RHBT2_MOUSE
ID RHBT2_MOUSE Reviewed; 728 AA.
AC Q91V93; Q8BYU3; Q8K1A8;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Rho-related BTB domain-containing protein 2;
DE AltName: Full=Deleted in breast cancer 2 gene protein homolog;
GN Name=Rhobtb2; Synonyms=Dbc2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], 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].
RC STRAIN=C57BL/6J;
RX PubMed=12370419; DOI=10.1073/pnas.212516099;
RA Hamaguchi M., Meth J.L., von Klitzing C., Wei W., Esposito D., Rodgers L.,
RA Walsh T., Welcsh P., King M.C., Wigler M.H.;
RT "DBC2, a candidate for a tumor suppressor gene involved in breast cancer.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13647-13652(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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).
CC -!- SUBUNIT: Interacts with HSP90AA1 and HSP90AB1. Interacts with CUL3.
CC {ECO:0000250|UniProtKB:Q9BYZ6}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, with highest expression
CC in brain. {ECO:0000269|PubMed:12426103}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AF420001; AAL16061.1; -; mRNA.
DR EMBL; AF420002; AAL16063.1; -; Genomic_DNA.
DR EMBL; AK038196; BAC29946.1; -; mRNA.
DR EMBL; BC026836; AAH26836.1; -; mRNA.
DR EMBL; BC056954; AAH56954.1; -; mRNA.
DR CCDS; CCDS27244.1; -.
DR RefSeq; NP_705734.4; NM_153514.5.
DR AlphaFoldDB; Q91V93; -.
DR SMR; Q91V93; -.
DR BioGRID; 232933; 1.
DR STRING; 10090.ENSMUSP00000022665; -.
DR iPTMnet; Q91V93; -.
DR PhosphoSitePlus; Q91V93; -.
DR MaxQB; Q91V93; -.
DR PaxDb; Q91V93; -.
DR PRIDE; Q91V93; -.
DR ProteomicsDB; 253271; -.
DR Antibodypedia; 22697; 110 antibodies from 22 providers.
DR DNASU; 246710; -.
DR Ensembl; ENSMUST00000022665; ENSMUSP00000022665; ENSMUSG00000022075.
DR GeneID; 246710; -.
DR KEGG; mmu:246710; -.
DR UCSC; uc011znx.1; mouse.
DR CTD; 23221; -.
DR MGI; MGI:2180557; Rhobtb2.
DR VEuPathDB; HostDB:ENSMUSG00000022075; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000158918; -.
DR HOGENOM; CLU_015517_0_0_1; -.
DR InParanoid; Q91V93; -.
DR OMA; CLCFTGG; -.
DR OrthoDB; 533443at2759; -.
DR PhylomeDB; Q91V93; -.
DR TreeFam; TF323347; -.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR BioGRID-ORCS; 246710; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rhobtb2; mouse.
DR PRO; PR:Q91V93; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91V93; protein.
DR Bgee; ENSMUSG00000022075; Expressed in pigmented layer of retina and 223 other tissues.
DR Genevisible; Q91V93; MM.
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: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 2: Evidence at transcript level;
KW GTP-binding; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..728
FT /note="Rho-related BTB domain-containing protein 2"
FT /id="PRO_0000198963"
FT DOMAIN 266..333
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..728
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 CONFLICT 191..192
FT /note="VA -> FD (in Ref. 1; AAL16061/AAL16063)"
FT /evidence="ECO:0000305"
FT CONFLICT 222..223
FT /note="RN -> KK (in Ref. 1; AAL16061/AAL16063)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="R -> K (in Ref. 1; AAL16061/AAL16063)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..237
FT /note="LPPK -> RNSE (in Ref. 1; AAL16061/AAL16063)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="R -> G (in Ref. 4; AAH26836)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="F -> L (in Ref. 4; AAH26836)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="T -> A (in Ref. 1; AAL16061/AAL16063)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="D -> G (in Ref. 1; AAL16061/AAL16063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 82650 MW; 2B7CB52380CFD6D1 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
SEGELGGPSG SGGPRPEDHR SHPEQHHHHH HHHHGRDFLL RAASFDVCES VDEAGGSGPA
GLRASTSDGI LRGNGTGYLP GRGRVLSSWS RAFVSIQEEM AEDPLTFKSR LMVVVKMDNS
IQPGPFRAVL KYLYTGELGE NERDLMHIAH IAELLEVFDL RMMVANILNN EAFMNQEITK
AFHVRRTNRV KECLAKGTFS DVTFILDDGT ISAHKPLLIS SCDWMAAMFG GPFVESSTRE
VVFPYTSKSC MRAVLEYLYT GMFTSSPDLD DMKLIVLANR LCLPHLVALT EQYTVTGLME
ATQMMVDIDG DVLVFLELAQ FHCAYQLADW CLHHICTNYN NVCRKFPRDM KAMSPENQEY
FEKHRWPPVW YLKEEDHYQR ARKEREKEDY LHLRRQPKRR WLFWNSPSSP SSSAAGSASP
SSSSSAVV