{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q13618","secondaryAccessions":["A8K536","B8ZZC3","O75415","Q569L3","Q9UBI8","Q9UET7"],"uniProtkbId":"CUL3_HUMAN","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-01-24","entryVersion":235,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cullin-3"},"shortNames":[{"value":"CUL-3"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2553"}],"value":"CUL3"},"synonyms":[{"value":"KIAA0617"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10500095"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11311237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15601839"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15897469"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15983046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16006525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16524876"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17543862"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18397884"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19261606"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19995937"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20389280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21670212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21840486"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22085717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22358839"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22578813"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22632832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23213400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23387299"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23453970"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23455478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23576762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24768539"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25270598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25684205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26399832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27565346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27664236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27716508"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27798626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29695787"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29769719"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33417871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35687106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36997086"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37526061"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38225631"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39504960"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39667934"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40396757"}],"value":"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 (PubMed:29695787). BCR complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (PubMed:27565346). 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 BCR complex depends on the BTB domain-containing protein as the substrate recognition component. BCR(KLHL42) is involved in ubiquitination of KATNA1. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, MACROH2A1 and DAXX, GLI2 and GLI3. Can also form a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B) (PubMed:22358839, PubMed:27716508). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; by mediating ubiquitination of WNK4 (PubMed:23387299, PubMed:23453970, PubMed:23576762). The BCR(KLHL20) E3 ubiquitin ligase complex is involved in interferon response and anterograde Golgi to endosome transport: it mediates both ubiquitination leading to degradation and 'Lys-33'-linked ubiquitination (PubMed:20389280, PubMed:21670212, PubMed:21840486, PubMed:24768539). The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB (PubMed:19995937). The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation (PubMed:23455478). The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway (PubMed:29769719). The BCR(KLHL25) ubiquitin ligase complex is involved in translational homeostasis by mediating ubiquitination and subsequent degradation of hypophosphorylated EIF4EBP1 (4E-BP1) (PubMed:22578813). The BCR(KLHL25) ubiquitin ligase complex is also involved in lipid synthesis by mediating ubiquitination and degradation of ACLY (PubMed:27664236). The BCR(KBTBD8) complex acts by mediating monoubiquitination of NOLC1 and TCOF1, leading to remodel the translational program of differentiating cells in favor of neural crest specification (PubMed:26399832). Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41 (PubMed:15983046). In concert with ATF2 and RBX1, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. The BCR(KCTD17) E3 ubiquitin ligase complex mediates ubiquitination and degradation of TCHP, a down-regulator of cilium assembly, thereby inducing ciliogenesis (PubMed:25270598). The BCR(KLHL24) E3 ubiquitin ligase complex mediates ubiquitination of KRT14, controls KRT14 levels during keratinocytes differentiation, and is essential for skin integrity (PubMed:27798626). The BCR(KLHL18) E3 ubiquitin ligase complex mediates the ubiquitination of AURKA leading to its activation at the centrosome which is required for initiating mitotic entry (PubMed:23213400). The BCR(KEAP1) E3 ubiquitin ligase complex acts as a key sensor of oxidative and electrophilic stress by mediating ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes (PubMed:15601839, PubMed:16006525). As part of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex functions mediates 'Lys-48' ubiquitination and proteasomal degradation of TIAM1 (PubMed:25684205). By controlling the ubiquitination of that RAC1 guanine exchange factors (GEF), regulates RAC1 signal transduction and downstream biological processes including the organization of the cytoskeleton, cell migration and cell proliferation (PubMed:25684205). The BCR(KBTBD4) E3 ubiquitin ligase complex targets CoREST corepressor complex components RCOR1, KDM1A/LSD1 and HDAC2 for proteasomal degradation with RCOR1 likely to be the primary target while degradation of KDM1A and HDAC2 is likely due to their association with RCOR1 (PubMed:33417871). It also targets RCOR3, MIER2 and MIER3 for proteasomal degradation as well as associated proteins ZNF217 and RREB1 with degradation being dependent on the presence of an ELM2 domain in the target proteins (PubMed:36997086). The BCR(ARMC5) complex mediates premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation by mediating ubiquitination of Pol II subunit POLR2A (PubMed:35687106, PubMed:38225631, PubMed:39504960, PubMed:39667934). Required for 'Lys-63'-linked ubiquitination of large ribosomal subunit protein MRPL12 (PubMed:37526061). Protects against human enterovirus D68 infection by mediating the ubiquitination and subsequent degradation of viral protein VP1 (PubMed:40396757)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27664236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35687106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38225631"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39504960"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39667934"}],"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9JLV5"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10230407"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10500095"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12609982"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14528312"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15107402"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15601839"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15897469"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15983046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16524876"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17543862"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18397884"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18573101"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19261606"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19995937"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20389280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21670212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21840486"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22085717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22358839"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22578813"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22632832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22748208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23135275"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23201271"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23213400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23349464"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23387299"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23453970"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23455478"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23573258"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23576762"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23776465"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24076655"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24192928"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24768539"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25270598"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25349211"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25684205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26399832"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26906416"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27561354"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27565346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27664236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27708159"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27798626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29276004"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29695787"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32341456"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33417871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35687106"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35862218"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38225631"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39504960"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39667934"},{"evidenceCode":"ECO:0000305"}],"value":"Forms neddylation-dependent homodimers. Component of multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes formed of CUL3, RBX1 and a variable BTB domain-containing protein acting as both, adapter to cullin and substrate recognition subunit. The BCR complex may be active as a heterodimeric complex, in which NEDD8, covalently attached to one CUL3 molecule, binds to the C-terminus of a second CUL3 molecule. Interacts with RBX1, RNF7, CYCE and TIP120A/CAND1 (PubMed:10230407, PubMed:10500095, PubMed:12609982). Part of the BCR(SPOP) containing SPOP, and of BCR containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL. Part of the probable BCR(KLHL9-KLHL13) complex with BTB domain proteins KLHL9 and KLHL13. Part of the BCR(KLHL41) complex containing KLHL41. Component of the BCR(KLHL12) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL12 and RBX1. Component of the BCR(KLHL3) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL3 and RBX1 (Probable). Part of the BCR(ENC1) complex containing ENC1. Part of a complex consisting of BMI1/PCGF4, CUL3 and SPOP. Part of a complex consisting of BRMS1, CUL3 and SPOP. Component of the BCR(KLHL21) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL21 and RBX1. Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL22 and RBX1. Component of the BCR(KLHL25) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL25 and RBX1 (PubMed:22578813, PubMed:27664236). Part of a complex consisting of MACROH2A1, CUL3 and SPOP. Component of the BCR(KLHL42) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL42. Interacts with KLHL42 (via the BTB domain). Interacts with KATNA1; the interaction is enhanced by KLHL42. Component of the BCR(KBTBD8) E3 ubiquitin ligase complex, at least composed of CUL3, KBTBD8 and RBX1 (PubMed:26399832). Interacts with KCTD5, KLHL9, KLHL11, KLHL13, GAN, ZBTB16, KLHL3, KLHL15, KLHL20, KLHL36, GMCL2, BTBD1. Part of a complex that contains CUL3, RBX1 and GAN. Interacts (via BTB domain) with KLHL17; the interaction regulates surface GRIK2 expression. Interacts with KCTD7. Part of the BCR(GAN) complex containing GAN. Part of the BCR(KEAP1) complex containing KEAP1 (PubMed:15601839, PubMed:15983046, PubMed:32341456). Interacts with KLHL10 (By similarity). Interacts with KAT5 and ATF2. Interacts with KCTD17 in the BCR(KCTD17) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD17 and RBX1 (PubMed:25270598). Interacts (when neddylated) with ARIH1; leading to activate the E3 ligase activity of ARIH1 (PubMed:24076655, PubMed:27565346). Interacts with COPS9 isoform 2 (PubMed:23776465). Interacts with PPP2R5B; this interaction is indirect and mediated through KLHL15-binding and leads to PPP2R5B proteasomal degradation (PubMed:23135275). Interacts with RBBP8/CtIP; this interaction is indirect and mediated through KLHL15-binding and leads to RBBP8 proteasomal degradation (PubMed:27561354). Interacts with KLHL24 in the BCR(KLHL24) E3 ubiquitin ligase complex, composed of CUL3, RBX1 and KLHL24 (PubMed:27798626). Interacts with RHOBTB2 (PubMed:15107402, PubMed:29276004). Interacts with AURKA and KLHL18 (via BTB domain) (PubMed:23213400). Interacts (unneddylated form) with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5; these interactions promote the cullin neddylation (PubMed:23201271, PubMed:24192928, PubMed:25349211, PubMed:26906416). Component of a BCR3 (BTB-CUL3-RBX1) E3 ubiquitin ligase complex, also named Cul3-RING ubiquitin ligase complex CUL3(KBTBD6/7), composed of CUL3, RBX1, KBTBD6 and KBTBD7 (PubMed:25684205). Component of the BCR(KBTBD2) E3 ubiquitin ligase complex, at least composed of CUL3, KBTBD2 and RBX1. Interacts with KBTBD2 (via the BTB domain) (PubMed:27708159). Component of the BCR(KBTBD4) E3 ubiquitin ligase complex, at least composed of CUL3, KBTBD4 and RBX1 (PubMed:33417871). Component of the BCR(ARMC5) E3 ubiquitin ligase complex, composed of CUL3, ARMC5 and RBX1 (PubMed:35862218, PubMed:35687106, PubMed:38225631, PubMed:39504960, PubMed:39667934). Component of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex, composed of at least CUL3, RBX1 and KLHL6 (PubMed:29695787)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30819806"}],"value":"(Microbial infection) Interacts with vaccinia virus protein A55/KBTB1; this interaction may direct the CUL3-RING E3 ligase complex to degrade cellular/viral target proteins that are normally 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