| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ARHGAP20 | BRWD3 | ENSP00000260283 | ENSP00000362372 | Rho GTPase-activating protein 20; GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | 0.959 |
| ATAD2B | BRWD3 | ENSP00000238789 | ENSP00000362372 | ATPase family AAA domain containing 2B. | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | 0.590 |
| ATAD2B | PHIP | ENSP00000238789 | ENSP00000275034 | ATPase family AAA domain containing 2B. | PH-interacting protein; Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. | 0.684 |
| BRWD3 | ARHGAP20 | ENSP00000362372 | ENSP00000260283 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | Rho GTPase-activating protein 20; GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. | 0.959 |
| BRWD3 | ATAD2B | ENSP00000362372 | ENSP00000238789 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | ATPase family AAA domain containing 2B. | 0.590 |
| BRWD3 | CUL4A | ENSP00000362372 | ENSP00000364589 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | Cullin-4A; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition co [...] | 0.756 |
| BRWD3 | CUL4B | ENSP00000362372 | ENSP00000384109 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | Cullin-4B; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and [...] | 0.914 |
| BRWD3 | DDB1 | ENSP00000362372 | ENSP00000301764 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | DNA damage-binding protein 1; Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin- protein ligase complexes which mediate the ubiqu [...] | 0.733 |
| BRWD3 | MED12 | ENSP00000362372 | ENSP00000363193 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | Mediator of RNA polymerase II transcription subunit 12; Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifi [...] | 0.557 |
| BRWD3 | NCOR2 | ENSP00000362372 | ENSP00000384018 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | Nuclear receptor corepressor 2; Transcriptional corepressor. Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Isoform 1 and isoform 4 have different affinities for different nuclear receptors. Involved in the regulation BCL6-dependent of the germinal center (GC) reactions, mainly through the control of the GC B-cells proliferation and survival. Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and and [...] | 0.654 |
| BRWD3 | PHIP | ENSP00000362372 | ENSP00000275034 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | PH-interacting protein; Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. | 0.726 |
| BRWD3 | UBXN7 | ENSP00000362372 | ENSP00000296328 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | UBX domain-containing protein 7; Ubiquitin-binding adapter that links a subset of NEDD8- associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates. | 0.887 |
| BRWD3 | ZNF711 | ENSP00000362372 | ENSP00000353922 | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | Zinc finger protein 711; Transcription regulator required for brain development. Probably acts as a transcription factor that binds to the promoter of target genes and recruits PHF8 histone demethylase, leading to activate expression of genes involved in neuron development, such as KDM5C. Belongs to the krueppel C2H2-type zinc-finger protein family. | 0.559 |
| CUL4A | BRWD3 | ENSP00000364589 | ENSP00000362372 | Cullin-4A; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition co [...] | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | 0.756 |
| CUL4A | CUL4B | ENSP00000364589 | ENSP00000384109 | Cullin-4A; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition co [...] | Cullin-4B; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and [...] | 0.999 |
| CUL4A | DDB1 | ENSP00000364589 | ENSP00000301764 | Cullin-4A; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition co [...] | DNA damage-binding protein 1; Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin- protein ligase complexes which mediate the ubiqu [...] | 0.999 |
| CUL4A | PHIP | ENSP00000364589 | ENSP00000275034 | Cullin-4A; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition co [...] | PH-interacting protein; Probable regulator of the insulin and insulin-like growth factor signaling pathways. Stimulates cell proliferation through regulation of cyclin transcription and has an anti-apoptotic activity through AKT1 phosphorylation and activation. Plays a role in the regulation of cell morphology and cytoskeletal organization. | 0.999 |
| CUL4A | UBXN7 | ENSP00000364589 | ENSP00000296328 | Cullin-4A; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition co [...] | UBX domain-containing protein 7; Ubiquitin-binding adapter that links a subset of NEDD8- associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates. | 0.944 |
| CUL4B | BRWD3 | ENSP00000384109 | ENSP00000362372 | Cullin-4B; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and [...] | Bromodomain and WD repeat-containing protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. | 0.914 |
| CUL4B | CUL4A | ENSP00000384109 | ENSP00000364589 | Cullin-4B; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and [...] | Cullin-4A; Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition co [...] | 0.999 |
