Full text data of RHOB
RHOB
(ARH6, ARHB)
[Confidence: low (only semi-automatic identification from reviews)]
Rho-related GTP-binding protein RhoB (Rho cDNA clone 6; h6; Flags: Precursor)
Rho-related GTP-binding protein RhoB (Rho cDNA clone 6; h6; Flags: Precursor)
UniProt
P62745
ID RHOB_HUMAN Reviewed; 196 AA.
AC P62745; B2R692; P01121; Q5U0H6; Q7RTN5; Q7RTR9; Q9CUV7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1988, sequence version 1.
DT 22-JAN-2014, entry version 120.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT sequenced by 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS
RP 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
RT GTPase 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;
RA Robertson D., Paterson H.F., Adamson P., Hall A., Monaghan P.;
RT "Ultrastructural localization of ras-related proteins using epitope-
RT tagged 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
RP AND LYS-194.
RX PubMed=1400319;
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
RT Rho-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.,
RA 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.,
RA Buerckstuemmer T., 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
RT regulate RhoB-mediated cell death after DNA damage.";
RL PLoS ONE 6:E17108-E17108(2011).
CC -!- FUNCTION: Mediates apoptosis in neoplastically transformed cells
CC after DNA damage. Not essential for development but affects cell
CC adhesion and growth factor signaling in transformed cells. Plays a
CC negative role in tumorigenesis as deletion causes tumor formation.
CC Involved in intracellular protein trafficking of a number of
CC proteins. Targets PKN1 to endosomes and is involved in trafficking
CC of the EGF receptor from late endosomes to lysosomes. Also
CC required for stability and nuclear trafficking of AKT1/AKT which
CC promotes endothelial cell survival during vascular development.
CC Serves as a microtubule-dependent signal that is required for the
CC myosin contractile ring formation during cell cycle cytokinesis.
CC Required for genotoxic stress-induced cell death in breast cancer
CC cells.
CC -!- SUBUNIT: Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts
CC with ARGGEF3, RTKN and AKAP13.
CC -!- INTERACTION:
CC 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
CC endosomal membrane (geranylgeranylated form). Plasma membrane
CC (farnesylated form). Also detected at the nuclear margin and in
CC the nucleus. Translocates to the equatorial region before furrow
CC formation in a ECT2-dependent manner.
CC -!- INDUCTION: Up-regulated by DNA damaging agents like H(2)O(2) or
CC ionizing radiation (IR).
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 -!- 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
CC and cause mislocalization, leading to apoptosis and antineoplastic
CC effects.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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 PIR; A01372; TVHURH.
DR RefSeq; NP_004031.1; NM_004040.2.
DR UniGene; Hs.502876; -.
DR PDB; 2FV8; X-ray; 1.90 A; A=4-187.
DR PDBsum; 2FV8; -.
DR ProteinModelPortal; P62745; -.
DR SMR; P62745; 2-185.
DR IntAct; P62745; 22.
DR MINT; MINT-4824810; -.
DR STRING; 9606.ENSP00000272233; -.
DR ChEMBL; CHEMBL1795102; -.
DR PhosphoSite; P62745; -.
DR DMDM; 51338601; -.
DR PaxDb; P62745; -.
DR PeptideAtlas; P62745; -.
DR PRIDE; P62745; -.
DR DNASU; 388; -.
DR Ensembl; ENST00000272233; ENSP00000272233; ENSG00000143878.
DR GeneID; 388; -.
DR KEGG; hsa:388; -.
DR UCSC; uc002rdv.3; human.
DR CTD; 388; -.
DR GeneCards; GC02P020568; -.
DR HGNC; HGNC:668; RHOB.
DR HPA; CAB004560; -.
DR MIM; 165370; gene.
DR neXtProt; NX_P62745; -.
DR PharmGKB; PA24950; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233974; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P62745; -.
DR KO; K07856; -.
DR OMA; VWEVFET; -.
DR OrthoDB; EOG73FQPD; -.
DR PhylomeDB; P62745; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; P62745; -.
DR ChiTaRS; RHOB; human.
DR EvolutionaryTrace; P62745; -.
DR GeneWiki; RHOB; -.
DR GenomeRNAi; 388; -.
DR NextBio; 1615; -.
DR PRO; PR:P62745; -.
DR ArrayExpress; P62745; -.
DR Bgee; P62745; -.
DR CleanEx; HS_RHOB; -.
