RHOB_HUMAN
ID RHOB_HUMAN Reviewed; 196 AA.
AC P62745; B2R692; P01121; Q5U0H6; Q7RTN5; Q7RTR9; Q9CUV7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Rho-related GTP-binding protein RhoB;
DE AltName: Full=Rho cDNA clone 6;
DE Short=h6;
DE Flags: Precursor;
GN Name=RHOB; Synonyms=ARH6, ARHB;
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].
RX PubMed=3283705; DOI=10.1093/nar/16.6.2717;
RA Chardin P., Madaule P., Tavitian A.;
RT "Coding sequence of human rho cDNAs clone 6 and clone 9.";
RL Nucleic Acids Res. 16:2717-2717(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
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].
RC TISSUE=Hippocampus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 8-27; 52-68; 105-118 AND 151-162, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-196.
RX PubMed=3888408; DOI=10.1016/0092-8674(85)90058-3;
RA Madaule P., Axel R.;
RT "A novel ras-related gene family.";
RL Cell 41:31-40(1985).
RN [11]
RP FUNCTION, AND INTERACTION WITH PKN1.
RX PubMed=9478917; DOI=10.1074/jbc.273.9.4811;
RA Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J.;
RT "PRK1 is targeted to endosomes by the small GTPase, RhoB.";
RL J. Biol. Chem. 273:4811-4814(1998).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF PHE-39.
RX PubMed=10508588; DOI=10.1016/s0960-9822(99)80422-9;
RA Gampel A., Parker P.J., Mellor H.;
RT "Regulation of epidermal growth factor receptor traffic by the small GTPase
RT rhoB.";
RL Curr. Biol. 9:955-958(1999).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-14.
RX PubMed=15226397; DOI=10.1242/jcs.01193;
RA Wherlock M., Gampel A., Futter C., Mellor H.;
RT "Farnesyltransferase inhibitors disrupt EGF receptor traffic through
RT modulation of the RhoB GTPase.";
RL J. Cell Sci. 117:3221-3231(2004).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=7537292; DOI=10.1177/43.5.7537292;
RA Robertson D., Paterson H.F., Adamson P., Hall A., Monaghan P.;
RT "Ultrastructural localization of ras-related proteins using epitope-tagged
RT plasmids.";
RL J. Histochem. Cytochem. 43:471-480(1995).
RN [15]
RP PALMITOYLATION AT CYS-189 AND CYS-192, ISOPRENYLATION AT CYS-193,
RP METHYLATION AT CYS-193, AND MUTAGENESIS OF CYS-189; CYS-192; CYS-193 AND
RP LYS-194.
RX PubMed=1400319; DOI=10.1016/s0021-9258(19)88661-1;
RA Adamson P., Marshall C.J., Hall A., Tilbrook P.A.;
RT "Post-translational modifications of p21rho proteins.";
RL J. Biol. Chem. 267:20033-20038(1992).
RN [16]
RP ISOPRENYLATION AT CYS-193, AND MUTAGENESIS OF CYS-192 AND CYS-193.
RX PubMed=7713879; DOI=10.1074/jbc.270.14.7864;
RA Armstrong S.A., Hannah V.C., Goldstein J.L., Brown M.S.;
RT "CAAX geranylgeranyl transferase transfers farnesyl as efficiently as
RT geranylgeranyl to RhoB.";
RL J. Biol. Chem. 270:7864-7868(1995).
RN [17]
RP INTERACTION WITH AKAP13.
RX PubMed=11546812; DOI=10.1074/jbc.m106629200;
RA Diviani D., Soderling J., Scott J.D.;
RT "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-
RT mediated stress fiber formation.";
RL J. Biol. Chem. 276:44247-44257(2001).
RN [18]
RP INTERACTION WITH ARHGEF3.
RX PubMed=12221096; DOI=10.1074/jbc.m207401200;
RA Arthur W.T., Ellerbroek S.M., Der C.J., Burridge K., Wennerberg K.;
RT "XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not
RT RhoC.";
RL J. Biol. Chem. 277:42964-42972(2002).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16236794; DOI=10.1091/mbc.e05-06-0569;
RA Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.;
RT "Dissecting the role of Rho-mediated signaling in contractile ring
RT formation.";
RL Mol. Biol. Cell 17:43-55(2006).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP FUNCTION, AND INDUCTION.
