RHBT2_HUMAN
ID RHBT2_HUMAN Reviewed; 727 AA.
AC Q9BYZ6; A8K9Z8; D3DSR8; E9PBU2; E9PEI7; O94825; Q8N4A8; Q9BZK6;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Rho-related BTB domain-containing protein 2;
DE AltName: Full=Deleted in breast cancer 2 gene protein;
DE AltName: Full=p83;
GN Name=RHOBTB2; Synonyms=DBC2, KIAA0717;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=12426103; DOI=10.1016/s0378-1119(02)00980-0;
RA Ramos S., Khademi F., Somesh B.P., Rivero F.;
RT "Genomic organization and expression profile of the small GTPases of the
RT RhoBTB family in human and mouse.";
RL Gene 298:147-157(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hamaguchi M., King D., Meth J., Odawara T., Wigler M.;
RT "Homozygously deleted genes in breast cancer.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hamaguchi M., Meth J., Odawara T.;
RT "Genomic sequence for DBC2.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [10]
RP INTERACTION WITH HSP90AA1 AND HSP90AB1.
RX PubMed=26517842; DOI=10.1371/journal.pone.0141786;
RA Prince T.L., Kijima T., Tatokoro M., Lee S., Tsutsumi S., Yim K., Rivas C.,
RA Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T., Beebe K.,
RA Trepel J.B., Neckers L.;
RT "Client proteins and small molecule inhibitors display distinct binding
RT preferences for constitutive and stress-induced HSP90 isoforms and their
RT conformationally restricted mutants.";
RL PLoS ONE 10:E0141786-E0141786(2015).
RN [11]
RP VARIANT ASP-488.
RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA Gyllensten U., Pinto D., Maciel P.;
RT "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL J. Med. Genet. 53:190-199(2016).
RN [12]
RP VARIANTS DEE64 GLY-452; HIS-461; ASP-488; GLN-489 AND TRP-489,
RP CHARACTERIZATION OF VARIANTS DEE64 GLY-452; HIS-461 AND GLN-489,
RP INVOLVEMENT IN DEE64, AND INTERACTION WITH CUL3.
RX PubMed=29276004; DOI=10.1016/j.ajhg.2017.11.008;
RG Deciphering Developmental Disorders Study;
RA Straub J., Konrad E.D.H., Gruener J., Toutain A., Bok L.A., Cho M.T.,
RA Crawford H.P., Dubbs H., Douglas G., Jobling R., Johnson D., Krock B.,
RA Mikati M.A., Nesbitt A., Nicolai J., Phillips M., Poduri A.,
RA Ortiz-Gonzalez X.R., Powis Z., Santani A., Smith L., Stegmann A.P.A.,
RA Stumpel C., Vreeburg M., Fliedner A., Gregor A., Sticht H., Zweier C.;
RT "Missense variants in RHOBTB2 cause a developmental and epileptic
RT encephalopathy in humans, and altered levels cause neurological defects in
RT Drosophila.";
RL Am. J. Hum. Genet. 102:44-57(2018).
RN [13]
RP VARIANTS DEE64 HIS-461; CYS-485 AND GLN-489, CHARACTERIZATION OF VARIANTS
RP DEE64 HIS-461; CYS-485 AND GLN-489, MUTAGENESIS OF TYR-284, AND INVOLVEMENT
RP IN DEE64.
RX PubMed=29768694; DOI=10.1002/humu.23550;
RA Belal H., Nakashima M., Matsumoto H., Yokochi K., Taniguchi-Ikeda M.,
RA Aoto K., Amin M.B., Maruyama A., Nagase H., Mizuguchi T., Miyatake S.,
RA Miyake N., Iijima K., Nonoyama S., Matsumoto N., Saitsu H.;
RT "De novo variants in RHOBTB2, an atypical Rho GTPase gene, cause epileptic
RT encephalopathy.";
RL Hum. Mutat. 39:1070-1075(2018).
CC -!- SUBUNIT: Interacts with HSP90AA1 and HSP90AB1 (PubMed:26517842).
CC Interacts with CUL3 (PubMed:29276004). {ECO:0000269|PubMed:26517842,
CC ECO:0000269|PubMed:29276004}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BYZ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BYZ6-2; Sequence=VSP_054098;
CC Name=3;
CC IsoId=Q9BYZ6-3; Sequence=VSP_054099;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest levels in neural tissues.
CC Expression is also detected in fetal lung, heart, and brain.
