PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22219362-1 2012 Cullin-3 (Cul3) functions as a scaffolding protein in the Bric-a-brac, Tramtrack, Broad-complex (BTB)-Cul3-Rbx1 ubiquitin E3 ligase complex. btb 97-100 cullin 3 Homo sapiens 0-8 22709582-1 2012 RhoBTB (BTB stands for broad-complex, tramtrack, bric a brac) proteins are tumor suppressors involved in the formation of cullin 3 (Cul3)-dependent ubiquitin ligase complexes. btb 3-6 cullin 3 Homo sapiens 122-130 22709582-1 2012 RhoBTB (BTB stands for broad-complex, tramtrack, bric a brac) proteins are tumor suppressors involved in the formation of cullin 3 (Cul3)-dependent ubiquitin ligase complexes. btb 3-6 cullin 3 Homo sapiens 132-136 22219362-1 2012 Cullin-3 (Cul3) functions as a scaffolding protein in the Bric-a-brac, Tramtrack, Broad-complex (BTB)-Cul3-Rbx1 ubiquitin E3 ligase complex. btb 97-100 cullin 3 Homo sapiens 10-14 22219362-1 2012 Cullin-3 (Cul3) functions as a scaffolding protein in the Bric-a-brac, Tramtrack, Broad-complex (BTB)-Cul3-Rbx1 ubiquitin E3 ligase complex. btb 97-100 cullin 3 Homo sapiens 102-106 21472142-6 2011 Indeed, the novel genes (KCASH2(KCTD21) and KCASH3(KCTD6)) share with REN(KCTD11) a number of features, such as a BTB domain required for the formation of a Cullin3 ubiquitin ligase complex and HDAC1 ubiquitination and degradation capability, suppressing the acetylation-dependent Hh/Gli signaling. btb 114-117 cullin 3 Homo sapiens 157-164 15601839-6 2005 Here we report that the human BTB-Kelch protein Keap1, a negative regulator of the antioxidative transcription factor Nrf2, binds to CUL3 and Nrf2 via its BTB and Kelch domains, respectively. btb 30-33 cullin 3 Homo sapiens 133-137 19818708-0 2009 Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. btb 81-84 cullin 3 Homo sapiens 85-89 30814284-3 2019 One family of VACV proteins are the BTB-BACK (broad-complex, tram-trac, and bric-a-brac [BTB] and C-terminal Kelch [BACK]) domain-containing, Kelch-like (BBK) family of predicted cullin-3 E3 ligase adaptors: A55, C2, and F3. btb 36-39 cullin 3 Homo sapiens 179-187 31898230-4 2020 Differently, a single BTB-containing adaptor molecule utilizing two protein interaction sites can link the CUL3 scaffold to the substrate, forming as many as 188 CUL3-BTB E3 ligase complexes in mammals. btb 22-25 cullin 3 Homo sapiens 107-111 30586619-2 2019 In CUL3-based CRLs, the substrate specificity is conferred by the interaction with one of around 183 existing BTB proteins, implying a broad spectrum of possible ubiquitylation signals and possible direct ubiquitylation substrates. btb 110-113 cullin 3 Homo sapiens 3-7 28743001-3 2017 GCL, a conserved BTB (Broad-complex, Tramtrack, and Bric-a-brac) protein, is a substrate-specific adaptor for Cullin3-RING ubiquitin ligase complex (CRL3GCL). btb 17-20 cullin 3 Homo sapiens 110-117 28963344-7 2017 SAXS data and structural modelling indicate that Cul3 may stabilize closed BTB pentamers by binding across their BTB-BTB interfaces. btb 75-78 cullin 3 Homo sapiens 49-53 28963344-7 2017 SAXS data and structural modelling indicate that Cul3 may stabilize closed BTB pentamers by binding across their BTB-BTB interfaces. btb 113-116 cullin 3 Homo sapiens 49-53 28963344-7 2017 SAXS data and structural modelling indicate that Cul3 may stabilize closed BTB pentamers by binding across their BTB-BTB interfaces. btb 113-116 cullin 3 Homo sapiens 49-53 30819806-4 2019 We report that the N-terminal BTB-BACK (BB) domain of A55 binds directly to the Cul3 N-terminal domain (Cul3-NTD), forming a 2:2 complex in solution. btb 30-33 cullin 3 Homo sapiens 80-84 30819806-4 2019 We report that the N-terminal BTB-BACK (BB) domain of A55 binds directly to the Cul3 N-terminal domain (Cul3-NTD), forming a 2:2 complex in solution. btb 30-33 cullin 3 Homo sapiens 104-108 30819806-5 2019 We solved the structure of an A55BB/Cul3-NTD complex from anisotropic crystals diffracting to 2.3/3.7 A resolution in the best/worst direction, revealing that the overall interaction and binding interface closely resemble the structures of cellular BTB/Cul3-NTD complexes, despite low sequence identity between A55 and cellular BTB domains. btb 249-252 cullin 3 Homo sapiens 36-40 24522926-6 2014 Significantly, expression of the BTB-only domain of EVM150 blocked NF-kappaB activation, demonstrating that EVM150 functioned independently of the kelch domain and its role as an