| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACOT8 | KLHL23 | ENSP00000217455 | ENSP00000376419 | Acyl-coenzyme A thioesterase 8; Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. More [...] | Kelch-like protein 23; Kelch like family member 23. | 0.778 |
| AMDHD1 | KLHL23 | ENSP00000266736 | ENSP00000376419 | Probable imidazolonepropionase; Amidohydrolase domain containing 1. | Kelch-like protein 23; Kelch like family member 23. | 0.750 |
| CUL3 | FBXL17 | ENSP00000264414 | ENSP00000437464 | Cullin-3; Core component of multiple cullin-RING-based BCR (BTB-CUL3- RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. BCR complexes and ARIH1 collaborate in tandem to mediate 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 cu [...] | F-box/LRR-repeat protein 17; Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome. The ability of the SCF(FBXL17) complex to eliminate compromised BTB di [...] | 0.605 |
| CUL3 | KLHL23 | ENSP00000264414 | ENSP00000376419 | Cullin-3; Core component of multiple cullin-RING-based BCR (BTB-CUL3- RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. BCR complexes and ARIH1 collaborate in tandem to mediate 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 cu [...] | Kelch-like protein 23; Kelch like family member 23. | 0.995 |
| DCDC2B | KLHL23 | ENSP00000386870 | ENSP00000376419 | Doublecortin domain containing 2B. | Kelch-like protein 23; Kelch like family member 23. | 0.478 |
| DCDC2C | KLHL23 | ENSP00000382097 | ENSP00000376419 | Doublecortin domain containing 2C. | Kelch-like protein 23; Kelch like family member 23. | 0.527 |
| FBXL17 | CUL3 | ENSP00000437464 | ENSP00000264414 | F-box/LRR-repeat protein 17; Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome. The ability of the SCF(FBXL17) complex to eliminate compromised BTB di [...] | Cullin-3; Core component of multiple cullin-RING-based BCR (BTB-CUL3- RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. BCR complexes and ARIH1 collaborate in tandem to mediate 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 cu [...] | 0.605 |
| FBXL17 | HNRNPL | ENSP00000437464 | ENSP00000221419 | F-box/LRR-repeat protein 17; Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome. The ability of the SCF(FBXL17) complex to eliminate compromised BTB di [...] | Heterogeneous nuclear ribonucleoprotein L; Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. | 0.481 |
| FBXL17 | KLHL23 | ENSP00000437464 | ENSP00000376419 | F-box/LRR-repeat protein 17; Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome. The ability of the SCF(FBXL17) complex to eliminate compromised BTB di [...] | Kelch-like protein 23; Kelch like family member 23. | 0.483 |
| HNRNPL | FBXL17 | ENSP00000221419 | ENSP00000437464 | Heterogeneous nuclear ribonucleoprotein L; Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. | F-box/LRR-repeat protein 17; Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome. The ability of the SCF(FBXL17) complex to eliminate compromised BTB di [...] | 0.481 |
| HNRNPL | KLHL23 | ENSP00000221419 | ENSP00000376419 | Heterogeneous nuclear ribonucleoprotein L; Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. | Kelch-like protein 23; Kelch like family member 23. | 0.457 |
| KLHL23 | ACOT8 | ENSP00000376419 | ENSP00000217455 | Kelch-like protein 23; Kelch like family member 23. | Acyl-coenzyme A thioesterase 8; Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Acyl-coenzyme A thioesterase 8/ACOT8 display no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. More [...] | 0.778 |
| KLHL23 | AMDHD1 | ENSP00000376419 | ENSP00000266736 | Kelch-like protein 23; Kelch like family member 23. | Probable imidazolonepropionase; Amidohydrolase domain containing 1. | 0.750 |
| KLHL23 | CUL3 | ENSP00000376419 | ENSP00000264414 | Kelch-like protein 23; Kelch like family member 23. | Cullin-3; Core component of multiple cullin-RING-based BCR (BTB-CUL3- RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. BCR complexes and ARIH1 collaborate in tandem to mediate 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 cu [...] | 0.995 |
| KLHL23 | DCDC2B | ENSP00000376419 | ENSP00000386870 | Kelch-like protein 23; Kelch like family member 23. | Doublecortin domain containing 2B. | 0.478 |
| KLHL23 | DCDC2C | ENSP00000376419 | ENSP00000382097 | Kelch-like protein 23; Kelch like family member 23. | Doublecortin domain containing 2C. | 0.527 |
| KLHL23 | FBXL17 | ENSP00000376419 | ENSP00000437464 | Kelch-like protein 23; Kelch like family member 23. | F-box/LRR-repeat protein 17; Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteaseome. The ability of the SCF(FBXL17) complex to eliminate compromised BTB di [...] | 0.483 |
| KLHL23 | HNRNPL | ENSP00000376419 | ENSP00000221419 | Kelch-like protein 23; Kelch like family member 23. | Heterogeneous nuclear ribonucleoprotein L; Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. | 0.457 |
| KLHL23 | KNCN | ENSP00000376419 | ENSP00000419705 | Kelch-like protein 23; Kelch like family member 23. | Kinocilin; May play a role in stabilizing dense microtubular networks or in vesicular trafficking. | 0.495 |
| KLHL23 | PHOSPHO2 | ENSP00000376419 | ENSP00000481046 | Kelch-like protein 23; Kelch like family member 23. | Pyridoxal phosphate phosphatase PHOSPHO2; Phosphatase that has high activity toward pyridoxal 5'- phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate. | 0.595 |