RX PubMed=21373644; DOI=10.1371/journal.pone.0017108;
RA Srougi M.C., Burridge K.;
RT "The nuclear guanine nucleotide exchange factors Ect2 and Net1 regulate
RT RhoB-mediated cell death after DNA damage.";
RL PLoS ONE 6:E17108-E17108(2011).
RN [22]
RP GLYCOSYLATION AT TYR-34 (MICROBIAL INFECTION).
RX PubMed=24141704; DOI=10.1038/nsmb.2688;
RA Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
RA Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
RA Aktories K.;
RT "A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation
RT of Gq and Gi proteins.";
RL Nat. Struct. Mol. Biol. 20:1273-1280(2013).
RN [23]
RP GLYCOSYLATION AT THR-37 (MICROBIAL INFECTION).
RX PubMed=24905543; DOI=10.1111/cmi.12321;
RA Genth H., Pauillac S., Schelle I., Bouvet P., Bouchier C.,
RA Varela-Chavez C., Just I., Popoff M.R.;
RT "Haemorrhagic toxin and lethal toxin from Clostridium sordellii strain
RT vpi9048: molecular characterization and comparative analysis of substrate
RT specificity of the large clostridial glucosylating toxins.";
RL Cell. Microbiol. 16:1706-1721(2014).
RN [24]
RP INTERACTION WITH RIPOR1.
RX PubMed=27807006; DOI=10.1242/jcs.198614;
RA Mardakheh F.K., Self A., Marshall C.J.;
RT "RHO binding to FAM65A regulates Golgi reorientation during cell
RT migration.";
RL J. Cell Sci. 129:4466-4479(2016).
CC -!- FUNCTION: Mediates apoptosis in neoplastically transformed cells after
CC DNA damage. Not essential for development but affects cell adhesion and
CC growth factor signaling in transformed cells. Plays a negative role in
CC tumorigenesis as deletion causes tumor formation. Involved in
CC intracellular protein trafficking of a number of proteins. Targets PKN1
CC to endosomes and is involved in trafficking of the EGF receptor from
CC late endosomes to lysosomes. Also required for stability and nuclear
CC trafficking of AKT1/AKT which promotes endothelial cell survival during
CC vascular development. Serves as a microtubule-dependent signal that is
CC required for the myosin contractile ring formation during cell cycle
CC cytokinesis. Required for genotoxic stress-induced cell death in breast
CC cancer cells. {ECO:0000269|PubMed:10508588,
CC ECO:0000269|PubMed:15226397, ECO:0000269|PubMed:16236794,
CC ECO:0000269|PubMed:21373644, ECO:0000269|PubMed:9478917}.
CC -!- SUBUNIT: Binds ROCK1 and ROCK2 (By similarity). Also binds PKN1/PRK1
CC (PubMed:9478917). Interacts with ARGGEF3 (PubMed:12221096). Interacts
CC with RTKN (By similarity). Interacts with AKAP13 (PubMed:11546812).
CC Interacts with RIPOR1 (PubMed:27807006). {ECO:0000250|UniProtKB:P62746,
CC ECO:0000250|UniProtKB:P62747, ECO:0000269|PubMed:11546812,
CC ECO:0000269|PubMed:12221096, ECO:0000269|PubMed:27807006,
CC ECO:0000269|PubMed:9478917}.
CC -!- INTERACTION:
CC P62745; Q9HCE7-2: SMURF1; NbExp=3; IntAct=EBI-602647, EBI-9845742;
CC P62745; Q13829: TNFAIP1; NbExp=5; IntAct=EBI-602647, EBI-2505861;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor. Cell
CC membrane; Lipid-anchor. Nucleus. Cleavage furrow. Note=Late endosomal
CC membrane (geranylgeranylated form). Plasma membrane (farnesylated
CC form). Also detected at the nuclear margin and in the nucleus.
CC Translocates to the equatorial region before furrow formation in a
CC ECT2-dependent manner.
CC -!- INDUCTION: Up-regulated by DNA damaging agents like H(2)O(2) or
CC ionizing radiation (IR). {ECO:0000269|PubMed:21373644}.
CC -!- PTM: Prenylation specifies the subcellular location of RHOB. The
CC farnesylated form is localized to the plasma membrane while the
CC geranylgeranylated form is localized to the endosome.
CC {ECO:0000269|PubMed:1400319, ECO:0000269|PubMed:7713879}.
