node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACTB | CAPZB | ENSGALP00000060844 | ENSGALP00000006415 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | 0.819 |
ACTB | CFL2 | ENSGALP00000060844 | ENSGALP00000016266 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | Cofilin-2; Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods; Belongs to the actin-binding proteins ADF family. | 0.999 |
ACTB | DSTN | ENSGALP00000060844 | ENSGALP00000014097 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | Destrin; Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner. | 0.823 |
ACTB | GSN | ENSGALP00000060844 | ENSGALP00000054518 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | 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 (By similarity). | 0.990 |
ACTB | PFN2 | ENSGALP00000060844 | ENSGALP00000073860 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | Profilin; Belongs to the profilin family. | 0.999 |
ACTB | PFN3 | ENSGALP00000060844 | ENSGALP00000015374 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | Profilin; Belongs to the profilin family. | 0.999 |
ACTB | PFN4 | ENSGALP00000060844 | ENSGALP00000030939 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | Profilin; Belongs to the profilin family. | 0.999 |
ACTB | TWF1 | ENSGALP00000060844 | ENSGALP00000043630 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | Uncharacterized protein. | 0.902 |
ACTB | TWF2 | ENSGALP00000060844 | ENSGALP00000052343 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | Twinfilin-2; Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin (By similarity). | 0.907 |
ACTB | WDR1 | ENSGALP00000060844 | ENSGALP00000024078 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | WD repeat-containing protein 1; Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. Enhances cofilin-mediated actin severing (By similarity); Belongs to the WD repeat AIP1 family. | 0.939 |
CAPZB | ACTB | ENSGALP00000006415 | ENSGALP00000060844 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | 0.819 |
CAPZB | CFL2 | ENSGALP00000006415 | ENSGALP00000016266 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | Cofilin-2; Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods; Belongs to the actin-binding proteins ADF family. | 0.690 |
CAPZB | DSTN | ENSGALP00000006415 | ENSGALP00000014097 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | Destrin; Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner. | 0.636 |
CAPZB | GSN | ENSGALP00000006415 | ENSGALP00000054518 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | 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 (By similarity). | 0.440 |
CAPZB | PFN2 | ENSGALP00000006415 | ENSGALP00000073860 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | Profilin; Belongs to the profilin family. | 0.435 |
CAPZB | PFN3 | ENSGALP00000006415 | ENSGALP00000015374 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | Profilin; Belongs to the profilin family. | 0.444 |
CAPZB | PFN4 | ENSGALP00000006415 | ENSGALP00000030939 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | Profilin; Belongs to the profilin family. | 0.619 |
CAPZB | TWF1 | ENSGALP00000006415 | ENSGALP00000043630 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | Uncharacterized protein. | 0.977 |
CAPZB | TWF2 | ENSGALP00000006415 | ENSGALP00000052343 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | Twinfilin-2; Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G- actin (By similarity). | 0.983 |
CAPZB | WDR1 | ENSGALP00000006415 | ENSGALP00000024078 | F-actin-capping protein subunit beta isoforms 1 and 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. May play a role in the regulation of cell morphology and cytoskeletal organization. | WD repeat-containing protein 1; Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. Enhances cofilin-mediated actin severing (By similarity); Belongs to the WD repeat AIP1 family. | 0.889 |