CC {ECO:0000269|PubMed:12426103}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 64 (DEE64)
CC [MIM:618004]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE64 is an autosomal dominant form characterized by
CC onset of seizures usually in the first year of life. Seizure types are
CC variable and include focal dyscognitive and generalized tonic-clonic
CC seizures, as well as febrile seizures in the mildest affected
CC individuals. Seizures tend to respond to medical treatment.
CC {ECO:0000269|PubMed:29276004, ECO:0000269|PubMed:29768694}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34917.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA34437.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RHOBTB2ID42109ch8p21.html";
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DR EMBL; AY009093; AAG61157.1; -; mRNA.
DR EMBL; AF315385; AAK07562.1; -; Genomic_DNA.
DR EMBL; AB018260; BAA34437.2; ALT_INIT; mRNA.
DR EMBL; AK292863; BAF85552.1; -; mRNA.
DR EMBL; AC107959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63644.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63646.1; -; Genomic_DNA.
DR EMBL; BC034917; AAH34917.1; ALT_INIT; mRNA.
DR CCDS; CCDS55210.1; -. [Q9BYZ6-2]
DR CCDS; CCDS55211.1; -. [Q9BYZ6-3]
DR CCDS; CCDS6034.1; -. [Q9BYZ6-1]
DR RefSeq; NP_001153508.1; NM_001160036.1. [Q9BYZ6-2]
DR RefSeq; NP_001153509.1; NM_001160037.1. [Q9BYZ6-3]
DR RefSeq; NP_055993.2; NM_015178.2. [Q9BYZ6-1]
DR RefSeq; XP_016868740.1; XM_017013251.1. [Q9BYZ6-2]
DR AlphaFoldDB; Q9BYZ6; -.
DR SMR; Q9BYZ6; -.
DR BioGRID; 116828; 170.
DR IntAct; Q9BYZ6; 15.
DR MINT; Q9BYZ6; -.
DR STRING; 9606.ENSP00000427926; -.
DR iPTMnet; Q9BYZ6; -.
DR PhosphoSitePlus; Q9BYZ6; -.
DR BioMuta; RHOBTB2; -.
DR DMDM; 26006845; -.
DR MassIVE; Q9BYZ6; -.
DR PaxDb; Q9BYZ6; -.
DR PeptideAtlas; Q9BYZ6; -.
DR PRIDE; Q9BYZ6; -.
DR ProteomicsDB; 19297; -.
DR ProteomicsDB; 19901; -.
DR ProteomicsDB; 79744; -. [Q9BYZ6-1]
DR Antibodypedia; 22697; 110 antibodies from 22 providers.
DR DNASU; 23221; -.
DR Ensembl; ENST00000251822.7; ENSP00000251822.7; ENSG00000008853.18. [Q9BYZ6-1]
DR Ensembl; ENST00000519685.5; ENSP00000427926.1; ENSG00000008853.18. [Q9BYZ6-2]
DR Ensembl; ENST00000522948.5; ENSP00000429141.1; ENSG00000008853.18. [Q9BYZ6-3]
DR GeneID; 23221; -.
DR KEGG; hsa:23221; -.
DR MANE-Select; ENST00000251822.7; ENSP00000251822.7; NM_015178.3; NP_055993.2.
DR UCSC; uc003xcp.3; human. [Q9BYZ6-1]
DR CTD; 23221; -.
DR DisGeNET; 23221; -.
DR GeneCards; RHOBTB2; -.
DR HGNC; HGNC:18756; RHOBTB2.
DR HPA; ENSG00000008853; Tissue enhanced (lung).
DR MalaCards; RHOBTB2; -.
DR MIM; 607352; gene.
DR MIM; 618004; phenotype.
DR neXtProt; NX_Q9BYZ6; -.
DR OpenTargets; ENSG00000008853; -.
DR PharmGKB; PA38678; -.
DR VEuPathDB; HostDB:ENSG00000008853; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000158918; -.
DR HOGENOM; CLU_015517_0_0_1; -.
DR InParanoid; Q9BYZ6; -.
DR OMA; CLCFTGG; -.
DR OrthoDB; 533443at2759; -.
DR PhylomeDB; Q9BYZ6; -.
DR TreeFam; TF323347; -.
DR PathwayCommons; Q9BYZ6; -.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR SignaLink; Q9BYZ6; -.
DR BioGRID-ORCS; 23221; 14 hits in 1111 CRISPR screens.
DR ChiTaRS; RHOBTB2; human.
DR GeneWiki; RHOBTB2; -.
DR GenomeRNAi; 23221; -.
DR Pharos; Q9BYZ6; Tbio.
DR PRO; PR:Q9BYZ6; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9BYZ6; protein.
DR Bgee; ENSG00000008853; Expressed in upper lobe of left lung and 134 other tissues.