CC -!- PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus
CC asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits
CC downstream signaling by an impaired interaction with diverse regulator
CC and effector proteins of Rho and leads to actin disassembly.
CC {ECO:0000269|PubMed:24141704}.
CC -!- PTM: (Microbial infection) Glucosylated at Thr-37 by C.difficile toxins
CC TcdA and TcdB in the colonic epithelium (PubMed:24905543).
CC Monoglucosylation completely prevents the recognition of the downstream
CC effector, blocking the GTPases in their inactive form, leading to actin
CC cytoskeleton disruption (PubMed:24905543).
CC {ECO:0000269|PubMed:24905543}.
CC -!- MISCELLANEOUS: RHOB is one of the targets of farnesyltransferase
CC inhibitors which are currently under investigation as cancer
CC therapeutics. These elevate the levels of geranylgeranylated RHOB and
CC cause mislocalization, leading to apoptosis and antineoplastic effects.
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="http://atlasgeneticsoncology.org/Genes/RHOBID42108ch2p24.html";
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DR EMBL; X06820; CAA29968.1; -; mRNA.
DR EMBL; AF498971; AAM21118.1; -; mRNA.
DR EMBL; CR542272; CAG47068.1; -; mRNA.
DR EMBL; AK124398; BAG54035.1; -; mRNA.
DR EMBL; AK312487; BAG35389.1; -; mRNA.
DR EMBL; BT019546; AAV38353.1; -; mRNA.
DR EMBL; BT019547; AAV38354.1; -; mRNA.
DR EMBL; AC023137; AAY24345.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00819.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00820.1; -; Genomic_DNA.
DR EMBL; BC066954; AAH66954.1; -; mRNA.
DR EMBL; M12174; AAA36565.1; -; mRNA.
DR EMBL; BK001232; DAA01138.1; -; mRNA.
DR EMBL; BK001671; DAA01912.1; -; Genomic_DNA.
DR CCDS; CCDS1699.1; -.
DR PIR; A01372; TVHURH.
DR RefSeq; NP_004031.1; NM_004040.3.
DR PDB; 2FV8; X-ray; 1.90 A; A=4-187.
DR PDB; 6HXU; X-ray; 1.19 A; A=1-183.
DR PDB; 6SGE; X-ray; 1.50 A; A/C=1-183.
DR PDBsum; 2FV8; -.
DR PDBsum; 6HXU; -.
DR PDBsum; 6SGE; -.
DR AlphaFoldDB; P62745; -.
DR SMR; P62745; -.
DR BioGRID; 106881; 831.
DR IntAct; P62745; 29.
DR MINT; P62745; -.
DR STRING; 9606.ENSP00000272233; -.
DR ChEMBL; CHEMBL1795102; -.
DR DrugBank; DB00083; Botulinum toxin type A.
DR GlyGen; P62745; 1 site.
DR iPTMnet; P62745; -.
DR PhosphoSitePlus; P62745; -.
DR SwissPalm; P62745; -.
DR BioMuta; RHOB; -.
DR DMDM; 51338601; -.
DR EPD; P62745; -.
DR jPOST; P62745; -.
DR MassIVE; P62745; -.
DR MaxQB; P62745; -.
DR PaxDb; P62745; -.
DR PeptideAtlas; P62745; -.
DR PRIDE; P62745; -.
DR ProteomicsDB; 57420; -.
DR TopDownProteomics; P62745; -.
DR ABCD; P62745; 1 sequenced antibody.
DR Antibodypedia; 3879; 225 antibodies from 34 providers.
DR DNASU; 388; -.
DR Ensembl; ENST00000272233.6; ENSP00000272233.4; ENSG00000143878.10.
DR GeneID; 388; -.
DR KEGG; hsa:388; -.
DR MANE-Select; ENST00000272233.6; ENSP00000272233.4; NM_004040.4; NP_004031.1.
DR UCSC; uc002rdv.4; human.
DR CTD; 388; -.
DR DisGeNET; 388; -.
DR GeneCards; RHOB; -.
DR HGNC; HGNC:668; RHOB.
DR HPA; ENSG00000143878; Low tissue specificity.
DR MIM; 165370; gene.
DR neXtProt; NX_P62745; -.
DR OpenTargets; ENSG00000143878; -.
DR PharmGKB; PA24950; -.
DR VEuPathDB; HostDB:ENSG00000143878; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00950000182945; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; P62745; -.
