BACD2_HUMAN
ID BACD2_HUMAN Reviewed; 316 AA.
AC Q13829; B7Z6M4; Q5TZQ1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2;
DE Short=hBACURD2;
DE AltName: Full=BTB/POZ domain-containing protein TNFAIP1;
DE AltName: Full=Protein B12;
DE AltName: Full=Tumor necrosis factor, alpha-induced protein 1, endothelial;
GN Name=TNFAIP1; Synonyms=BACURD2, EDP1;
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] (ISOFORM 1).
RC TISSUE=Endothelial cell;
RX PubMed=1370465; DOI=10.1016/s0021-9258(18)48432-3;
RA Wolf F.W., Marks R.M., Sarma V., Byers M.G., Katz R.W., Shows T.B.,
RA Dixit V.M.;
RT "Characterization of a novel tumor necrosis factor-alpha-induced
RT endothelial primary response gene.";
RL J. Biol. Chem. 267:1317-1326(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
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] (ISOFORM 1).
RC TISSUE=Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-280, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RHOB.
RX PubMed=19637314; DOI=10.1002/ijc.24617;
RA Kim D.M., Chung K.S., Choi S.J., Jung Y.J., Park S.K., Han G.H., Ha J.S.,
RA Song K.B., Choi N.S., Kim H.M., Won M., Seo Y.S.;
RT "RhoB induces apoptosis via direct interaction with TNFAIP1 in HeLa
RT cells.";
RL Int. J. Cancer 125:2520-2527(2009).
RN [11]
RP INTERACTION WITH CSNK2B AND PCNA, PHOSPHORYLATION AT SER-280, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF SER-142; THR-237; SER-265; SER-278 AND
RP SER-280.
RX PubMed=19851886; DOI=10.1007/s11033-009-9863-1;
RA Yang L., Liu N., Hu X., Zhang W., Wang T., Li H., Zhang B., Xiang S.,
RA Zhou J., Zhang J.;
RT "CK2 phosphorylates TNFAIP1 to affect its subcellular localization and
RT interaction with PCNA.";
RL Mol. Biol. Rep. 37:2967-2973(2010).
RN [12]
RP FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE
RP COMPLEX, INTERACTION WITH RHOA, AND MUTAGENESIS OF 71-ILE--ILE-73.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-280, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex involved in regulation of cytoskeleton
CC structure. The BCR(TNFAIP1) E3 ubiquitin ligase complex mediates the
CC ubiquitination of RHOA, leading to its degradation by the proteasome,
CC thereby regulating the actin cytoskeleton and cell migration. Its
CC interaction with RHOB may regulate apoptosis. May enhance the PCNA-
CC dependent DNA polymerase delta activity. {ECO:0000269|PubMed:19637314,
CC ECO:0000269|PubMed:19782033}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the BCR(TNFAIP1) E3 ubiquitin ligase complex, at
CC least composed of CUL3, TNFAIP1/BACURD2 and RBX1. Interacts with RHOA;
CC with a preference for RhoA-GDP. Interacts with RHOB. Interacts with
CC PCNA. Interacts with CSNK2B. {ECO:0000269|PubMed:19637314,
CC ECO:0000269|PubMed:19782033, ECO:0000269|PubMed:19851886}.
