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FUNCTION E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair (PubMed:10230407, PubMed:10579999, PubMed:11961546, PubMed:15983046, PubMed:16678110, PubMed:19112177, PubMed:19679664, PubMed:22748924, PubMed:23455478, PubMed:27565346, PubMed:29769719, PubMed:32355176, PubMed:33417871, PubMed:37844242, PubMed:38326650, PubMed:39504960, PubMed:39667934, PubMed:38316879). CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets (PubMed:27565346). The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex mediates ubiquitination of Pol II subunit POLR2A at 'Lys-1268', a critical TC-NER checkpoint (PubMed:32355176, PubMed:34526721). Core component of the Cul7-RING(FBXW8) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:35982156). Core component of a Cul9-RING ubiquitin ligase complex composed of CUL9 and RBX1, which mediates mono-ubiquitination of p53/TP53 (PubMed:38605244). Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. As part of a multisubunit complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A (PubMed:19920177).CATALYTIC ACTIVITY S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.CATALYTIC ACTIVITY S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine.PATHWAY Protein modification; protein ubiquitination.PATHWAY Protein modification; protein neddylation.SUBUNIT Component of multiple Cul1-RING E3 ubiquitin-protein ligase complexes commonly known as SCF (SKP1-CUL1-F-box) complexes, consisting of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein (PubMed:10230406, PubMed:11961546, PubMed:20596027, PubMed:22748924, PubMed:38326650, PubMed:39880951). Part of a SCF(SKP2) complex consisting of CUL1, RBX1, SKP1 and SKP2 (PubMed:10230406, PubMed:11961546). Part of a SCF(FBXO3) complex consisting of CUL1, FBXO3, RBX1 and SKP1; this complex interacts with PML via FBXO3 (PubMed:18809579). Component of the SCF(Cyclin F) complex consisting of CUL1, RBX1, SKP1 and CCNF (PubMed:20596027). Identified in a SCF E3 ubiquitin ligase complex together with HINT1 and CDC34 (PubMed:19112177). Component of multiple Cul2-RING (CRL2) E3 ubiquitin-protein ligase complexes consisting of CUL2, Elongin BC (ELOB and ELOC), RBX1 and a variable substrate-specific adapter; this complex is also known as ECS (Elongin BC-CUL2/5-SOCS-box protein) complex and may consists of CUL2 or CUL5 (PubMed:11384984, PubMed:38326650). Component of the CRL2(LRR1) complex with the substrate recognition component LRR1 (PubMed:34700328). Part of the ECS(VHL) or CBC(VHL) complex composed of CUL2 or CUL5, RBX1, ELOB, ELOC and VHL (PubMed:10213691, PubMed:38326650). Part of the CRL2 complex with elongin BC complex (ELOB and ELOC), CUL2 and MED8; and part of the CRL5 complex with elongin BC complex (ELOB and ELOC), CUL5 and MUF1 (PubMed:11384984, PubMed:12149480, PubMed:37844242). Component of multiple BCR (BTB-CUL3-RBX1) or Cul3-RING E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein (PubMed:15983046). Part of the BCR(ENC1) complex containing ENC1 (PubMed:15983046). Part of the BCR(GAN) complex containing GAN (PubMed:15983046). Part of the BCR(KLHL41) complex containing KLHL41 (PubMed:15983046). Part of the BCR(KEAP1) complex containing KEAP1 (PubMed:15983046). Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL22 and RBX1 (PubMed:23455478). Component of the BCR(KBTBD4) E3 ubiquitin ligase complex, at least composed of CUL3, KBTBD4 and RBX1 (PubMed:33417871). Component of a BCR(KBTBD6/7) complex, composed of CUL3, RBX1, KBTBD6 and KBTBD7 (PubMed:25684205). Component of the BCR(ARMC5) E3 ubiquitin ligase complex, composed of CUL3, ARMC5 and RBX1 (PubMed:35687106, PubMed:38225631, PubMed:39504960, PubMed:39667934). Component of Cul4-RING E3 ubiquitin-protein ligase complex, known as the CSA complex or DCX(ERCC8) complex, containing CUL4A, ERCC8, RBX1 and DDB1; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II (PubMed:12732143, PubMed:32355176, PubMed:38316879). Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of CUL4A, RBX1, DET1, DDB1, and COP1 (PubMed:14739464). Part of an E3 ligase complex composed of CUL4A or CUL4B, RBX1, DDB1 and DDB2 (PubMed:16678110). Component of a Cul5-RING (CRL5) ubiquitin ligase complex consisting of CUL5, ELOB, ELOC, elongin A/ELOA, and RBX1 (PubMed:19920177). Part of CRL5 ubiquitin ligase complex with CUL5, ELOB, ELOC, SOCS1 or WSB1. Component of the Cul7-RING(FBXW8) complex consisting of CUL7, RBX1, SKP1 and FBXW8; within the complex interacts with CUL7 (PubMed:12481031, PubMed:35982156). Component of the Cul9-RING complex consisting of CUL9 and RBX1; the CUL9-RBX1 complex is a heterododecamer composed of six CUL9 and six RBX1 protomers (PubMed:38605244). Interacts directly with CUL1, CUL2, CUL7 and CUL9; probably also with CUL3, CUL4A, CUL4B and CUL5 (PubMed:10230407, PubMed:12481031, PubMed:35982156, PubMed:38605244, PubMed:38326650). Interacts with CDC34 (PubMed:22748924). Interacts with GLMN; GLMN competes for the binding site of the E2 ubiquitin-conjugating enzyme CDC34 and disrupts CDC34 binding (PubMed:22748924). Interacts with COPS6 (PubMed:11337588). Interacts with UBE2M (PubMed:19250909). Interacts with SESN1 and SESN2 (PubMed:23274085). Interacts with NOTCH2 (PubMed:29149593). Interacts with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5 (PubMed:24192928, PubMed:25349211, PubMed:26906416). Interacts with CAND1 (By similarity).SUBUNIT (Microbial infection) Interacts with human adenovirus 5 protein E1A; this interaction inhibits RBX1-CUL1-dependent elongation reaction of ubiquitin chains by the SCF(FBW7) complex.INTERACTION Widely expressed.DOMAIN The RING-type zinc finger domain is essential for ubiquitin ligase activity (PubMed:10230407). It coordinates an additional third zinc ion (PubMed:11961546, PubMed:22748924).SIMILARITY Belongs to the RING-box family.SEQUENCE CAUTION Extended N-terminus.
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