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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
 
 
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