ID   RHBT1_HUMAN             Reviewed;         696 AA.
AC   O94844;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=Rho-related BTB domain-containing protein 1;
GN   Name=RHOBTB1; Synonyms=KIAA0740;
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], 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 [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   -!- INTERACTION:
CC       O94844; Q92993: KAT5; NbExp=3; IntAct=EBI-6426999, EBI-399080;
CC       O94844; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-6426999, EBI-11742507;
CC       O94844; P17252: PRKCA; NbExp=3; IntAct=EBI-6426999, EBI-1383528;
CC       O94844; O60260-5: PRKN; NbExp=3; IntAct=EBI-6426999, EBI-21251460;
CC       O94844; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-6426999, EBI-9090795;
CC       O94844; P61981: YWHAG; NbExp=3; IntAct=EBI-6426999, EBI-359832;
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with highest levels in skeletal muscle,
CC       placenta, testis, stomach, and kidney, followed by uterus and adrenal
CC       gland. Expressed in a variety of fetal tissues.
CC       {ECO:0000269|PubMed:12426103}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42981/RHOBTB1";
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DR   EMBL; AB018283; BAA34460.2; -; mRNA.
DR   EMBL; AK075129; BAC11421.1; -; mRNA.
DR   EMBL; BC032848; AAH32848.1; -; mRNA.
DR   EMBL; BC041791; AAH41791.1; -; mRNA.
DR   CCDS; CCDS7261.1; -.
DR   RefSeq; NP_001229288.1; NM_001242359.1.
DR   RefSeq; NP_055651.1; NM_014836.4.
DR   RefSeq; XP_006718147.1; XM_006718084.1.
DR   RefSeq; XP_006718148.1; XM_006718085.1.
DR   RefSeq; XP_011538726.1; XM_011540424.1.
DR   RefSeq; XP_016872489.1; XM_017017000.1.
DR   RefSeq; XP_016872490.1; XM_017017001.1.
DR   AlphaFoldDB; O94844; -.
DR   SMR; O94844; -.
DR   BioGRID; 115217; 155.
DR   IntAct; O94844; 24.
DR   STRING; 9606.ENSP00000338671; -.
DR   iPTMnet; O94844; -.
DR   PhosphoSitePlus; O94844; -.
DR   BioMuta; RHOBTB1; -.
DR   EPD; O94844; -.
DR   MassIVE; O94844; -.
DR   PaxDb; 9606-ENSP00000338671; -.
DR   PeptideAtlas; O94844; -.
DR   ProteomicsDB; 50478; -.
DR   Pumba; O94844; -.
DR   Antibodypedia; 14385; 202 antibodies from 28 providers.
DR   DNASU; 9886; -.
DR   Ensembl; ENST00000337910.10; ENSP00000338671.5; ENSG00000072422.17.
DR   Ensembl; ENST00000357917.4; ENSP00000350595.4; ENSG00000072422.17.
DR   GeneID; 9886; -.
DR   KEGG; hsa:9886; -.
DR   MANE-Select; ENST00000337910.10; ENSP00000338671.5; NM_014836.5; NP_055651.1.
DR   UCSC; uc001jlh.4; human.
DR   AGR; HGNC:18738; -.
DR   CTD; 9886; -.
DR   DisGeNET; 9886; -.
DR   GeneCards; RHOBTB1; -.
DR   HGNC; HGNC:18738; RHOBTB1.
DR   HPA; ENSG00000072422; Tissue enhanced (skeletal).
DR   MIM; 607351; gene.
DR   neXtProt; NX_O94844; -.
DR   OpenTargets; ENSG00000072422; -.
DR   PharmGKB; PA38664; -.
DR   VEuPathDB; HostDB:ENSG00000072422; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   GeneTree; ENSGT00940000159995; -.
DR   HOGENOM; CLU_015517_0_0_1; -.
DR   InParanoid; O94844; -.
DR   OMA; SRDFQGQ; -.
DR   OrthoDB; 2898387at2759; -.
DR   PhylomeDB; O94844; -.
DR   TreeFam; TF323347; -.
DR   PathwayCommons; O94844; -.
DR   Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR   SignaLink; O94844; -.
DR   SIGNOR; O94844; -.
DR   BioGRID-ORCS; 9886; 14 hits in 1193 CRISPR screens.
DR   ChiTaRS; RHOBTB1; human.
DR   GeneWiki; RHOBTB1; -.
DR   GenomeRNAi; 9886; -.
DR   Pharos; O94844; Tbio.
DR   PRO; PR:O94844; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; O94844; Protein.
DR   Bgee; ENSG00000072422; Expressed in vastus lateralis and 200 other cell types or tissues.
DR   ExpressionAtlas; O94844; baseline and differential.
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:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   CDD; cd18530; BACK_RHOBTB1; 1.
DR   CDD; cd18355; BTB1_POZ_RHOBTB1; 1.
DR   CDD; cd18358; BTB2_POZ_RHOBTB1; 1.
DR   CDD; cd01873; RhoBTB; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; RHO FAMILY GTPASE; 1.
DR   PANTHER; PTHR24072:SF120; RHO-RELATED BTB DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00651; BTB; 2.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00225; BTB; 2.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54695; POZ domain; 2.
DR   PROSITE; PS50097; BTB; 2.
DR   PROSITE; PS51420; RHO; 1.
DR   Genevisible; O94844; HS.
PE   1: Evidence at protein level;
KW   GTP-binding; Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..696
FT                   /note="Rho-related BTB domain-containing protein 1"
FT                   /id="PRO_0000198960"
FT   DOMAIN          266..427
FT                   /note="BTB 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          485..552
FT                   /note="BTB 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REGION          1..210
FT                   /note="Rho-like"
FT   REGION          327..348
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"
SQ   SEQUENCE   696 AA;  79417 MW;  41ECB4425CD32A1A CRC64;
     MDADMDYERP NVETIKCVVV GDNAVGKTRL ICARACNTTL TQYQLLATHV PTVWAIDQYR
     VCQEVLERSR DVVDEVSVSL RLWDTFGDHH KDRRFAYGRS DVVVLCFSIA NPNSLNHVKS
     MWYPEIKHFC PRTPVILVGC QLDLRYADLE AVNRARRPLA RPIKRGDILP PEKGREVAKE
     LGLPYYETSV FDQFGIKDVF DNAIRAALIS RRHLQFWKSH LKKVQKPLLQ APFLPPKAPP
     PVIKIPECPS MGTNEAACLL DNPLCADVLF ILQDQEHIFA HRIYLATSSS KFYDLFLMEC
     EESPNGSEGA CEKEKQSRDF QGRILSVDPE EEREEGPPRI PQADQWKSSN KSLVEALGLE
     AEGAVPETQT LTGWSKGFIG MHREMQVNPI SKRMGPMTVV RMDASVQPGP FRTLLQFLYT
     GQLDEKEKDL VGLAQIAEVL EMFDLRMMVE NIMNKEAFMN QEITKAFHVR KANRIKECLS
     KGTFSDVTFK LDDGAISAHK PLLICSCEWM AAMFGGSFVE SANSEVYLPN INKISMQAVL
     DYLYTKQLSP NLDLDPLELI ALANRFCLPH LVALAEQHAV QELTKAATSG VGIDGEVLSY
     LELAQFHNAH QLAAWCLHHI CTNYNSVCSK FRKEIKSKSA DNQEYFERHR WPPVWYLKEE
     DHYQRVKRER EKEDIALNKH RSRRKWCFWN SSPAVA
//