BACD1_HUMAN
ID BACD1_HUMAN Reviewed; 329 AA.
AC Q8WZ19; A8K0R5; Q96P93; Q96SA1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1 {ECO:0000303|PubMed:19782033};
DE Short=hBACURD1 {ECO:0000303|PubMed:19782033};
DE AltName: Full=BTB/POZ domain-containing protein KCTD13 {ECO:0000305};
DE AltName: Full=Polymerase delta-interacting protein 1 {ECO:0000303|PubMed:11593007};
DE AltName: Full=TNFAIP1-like protein;
GN Name=KCTD13;
GN Synonyms=BACURD1 {ECO:0000303|PubMed:19782033},
GN PDIP1 {ECO:0000303|PubMed:11593007}, POLDIP1; ORFNames=FKSG86, PP6832;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH PCNA AND
RP POLD2, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11593007; DOI=10.1073/pnas.221452098;
RA He H., Tan C.-K., Downey K.M., So A.G.;
RT "A tumor necrosis factor alpha- and interleukin 6-inducible protein that
RT interacts with the small subunit of DNA polymerase delta and proliferating
RT cell nuclear antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11979-11984(2001).
RN [2]
RP SEQUENCE REVISION.
RA He H., Tan C.-K., Downey K.M., So A.G.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Y.-G., Gong L.;
RT "Cloning and characterization of FKSG86, a novel gene encoding a TNFAIP1-
RT like protein.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE
RP COMPLEX, INTERACTION WITH RHOA, AND MUTAGENESIS OF 84-VAL--ILE-86.
RX PubMed=19782033; DOI=10.1016/j.molcel.2009.09.004;
RA Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M.,
RA Peng H.B., Shao F.;
RT "Cullin mediates degradation of RhoA through evolutionarily conserved BTB
RT adaptors to control actin cytoskeleton structure and cell movement.";
RL Mol. Cell 35:841-855(2009).
RN [10]
RP INTERACTION WITH SPRTN.
RX PubMed=22902628; DOI=10.1074/jbc.m112.400135;
RA Ghosal G., Leung J.W., Nair B.C., Fong K.W., Chen J.;
RT "Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a
RT regulator of translesion synthesis.";
RL J. Biol. Chem. 287:34225-34233(2012).
RN [11]
RP POSSIBLE DISEASE MODIFIER FOR AUTISM AND SCHIZOPHRENIA.
RX PubMed=22596160; DOI=10.1038/nature11091;
RA Golzio C., Willer J., Talkowski M.E., Oh E.C., Taniguchi Y., Jacquemont S.,
RA Reymond A., Sun M., Sawa A., Gusella J.F., Kamiya A., Beckmann J.S.,
RA Katsanis N.;
RT "KCTD13 is a major driver of mirrored neuroanatomical phenotypes of the
RT 16p11.2 copy number variant.";
RL Nature 485:363-367(2012).
RN [12]
RP POSSIBLE DISEASE MODIFIER FOR AUTISM AND SCHIZOPHRENIA.
RX PubMed=25695269; DOI=10.1016/j.neuron.2015.01.010;
RA Lin G.N., Corominas R., Lemmens I., Yang X., Tavernier J., Hill D.E.,
RA Vidal M., Sebat J., Iakoucheva L.M.;
RT "Spatiotemporal 16p11.2 protein network implicates cortical late mid-fetal
RT brain development and KCTD13-Cul3-RhoA pathway in psychiatric diseases.";
RL Neuron 85:742-754(2015).
RN [13]
RP VARIANT ASN-200.
RX PubMed=27668412; DOI=10.1097/ypg.0000000000000145;
RA Degenhardt F., Heinemann B., Strohmaier J., Pfohl M.A., Giegling I.,
RA Hofmann A., Ludwig K.U., Witt S.H., Ludwig M., Forstner A.J., Albus M.,
RA Schwab S.G., Borrmann-Hassenbach M., Lennertz L., Wagner M., Hoffmann P.,
RA Rujescu D., Maier W., Cichon S., Rietschel M., Noethen M.M.;
RT "Identification of rare variants in KCTD13 at the schizophrenia risk locus
RT 16p11.2.";
RL Psychiatr. Genet. 26:293-296(2016).
RN [14] {ECO:0007744|PDB:4UIJ}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 27-144, AND SUBUNIT.
RX PubMed=28963344; DOI=10.1042/bcj20170527;
RA Pinkas D.M., Sanvitale C.E., Bufton J.C., Sorrell F.J., Solcan N.,
RA Chalk R., Doutch J., Bullock A.N.;
RT "Structural complexity in the KCTD family of Cullin3-dependent E3 ubiquitin
RT ligases.";
RL Biochem. J. 474:3747-3761(2017).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex required for synaptic transmission
CC (PubMed:19782033). The BCR(KCTD13) E3 ubiquitin ligase complex mediates
CC the ubiquitination of RHOA, leading to its degradation by the
CC proteasome (PubMed:19782033) Degradation of RHOA regulates the actin
CC cytoskeleton and promotes synaptic transmission (By similarity).