DR OMA; WEVFETA; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; P62745; -.
DR TreeFam; TF300837; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P62745; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR SignaLink; P62745; -.
DR SIGNOR; P62745; -.
DR BioGRID-ORCS; 388; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; RHOB; human.
DR EvolutionaryTrace; P62745; -.
DR GeneWiki; RHOB; -.
DR GenomeRNAi; 388; -.
DR Pharos; P62745; Tbio.
DR PRO; PR:P62745; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P62745; protein.
DR Bgee; ENSG00000143878; Expressed in mucosa of stomach and 209 other tissues.
DR Genevisible; P62745; HS.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IEA:Ensembl.
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:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
DR GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IGI:BHF-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Angiogenesis; Apoptosis; Cell adhesion;
KW Cell membrane; Developmental protein; Differentiation;
KW Direct protein sequencing; Endosome; Glycoprotein; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Nucleus; Palmitate;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport; Tumor suppressor.
FT CHAIN 1..193
FT /note="Rho-related GTP-binding protein RhoB"
FT /id="PRO_0000030417"
FT PROPEP 194..196
FT /note="Removed in mature form"
FT /id="PRO_0000030418"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 41
FT /note="ADP-ribosylasparagine; by botulinum toxin"
FT /evidence="ECO:0000250"
FT MOD_RES 154
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62746"
FT MOD_RES 193
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:1400319"
FT LIPID 189
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:1400319"
FT LIPID 192
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:1400319"
FT LIPID 193
FT /note="S-farnesyl cysteine; in plasma membrane form"
FT /evidence="ECO:0000269|PubMed:1400319,
FT ECO:0000269|PubMed:7713879"
FT LIPID 193
FT /note="S-geranylgeranyl cysteine; in endosomal form"
FT /evidence="ECO:0000269|PubMed:1400319,
FT ECO:0000269|PubMed:7713879"
FT CARBOHYD 34
FT /note="O-linked (GlcNAc) tyrosine; by Photorhabdus
FT PAU_02230"
FT /evidence="ECO:0000269|PubMed:24141704"
FT CARBOHYD 37
FT /note="(Microbial infection) O-linked (Glc) threonine; by
FT C.difficile toxins TcdA and TcdB"
FT /evidence="ECO:0000269|PubMed:24905543"
FT MUTAGEN 14
FT /note="G->V: No effect on internalization of EGF receptor
FT but decreases trafficking of receptor to the lysosome with
FT associated accumulation in late endosomes."
FT /evidence="ECO:0000269|PubMed:15226397"
FT MUTAGEN 39
FT /note="F->G: Abolishes binding to PKN1 and trafficking of
FT EGF receptor."
FT /evidence="ECO:0000269|PubMed:10508588"
FT MUTAGEN 189
FT /note="C->S: No effect on prenylation. Reduced
FT palmitoylation. Abolishes palmitoylation; when associated
FT with S-192."
FT /evidence="ECO:0000269|PubMed:1400319"
FT MUTAGEN 192
FT /note="C->S: Reduced geranylgeranylation but no effect on
FT farnesylation. Reduced palmitoylation. Abolishes
FT palmitoylation; when associated with S-189."
FT /evidence="ECO:0000269|PubMed:1400319,
FT ECO:0000269|PubMed:7713879"
FT MUTAGEN 193
FT /note="C->S: Abolishes methylation, palmitoylation and
FT prenylation."
FT /evidence="ECO:0000269|PubMed:1400319,
FT ECO:0000269|PubMed:7713879"
FT MUTAGEN 194
FT /note="K->L: No effect on palmitoylation or prenylation."
FT /evidence="ECO:0000269|PubMed:1400319"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:6HXU"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:6HXU"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:6HXU"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:6HXU"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:6HXU"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6HXU"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:6HXU"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6HXU"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:6HXU"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:6HXU"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6HXU"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:6HXU"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:6HXU"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:6HXU"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:6HXU"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6HXU"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:6HXU"
SQ SEQUENCE 196 AA; 22123 MW; CCE6FD53AE00CD83 CRC64;
MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG KQVELALWDT
AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV PEVKHFCPNV PIILVANKKD
LRSDEHVRTE LARMKQEPVR TDDGRAMAVR IQAYDYLECS AKTKEGVREV FETATRAALQ
KRYGSQNGCI NCCKVL