CC -!- INTERACTION:
CC Q13829; P02649: APOE; NbExp=3; IntAct=EBI-2505861, EBI-1222467;
CC Q13829; Q9H6L4: ARMC7; NbExp=6; IntAct=EBI-2505861, EBI-742909;
CC Q13829; P54253: ATXN1; NbExp=3; IntAct=EBI-2505861, EBI-930964;
CC Q13829; Q7Z479: CAPN7; NbExp=3; IntAct=EBI-2505861, EBI-10213454;
CC Q13829; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-2505861, EBI-1765641;
CC Q13829; Q9H257: CARD9; NbExp=3; IntAct=EBI-2505861, EBI-751319;
CC Q13829; Q16543: CDC37; NbExp=3; IntAct=EBI-2505861, EBI-295634;
CC Q13829; Q13618: CUL3; NbExp=4; IntAct=EBI-2505861, EBI-456129;
CC Q13829; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-2505861, EBI-6255981;
CC Q13829; Q9NQT4: EXOSC5; NbExp=6; IntAct=EBI-2505861, EBI-371876;
CC Q13829; P01100: FOS; NbExp=3; IntAct=EBI-2505861, EBI-852851;
CC Q13829; P50440: GATM; NbExp=3; IntAct=EBI-2505861, EBI-2552594;
CC Q13829; P14136: GFAP; NbExp=3; IntAct=EBI-2505861, EBI-744302;
CC Q13829; P62993: GRB2; NbExp=3; IntAct=EBI-2505861, EBI-401755;
CC Q13829; O14929: HAT1; NbExp=3; IntAct=EBI-2505861, EBI-2339359;
CC Q13829; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-2505861, EBI-5460660;
CC Q13829; P42858: HTT; NbExp=3; IntAct=EBI-2505861, EBI-466029;
CC Q13829; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-2505861, EBI-1055254;
CC Q13829; Q9H3F6: KCTD10; NbExp=6; IntAct=EBI-2505861, EBI-2505886;
CC Q13829; Q8WZ19: KCTD13; NbExp=11; IntAct=EBI-2505861, EBI-742916;
CC Q13829; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2505861, EBI-739832;
CC Q13829; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2505861, EBI-741158;
CC Q13829; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-2505861, EBI-398874;
CC Q13829; O15160: POLR1C; NbExp=9; IntAct=EBI-2505861, EBI-1055079;
CC Q13829; P54619: PRKAG1; NbExp=3; IntAct=EBI-2505861, EBI-1181439;
CC Q13829; P25786: PSMA1; NbExp=3; IntAct=EBI-2505861, EBI-359352;
CC Q13829; P62745: RHOB; NbExp=5; IntAct=EBI-2505861, EBI-602647;
CC Q13829; P00441: SOD1; NbExp=3; IntAct=EBI-2505861, EBI-990792;
CC Q13829; P12931: SRC; NbExp=3; IntAct=EBI-2505861, EBI-621482;
CC Q13829; O75716: STK16; NbExp=3; IntAct=EBI-2505861, EBI-749295;
CC Q13829; Q13829: TNFAIP1; NbExp=4; IntAct=EBI-2505861, EBI-2505861;
CC Q13829; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-2505861, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endosome. Note=Colocalizes
CC with RHOB in endosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13829-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13829-2; Sequence=VSP_056029;
CC -!- INDUCTION: By TNF, IL1B/interleukin-1 beta and bacterial
CC lipopolysaccharides (LPS).
CC -!- PTM: Phosphorylation at Ser-280 by CK2 facilitates the nucleus
CC localization and increases interaction with PCNA.
CC {ECO:0000269|PubMed:19851886}.
CC -!- SIMILARITY: Belongs to the BACURD family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/tnfaip1/";
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DR EMBL; M80783; AAA58385.1; -; mRNA.
DR EMBL; AK300584; BAH13310.1; -; mRNA.
DR EMBL; AK312387; BAG35304.1; -; mRNA.
DR EMBL; CR456819; CAG33100.1; -; mRNA.
DR EMBL; BT020121; AAV38924.1; -; mRNA.
DR EMBL; AY065346; AAL38649.1; -; Genomic_DNA.
DR EMBL; AC002094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471159; EAW51077.1; -; Genomic_DNA.
DR EMBL; BC001643; AAH01643.1; -; mRNA.
DR EMBL; BC001949; AAH01949.1; -; mRNA.
DR CCDS; CCDS11227.1; -. [Q13829-1]
DR RefSeq; NP_066960.1; NM_021137.4. [Q13829-1]
DR AlphaFoldDB; Q13829; -.
DR SMR; Q13829; -.
DR BioGRID; 112981; 84.
DR IntAct; Q13829; 69.
DR MINT; Q13829; -.
DR STRING; 9606.ENSP00000226225; -.
DR iPTMnet; Q13829; -.
DR PhosphoSitePlus; Q13829; -.
DR BioMuta; TNFAIP1; -.
DR DMDM; 2833248; -.
DR EPD; Q13829; -.
DR jPOST; Q13829; -.
DR MassIVE; Q13829; -.
DR MaxQB; Q13829; -.
DR PaxDb; Q13829; -.
DR PeptideAtlas; Q13829; -.
DR PRIDE; Q13829; -.
DR ProteomicsDB; 59698; -. [Q13829-1]
DR ProteomicsDB; 6790; -.