CC {ECO:0000250|UniProtKB:Q8BGV7, ECO:0000269|PubMed:19782033}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:19782033}.
CC -!- SUBUNIT: Homotetramer; forms a two-fold symmetric tetramer in solution
CC (PubMed:28963344). Interacts with CUL3; interaction is direct and forms
CC a 5:5 heterodecamer (PubMed:28963344). Component of the BCR(KCTD13) E3
CC ubiquitin ligase complex, at least composed of CUL3, KCTD13/BACURD1 and
CC RBX1. Interacts with RHOA; with a preference for RhoA-GDP
CC (PubMed:19782033). Interacts with POLD2 and PCNA (PubMed:11593007).
CC Interacts with SPRTN (PubMed:22902628). {ECO:0000269|PubMed:11593007,
CC ECO:0000269|PubMed:19782033, ECO:0000269|PubMed:22902628,
CC ECO:0000269|PubMed:28963344}.
CC -!- INTERACTION:
CC Q8WZ19; Q9H6L4: ARMC7; NbExp=4; IntAct=EBI-742916, EBI-742909;
CC Q8WZ19; O95817: BAG3; NbExp=3; IntAct=EBI-742916, EBI-747185;
CC Q8WZ19; Q16543: CDC37; NbExp=3; IntAct=EBI-742916, EBI-295634;
CC Q8WZ19; Q13618: CUL3; NbExp=7; IntAct=EBI-742916, EBI-456129;
CC Q8WZ19; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-742916, EBI-371876;
CC Q8WZ19; P21333-2: FLNA; NbExp=3; IntAct=EBI-742916, EBI-9641086;
CC Q8WZ19; P51114: FXR1; NbExp=2; IntAct=EBI-742916, EBI-713291;
CC Q8WZ19; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-742916, EBI-739467;
CC Q8WZ19; P04792: HSPB1; NbExp=3; IntAct=EBI-742916, EBI-352682;
CC Q8WZ19; Q9H3F6: KCTD10; NbExp=4; IntAct=EBI-742916, EBI-2505886;
CC Q8WZ19; Q8WZ19: KCTD13; NbExp=6; IntAct=EBI-742916, EBI-742916;
CC Q8WZ19; O60333-2: KIF1B; NbExp=3; IntAct=EBI-742916, EBI-10975473;
CC Q8WZ19; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-742916, EBI-739832;
CC Q8WZ19; P31153: MAT2A; NbExp=3; IntAct=EBI-742916, EBI-1050743;
CC Q8WZ19; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-742916, EBI-741158;
CC Q8WZ19; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-742916, EBI-473160;
CC Q8WZ19; O15160: POLR1C; NbExp=3; IntAct=EBI-742916, EBI-1055079;
CC Q8WZ19; P60891: PRPS1; NbExp=3; IntAct=EBI-742916, EBI-749195;
CC Q8WZ19; P25786: PSMA1; NbExp=3; IntAct=EBI-742916, EBI-359352;
CC Q8WZ19; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-742916, EBI-396669;
CC Q8WZ19; Q13829: TNFAIP1; NbExp=11; IntAct=EBI-742916, EBI-2505861;
CC Q8WZ19; O76024: WFS1; NbExp=3; IntAct=EBI-742916, EBI-720609;
CC Q8WZ19; Q96E35: ZMYND19; NbExp=7; IntAct=EBI-742916, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11593007}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
CC {ECO:0000269|PubMed:11593007}.
CC -!- INDUCTION: By TNF and IL6/interleukin-6. {ECO:0000269|PubMed:11593007}.
CC -!- DISEASE: Note=The gene represented in this entry may act as a disease
CC modifier for autism and schizophrenia associated with recurrent
CC deletions and duplications of chromosome 16p11.2 region
CC (PubMed:22596160, PubMed:25695269). {ECO:0000269|PubMed:22596160,
CC ECO:0000269|PubMed:25695269}.
CC -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}.
CC -!- CAUTION: Baed on animal models in mouse and zebrafish, it was suggested
CC that KCTD13 is the major factor inducing the macrocephaly phenotype
CC associated with the 16p11.2 deletion (PubMed:22596160). However, a
CC subsequent report showed that KCTD13 does not play a role in brain
CC size. {ECO:0000269|PubMed:22596160}.
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DR EMBL; AF401315; AAL14962.2; -; mRNA.
DR EMBL; AY027918; AAK27301.1; -; mRNA.
DR EMBL; AF289573; AAL55757.1; -; mRNA.
DR EMBL; AK289630; BAF82319.1; -; mRNA.
DR EMBL; AC120114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471238; EAW79969.1; -; Genomic_DNA.
DR EMBL; BC036228; AAH36228.1; -; mRNA.
DR CCDS; CCDS10661.1; -.
DR RefSeq; NP_849194.1; NM_178863.4.
DR PDB; 4UIJ; X-ray; 2.70 A; A/B/C/D=27-144.
DR PDBsum; 4UIJ; -.
DR AlphaFoldDB; Q8WZ19; -.
DR SMR; Q8WZ19; -.
DR BioGRID; 129001; 50.