DR ExpressionAtlas; Q9BYZ6; baseline and differential.
DR Genevisible; Q9BYZ6; HS.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.30.710.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00651; BTB; 2.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00225; BTB; 2.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54695; SSF54695; 2.
DR PROSITE; PS50097; BTB; 2.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Epilepsy; GTP-binding;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..727
FT /note="Rho-related BTB domain-containing protein 2"
FT /id="PRO_0000198962"
FT DOMAIN 266..442
FT /note="BTB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 500..567
FT /note="BTB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..210
FT /note="Rho-like"
FT REGION 304..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 84..88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MQAWRKGPDGPQKTSSDSMSRLM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054098"
FT VAR_SEQ 1
FT /note="M -> MKARSRLM (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054099"
FT VARIANT 452
FT /note="A -> G (in DEE64; reduced RHOBTB2 proteasomal
FT degradation; does not affect interaction with CUL3;
FT dbSNP:rs1554504656)"
FT /evidence="ECO:0000269|PubMed:29276004"
FT /id="VAR_080812"
FT VARIANT 461
FT /note="R -> H (in DEE64; reduced RHOBTB2 proteasomal
FT degradation; does not affect interaction with CUL3;
FT dbSNP:rs1554504663)"
FT /evidence="ECO:0000269|PubMed:29276004,
FT ECO:0000269|PubMed:29768694"
FT /id="VAR_080813"
FT VARIANT 485
FT /note="R -> C (in DEE64; decreased proteasomal degradation;
FT does not affect interaction with CUL3; dbSNP:rs1563292586)"
FT /evidence="ECO:0000269|PubMed:29768694"
FT /id="VAR_080814"
FT VARIANT 488
FT /note="N -> D (in DEE64; also found in a patient with Rett
FT syndrome-like phenotype; dbSNP:rs1554504678)"
FT /evidence="ECO:0000269|PubMed:26740508,
FT ECO:0000269|PubMed:29276004"
FT /id="VAR_079030"
FT VARIANT 489
FT /note="R -> Q (in DEE64; reduced RHOBTB2 proteasomal
FT degradation; does not affect interaction with CUL3;
FT dbSNP:rs1554504684)"
FT /evidence="ECO:0000269|PubMed:29276004,
FT ECO:0000269|PubMed:29768694"
FT /id="VAR_080815"
FT VARIANT 489
FT /note="R -> W (in DEE64; dbSNP:rs1554504681)"
FT /evidence="ECO:0000269|PubMed:29276004"
FT /id="VAR_080816"
FT MUTAGEN 284
FT /note="Y->D: Results in decreased interaction with CUL3."
FT /evidence="ECO:0000269|PubMed:29768694"
FT CONFLICT 255
FT /note="C -> G (in Ref. 2; AAG61157)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="I -> F (in Ref. 6; BAF85552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 82626 MW; 25C7493B2894A1B3 CRC64;
MDSDMDYERP NVETIKCVVV GDNAVGKTRL ICARACNATL TQYQLLATHV PTVWAIDQYR
VCQEVLERSR DVVDDVSVSL RLWDTFGDHH KDRRFAYGRS DVVVLCFSIA NPNSLHHVKT
MWYPEIKHFC PRAPVILVGC QLDLRYADLE AVNRARRPLA RPIKPNEILP PEKGREVAKE
LGIPYYETSV VAQFGIKDVF DNAIRAALIS RRHLQFWKSH LRNVQRPLLQ APFLPPKPPP
PIIVVPDPPS SSEECPAHLL EDPLCADVIL VLQERVRIFA HKIYLSTSSS KFYDLFLMDL
SEGELGGPSE PGGTHPEDHQ GHSDQHHHHH HHHHGRDFLL RAASFDVCES VDEAGGSGPA
GLRASTSDGI LRGNGTGYLP GRGRVLSSWS RAFVSIQEEM AEDPLTYKSR LMVVVKMDSS
IQPGPFRAVL KYLYTGELDE NERDLMHIAH IAELLEVFDL RMMVANILNN EAFMNQEITK
AFHVRRTNRV KECLAKGTFS DVTFILDDGT ISAHKPLLIS SCDWMAAMFG GPFVESSTRE
VVFPYTSKSC MRAVLEYLYT GMFTSSPDLD DMKLIILANR LCLPHLVALT EQYTVTGLME
ATQMMVDIDG DVLVFLELAQ FHCAYQLADW CLHHICTNYN NVCRKFPRDM KAMSPENQEY
FEKHRWPPVW YLKEEDHYQR ARKEREKEDY LHLKRQPKRR WLFWNSPSSP SSSAASSSSP
SSSSAVV