adapter for cullin-3-based ubiquitin ligases. btb 33-36 cullin 3 Homo sapiens 191-199 26334369-7 2016 Finally, we confirm the 5:5 assembly of KCTD9/Cul3 complexes by cryo-electron microscopy and provide a molecular rationale for BTB-mediated Cul3 binding specificity in the KCTD family. btb 127-130 cullin 3 Homo sapiens 46-50 26334369-7 2016 Finally, we confirm the 5:5 assembly of KCTD9/Cul3 complexes by cryo-electron microscopy and provide a molecular rationale for BTB-mediated Cul3 binding specificity in the KCTD family. btb 127-130 cullin 3 Homo sapiens 140-144 26188516-1 2015 Based on its specific interaction with cullin3 mediated by an N-terminal BTB/POZ homologous domain, KCTD5 has been proposed to function as substrate adapter for cullin3 based ubiquitin E3 ligases. btb 73-76 cullin 3 Homo sapiens 39-46 26188516-1 2015 Based on its specific interaction with cullin3 mediated by an N-terminal BTB/POZ homologous domain, KCTD5 has been proposed to function as substrate adapter for cullin3 based ubiquitin E3 ligases. btb 73-76 cullin 3 Homo sapiens 161-168 25848797-1 2015 Cullin3 (Cul3), a key factor of protein ubiquitination, is able to interact with dozens of different proteins containing a BTB (Bric-a-brac, Tramtrack and Broad Complex) domain. btb 123-126 cullin 3 Homo sapiens 0-7 25848797-1 2015 Cullin3 (Cul3), a key factor of protein ubiquitination, is able to interact with dozens of different proteins containing a BTB (Bric-a-brac, Tramtrack and Broad Complex) domain. btb 123-126 cullin 3 Homo sapiens 9-13 25848797-6 2015 Cul3-derived staple peptides are also able to bind the BTB of the pentameric KCTD5. btb 55-58 cullin 3 Homo sapiens 0-4 25848797-7 2015 Interestingly, the affinity of these peptides is of the same order of magnitude of that reported for the interaction of full-length Cul3 with some BTB containing proteins. btb 147-150 cullin 3 Homo sapiens 132-136 27152988-6 2016 Finally, negative-stain electron micrographs of KCTD6(BTB) in complex with Cullin3 show the presence of assemblies with a five-pointed pinwheel shape. btb 54-57 cullin 3 Homo sapiens 75-82 24896564-5 2014 In addition to providing the first structural confirmation of antagonist binding to Keap1 BTB, we also present biochemical evidence that adduction of Cys 151 by CDDO is capable of inhibiting the binding of Cul3 to Keap1, and discuss how this class of compound might exert Nrf2 activation through disruption of the BTB-Cul3 interface. btb 314-317 cullin 3 Homo sapiens 206-210 23349464-2 2013 Cul3-based Cullin-RING ligases are uniquely associated with BTB adaptors that incorporate homodimerization, Cul3 assembly, and substrate recognition into a single multidomain protein, of which the best known are BTB-BACK-Kelch domain proteins, including KEAP1. btb 60-63 cullin 3 Homo sapiens 0-4 24450635-3 2014 The Cul3-based CRLs uniquely assemble with BTB (broad complex/tramtrack/bric-a-brac) proteins that also homodimerize and perform the role of both the Cullin adapter and the substrate-recognition component of the E3. btb 43-46 cullin 3 Homo sapiens 4-8 24067371-6 2013 Our own recent study identified the mitotic kinase PLK1 as a direct target of the CUL3 E3-ligase complex containing BTB-KELCH adaptor protein KLHL22. btb 116-119 cullin 3 Homo sapiens 82-86 23847398-3 2013 The Nrf2 transcription function and its degradation by the proteasomal pathway (Keap1-Nrf2-Cul3-Roc1 complex) are regulated by the cytoplasmic repressor protein, Keap1 which possesses BTB, BACK (IVR region) and Kelch domains. btb 184-187 cullin 3 Homo sapiens 91-95 23349464-2 2013 Cul3-based Cullin-RING ligases are uniquely associated with BTB adaptors that incorporate homodimerization, Cul3 assembly, and substrate recognition into a single multidomain protein, of which the best known are BTB-BACK-Kelch domain proteins, including KEAP1. btb 60-63 cullin 3 Homo sapiens 108-112 23349464-5 2013 We show that Cul3 interaction is dependent on a unique N-terminal extension sequence that packs against the 3-box in a hydrophobic groove centrally located between the BTB and BACK domains. btb 168-171 cullin 3 Homo sapiens 13-17 23573258-6 2013 Both the BTB and BACK domains contribute to the Cul3 interaction surface, and an extended model of the dimeric CRL3 complex places the two E2 binding sites in a suprafacial arrangement with respect to the presumed substrate-binding sites. btb 9-12 cullin 3 Homo sapiens 48-52