node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ESPN | TRIOBP | ENSP00000367059 | ENSP00000384312 | espin; Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimensions, dynamics and signaling capacities of the actin filament-rich, microvillus-type specializations that mediate sensory transduction in variouS mechanosensory and chemosensory cells (By similarity) | TRIO and F-actin binding protein | 0.476 |
HECTD3 | TRIOBP | ENSP00000361245 | ENSP00000384312 | HECT domain containing E3 ubiquitin protein ligase 3; E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus faciliting cell cycle progression by regulating the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By similarity) | TRIO and F-actin binding protein | 0.576 |
IQGAP1 | MYH9 | ENSP00000268182 | ENSP00000216181 | IQ motif containing GTPase activating protein 1; Binds to activated CDC42 but does not stimulate its GTPase activity. It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth | myosin, heavy chain 9, non-muscle; Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping | 0.719 |
MYH9 | IQGAP1 | ENSP00000216181 | ENSP00000268182 | myosin, heavy chain 9, non-muscle; Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping | IQ motif containing GTPase activating protein 1; Binds to activated CDC42 but does not stimulate its GTPase activity. It associates with calmodulin. Could serve as an assembly scaffold for the organization of a multimolecular complex that would interface incoming signals to the reorganization of the actin cytoskeleton at the plasma membrane. May promote neurite outgrowth | 0.719 |
PLK1 | TERF1 | ENSP00000300093 | ENSP00000276603 | polo-like kinase 1; Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55 [...] | telomeric repeat binding factor (NIMA-interacting) 1; Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double- stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair [...] | 0.836 |
PLK1 | TRIOBP | ENSP00000300093 | ENSP00000384312 | polo-like kinase 1; Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55 [...] | TRIO and F-actin binding protein | 0.576 |
TERF1 | PLK1 | ENSP00000276603 | ENSP00000300093 | telomeric repeat binding factor (NIMA-interacting) 1; Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double- stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair [...] | polo-like kinase 1; Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55 [...] | 0.836 |
TERF1 | TRIOBP | ENSP00000276603 | ENSP00000384312 | telomeric repeat binding factor (NIMA-interacting) 1; Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double- stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair [...] | TRIO and F-actin binding protein | 0.576 |
TRIOBP | ESPN | ENSP00000384312 | ENSP00000367059 | TRIO and F-actin binding protein | espin; Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimensions, dynamics and signaling capacities of the actin filament-rich, microvillus-type specializations that mediate sensory transduction in variouS mechanosensory and chemosensory cells (By similarity) | 0.476 |
TRIOBP | HECTD3 | ENSP00000384312 | ENSP00000361245 | TRIO and F-actin binding protein | HECT domain containing E3 ubiquitin protein ligase 3; E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus faciliting cell cycle progression by regulating the turn-over of TRIOBP. Mediates also ubiquitination of STX8 (By similarity) | 0.576 |
TRIOBP | PLK1 | ENSP00000384312 | ENSP00000300093 | TRIO and F-actin binding protein | polo-like kinase 1; Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55 [...] | 0.576 |
TRIOBP | TERF1 | ENSP00000384312 | ENSP00000276603 | TRIO and F-actin binding protein | telomeric repeat binding factor (NIMA-interacting) 1; Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double- stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair [...] | 0.576 |