DR Antibodypedia; 2839; 299 antibodies from 32 providers.
DR DNASU; 7126; -.
DR Ensembl; ENST00000226225.7; ENSP00000226225.2; ENSG00000109079.10. [Q13829-1]
DR Ensembl; ENST00000544907.6; ENSP00000440749.2; ENSG00000109079.10. [Q13829-2]
DR GeneID; 7126; -.
DR KEGG; hsa:7126; -.
DR MANE-Select; ENST00000226225.7; ENSP00000226225.2; NM_021137.5; NP_066960.1.
DR UCSC; uc002hay.4; human. [Q13829-1]
DR CTD; 7126; -.
DR DisGeNET; 7126; -.
DR GeneCards; TNFAIP1; -.
DR HGNC; HGNC:11894; TNFAIP1.
DR HPA; ENSG00000109079; Low tissue specificity.
DR MIM; 191161; gene.
DR neXtProt; NX_Q13829; -.
DR OpenTargets; ENSG00000109079; -.
DR PharmGKB; PA36591; -.
DR VEuPathDB; HostDB:ENSG00000109079; -.
DR eggNOG; KOG2716; Eukaryota.
DR GeneTree; ENSGT00950000183143; -.
DR HOGENOM; CLU_060008_2_0_1; -.
DR InParanoid; Q13829; -.
DR OMA; EMSGDTC; -.
DR OrthoDB; 1306250at2759; -.
DR PhylomeDB; Q13829; -.
DR TreeFam; TF315649; -.
DR PathwayCommons; Q13829; -.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q13829; -.
DR SIGNOR; Q13829; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7126; 15 hits in 1115 CRISPR screens.
DR ChiTaRS; TNFAIP1; human.
DR GeneWiki; TNFAIP1; -.
DR GenomeRNAi; 7126; -.
DR Pharos; Q13829; Tbio.
DR PRO; PR:Q13829; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q13829; protein.
DR Bgee; ENSG00000109079; Expressed in hair follicle and 209 other tissues.
DR ExpressionAtlas; Q13829; baseline and differential.
DR Genevisible; Q13829; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030332; F:cyclin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IEP: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: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 Alternative splicing; Cytoplasm; Endosome; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..316
FT /note="BTB/POZ domain-containing adapter for CUL3-mediated
FT RhoA degradation protein 2"
FT /id="PRO_0000191300"
FT DOMAIN 28..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 268..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 280
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:19851886,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056029"
FT MUTAGEN 71..73
FT /note="ILI->AAA: Abolishes interaction with CUL3 and
FT induces abnormal actin stress fibers."
FT /evidence="ECO:0000269|PubMed:19782033"
FT MUTAGEN 142
FT /note="S->A: Does not affect phosphorylation level; when
FT associated with A-237."
FT /evidence="ECO:0000269|PubMed:19851886"
FT MUTAGEN 237
FT /note="T->A: Does not affect phosphorylation level; when
FT associated with A-142."
FT /evidence="ECO:0000269|PubMed:19851886"
FT MUTAGEN 265
FT /note="S->A: Does not affect phosphorylation level."
FT /evidence="ECO:0000269|PubMed:19851886"
FT MUTAGEN 278
FT /note="S->A: Slightly impairs phosphorylation level."
FT /evidence="ECO:0000269|PubMed:19851886"
FT MUTAGEN 280
FT /note="S->A: Strongly impairs phosphorylation level."
FT /evidence="ECO:0000269|PubMed:19851886"
SQ SEQUENCE 316 AA; 36204 MW; D20B810A00507DCF CRC64;
MSGDTCLCPA SGAKPKLSGF KGGGLGNKYV QLNVGGSLYY TTVRALTRHD TMLKAMFSGR
MEVLTDKEGW ILIDRCGKHF GTILNYLRDD TITLPQNRQE IKELMAEAKY YLIQGLVNMC
QSALQDKKDS YQPVCNIPII TSLKEEERLI ESSTKPVVKL LYNRSNNKYS YTSNSDDHLL
KNIELFDKLS LRFNGRVLFI KDVIGDEICC WSFYGQGRKL AEVCCTSIVY ATEKKQTKVE
FPEARIYEET LNVLLYETPR VPDNSLLEAT SRSRSQASPS EDEETFELRD RVRRIHVKRY
STYDDRQLGH QSTHRD