DR IntAct; Q8WZ19; 36.
DR MINT; Q8WZ19; -.
DR STRING; 9606.ENSP00000455785; -.
DR iPTMnet; Q8WZ19; -.
DR PhosphoSitePlus; Q8WZ19; -.
DR BioMuta; KCTD13; -.
DR DMDM; 51701604; -.
DR EPD; Q8WZ19; -.
DR jPOST; Q8WZ19; -.
DR MassIVE; Q8WZ19; -.
DR MaxQB; Q8WZ19; -.
DR PaxDb; Q8WZ19; -.
DR PeptideAtlas; Q8WZ19; -.
DR PRIDE; Q8WZ19; -.
DR ProteomicsDB; 75205; -.
DR Antibodypedia; 13396; 145 antibodies from 18 providers.
DR DNASU; 253980; -.
DR Ensembl; ENST00000308768.9; ENSP00000311202.5; ENSG00000174943.11.
DR Ensembl; ENST00000568000.6; ENSP00000455785.1; ENSG00000174943.11.
DR GeneID; 253980; -.
DR KEGG; hsa:253980; -.
DR MANE-Select; ENST00000568000.6; ENSP00000455785.1; NM_178863.5; NP_849194.1.
DR UCSC; uc002duv.5; human.
DR CTD; 253980; -.
DR DisGeNET; 253980; -.
DR GeneCards; KCTD13; -.
DR HGNC; HGNC:22234; KCTD13.
DR HPA; ENSG00000174943; Tissue enhanced (brain, testis).
DR MIM; 608947; gene.
DR neXtProt; NX_Q8WZ19; -.
DR OpenTargets; ENSG00000174943; -.
DR PharmGKB; PA134907908; -.
DR VEuPathDB; HostDB:ENSG00000174943; -.
DR eggNOG; KOG2716; Eukaryota.
DR GeneTree; ENSGT00950000183143; -.
DR HOGENOM; CLU_060008_0_0_1; -.
DR InParanoid; Q8WZ19; -.
DR OMA; PPLENCA; -.
DR OrthoDB; 1306250at2759; -.
DR PhylomeDB; Q8WZ19; -.
DR TreeFam; TF315649; -.
DR PathwayCommons; Q8WZ19; -.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q8WZ19; -.
DR SIGNOR; Q8WZ19; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 253980; 14 hits in 1088 CRISPR screens.
DR ChiTaRS; KCTD13; human.
DR GeneWiki; KCTD13; -.
DR GenomeRNAi; 253980; -.
DR Pharos; Q8WZ19; Tbio.
DR PRO; PR:Q8WZ19; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8WZ19; protein.
DR Bgee; ENSG00000174943; Expressed in right testis and 158 other tissues.
DR ExpressionAtlas; Q8WZ19; baseline and differential.
DR Genevisible; Q8WZ19; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR045068; BACURD1-3.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR PANTHER; PTHR11145; PTHR11145; 1.
DR Pfam; PF02214; BTB_2; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autism; Autism spectrum disorder; Disease variant; Nucleus;
KW Reference proteome; Schizophrenia; Ubl conjugation pathway.
FT CHAIN 1..329
FT /note="BTB/POZ domain-containing adapter for CUL3-mediated
FT RhoA degradation protein 1"
FT /id="PRO_0000191297"
FT DOMAIN 41..109
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 200
FT /note="D -> N (found in a patient with schizophrenia;
FT unknown pathological significance; dbSNP:rs774536350)"
FT /evidence="ECO:0000269|PubMed:27668412"
FT /id="VAR_080045"
FT MUTAGEN 84..86
FT /note="VLI->AAA: Abolishes interaction with CUL3 and
FT induces abnormal actin stress fibers."
FT /evidence="ECO:0000269|PubMed:19782033"
FT CONFLICT 251
FT /note="K -> N (in Ref. 3; AAK27301)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="K -> R (in Ref. 3; AAK27301)"
FT /evidence="ECO:0000305"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4UIJ"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:4UIJ"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:4UIJ"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4UIJ"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:4UIJ"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4UIJ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4UIJ"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4UIJ"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:4UIJ"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:4UIJ"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:4UIJ"
SQ SEQUENCE 329 AA; 36357 MW; 17A8AC2DBE81EE78 CRC64;
MSAEASGPAA AAAPSLEAPK PSGLEPGPAA YGLKPLTPNS KYVKLNVGGS LHYTTLRTLT
GQDTMLKAMF SGRVEVLTDA GGWVLIDRSG RHFGTILNYL RDGSVPLPES TRELGELLGE
ARYYLVQGLI EDCQLALQQK RETLSPLCLI PMVTSPREEQ QLLASTSKPV VKLLHNRSNN
KYSYTSTSDD NLLKNIELFD KLALRFHGRL LFLKDVLGDE ICCWSFYGQG RKIAEVCCTS
IVYATEKKQT KVEFPEARIF EETLNILIYE TPRGPDPALL EATGGAAGAG GAGRGEDEEN
REHRVRRIHV RRHITHDERP HGQQIVFKD
