to the actin family. | Adenylyl cyclase-associated protein 1; Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity; Belongs to the CAP family. | 0.957 |
ACTA1 | CAPZA1 | ENSP00000355645 | ENSP00000263168 | Actin, alpha skeletal muscle, intermediate form; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells; Belongs to the actin family. | 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. | 0.932 |
ACTA1 | CAPZB | ENSP00000355645 | ENSP00000401010 | Actin, alpha skeletal muscle, intermediate form; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells; Belongs to the actin family. | 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. | 0.942 |
ACTA1 | CFL1 | ENSP00000355645 | ENSP00000432660 | Actin, alpha skeletal muscle, intermediate form; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells; Belongs to the actin family. | Cofilin-1; Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Required for neural tube morphogenesis and neural crest cell migration (By similarity). | 0.978 |
ACTA1 | DSTN | ENSP00000355645 | ENSP00000246069 | Actin, alpha skeletal muscle, intermediate form; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells; Belongs to the actin family. | Destrin; Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner. | 0.572 |
ACTA1 | GSN | ENSP00000355645 | ENSP00000362924 | Actin, alpha skeletal muscle, intermediate form; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells; Belongs to the actin family. | Gelsolin; 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). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. | 0.986 |
ACTA1 | TWF1 | ENSP00000355645 | ENSP00000449428 | Actin, alpha skeletal muscle, intermediate form; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells; Belongs to the actin family. | Twinfilin-1; Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity). | 0.938 |
CAP1 | ACTA1 | ENSP00000361883 | ENSP00000355645 | Adenylyl cyclase-associated protein 1; Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity; Belongs to the CAP family. | Actin, alpha skeletal muscle, intermediate form; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells; Belongs to the actin family. | 0.957 |
CAP1 | CAPZB | ENSP00000361883 | ENSP00000401010 | Adenylyl cyclase-associated protein 1; Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity; Belongs to the CAP family. | 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. | 0.730 |
CAP1 | CFL1 | ENSP00000361883 | ENSP00000432660 | Adenylyl cyclase-associated protein 1; Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity; Belongs to the CAP family. | Cofilin-1; Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Required for neural tube morphogenesis and neural crest cell migration (By similarity). | 0.978 |
CAP1 | DSTN | ENSP00000361883 | ENSP00000246069 | Adenylyl cyclase-associated protein 1; Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity; Belongs to the CAP family. | Destrin; Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner. | 0.578 |
CAP1 | TWF1 | ENSP00000361883 | ENSP00000449428 | Adenylyl cyclase-associated protein 1; Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity; Belongs to the CAP family. | Twinfilin-1; Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity). | 0.912 |
CAPZA1 | ACTA1 | ENSP00000263168 | ENSP00000355645 | 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. | Actin, alpha skeletal muscle, intermediate form; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells; Belongs to the actin family. | 0.932 |
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 | CFL1 | ENSP00000263168 | ENSP00000432660 | 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. | Cofilin-1; Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Required for neural tube morphogenesis and neural crest cell migration (By similarity). | 0.720 |
CAPZA1 | DSTN | ENSP00000263168 | ENSP00000246069 | 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. | Destrin; Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner. | 0.554 |
CAPZA1 | GSN | ENSP00000263168 | ENSP00000362924 | 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. | Gelsolin; 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). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. | 0.626 |
CAPZA1 | MYO1C | ENSP00000263168 | ENSP00000496954 | 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. | Unconventional myosin-Ic; 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. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in st [...] | 0.587 |
CAPZA1 | PLS1 | ENSP00000263168 | ENSP00000336831 | 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. | Plastin-1; Actin-bundling protein in the absence of calcium. | 0.655 |
CAPZA1 | TWF1 | ENSP00000263168 | ENSP00000449428 | 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. | Twinfilin-1; Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity). | 0.980 |