DR Genevestigator; P62745; -.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IDA: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; TAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; TAS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
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:0000910; P:cytokinesis; IMP:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:UniProtKB.
DR GO; GO:0006927; P:transformed cell apoptotic process; ISS:UniProtKB.
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 Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
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;
KW Cell adhesion; Cell membrane; Complete proteome;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Endosome; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport; Tumor suppressor.
FT CHAIN 1 193 Rho-related GTP-binding protein RhoB.
FT /FTId=PRO_0000030417.
FT PROPEP 194 196 Removed in mature form.
FT /FTId=PRO_0000030418.
FT NP_BIND 12 19 GTP (By similarity).
FT NP_BIND 59 63 GTP (By similarity).
FT NP_BIND 117 120 GTP (By similarity).
FT MOTIF 34 42 Effector region (Potential).
FT MOD_RES 41 41 ADP-ribosylasparagine; by botulinum toxin
FT (By similarity).
FT MOD_RES 154 154 Phosphotyrosine (By similarity).
FT MOD_RES 193 193 Cysteine methyl ester.
FT LIPID 189 189 S-palmitoyl cysteine.
FT LIPID 192 192 S-palmitoyl cysteine.
FT LIPID 193 193 S-farnesyl cysteine; in plasma membrane
FT form.
FT LIPID 193 193 S-geranylgeranyl cysteine; in endosomal
FT form.
FT MUTAGEN 14 14 G->V: No effect on internalization of EGF
FT receptor but decreases trafficking of
FT receptor to the lysosome with associated
FT accumulation in late endosomes.
FT MUTAGEN 39 39 F->G: Abolishes binding to PKN1 and
FT trafficking of EGF receptor.
FT MUTAGEN 189 189 C->S: No effect on prenylation. Reduced
FT palmitoylation. Abolishes palmitoylation;
FT when associated with S-192.
FT MUTAGEN 192 192 C->S: Reduced geranylgeranylation but no
FT effect on farnesylation. Reduced
FT palmitoylation. Abolishes palmitoylation;
FT when associated with S-189.
FT MUTAGEN 193 193 C->S: Abolishes methylation,
FT palmitoylation and prenylation.
FT MUTAGEN 194 194 K->L: No effect on palmitoylation or
FT prenylation.
FT STRAND 4 12
FT HELIX 18 27
FT STRAND 41 48
FT STRAND 51 59
FT TURN 67 69
FT HELIX 70 73
FT STRAND 79 85
FT HELIX 89 97
FT HELIX 99 106
FT STRAND 112 117
FT HELIX 119 123
FT HELIX 125 133
FT HELIX 141 150
FT STRAND 154 158
FT TURN 161 163
FT HELIX 167 179
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
//
ID RHOB_HUMAN Reviewed; 196 AA.
AC P62745; B2R692; P01121; Q5U0H6; Q7RTN5; Q7RTR9; Q9CUV7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1988, sequence version 1.
DT 22-JAN-2014, entry version 120.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT sequenced by 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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS
RP 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
RT GTPase 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;
RA Robertson D., Paterson H.F., Adamson P., Hall A., Monaghan P.;
RT "Ultrastructural localization of ras-related proteins using epitope-
RT tagged 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
RP AND LYS-194.
RX PubMed=1400319;
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
RT Rho-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.,
RA 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.,
RA Buerckstuemmer T., 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
RT regulate RhoB-mediated cell death after DNA damage.";
RL PLoS ONE 6:E17108-E17108(2011).
CC -!- FUNCTION: Mediates apoptosis in neoplastically transformed cells
CC after DNA damage. Not essential for development but affects cell
CC adhesion and growth factor signaling in transformed cells. Plays a
CC negative role in tumorigenesis as deletion causes tumor formation.
CC Involved in intracellular protein trafficking of a number of
CC proteins. Targets PKN1 to endosomes and is involved in trafficking
CC of the EGF receptor from late endosomes to lysosomes. Also
CC required for stability and nuclear trafficking of AKT1/AKT which
CC promotes endothelial cell survival during vascular development.
CC Serves as a microtubule-dependent signal that is required for the
CC myosin contractile ring formation during cell cycle cytokinesis.
CC Required for genotoxic stress-induced cell death in breast cancer
CC cells.
CC -!- SUBUNIT: Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts
CC with ARGGEF3, RTKN and AKAP13.
CC -!- INTERACTION:
CC 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
CC endosomal membrane (geranylgeranylated form). Plasma membrane
CC (farnesylated form). Also detected at the nuclear margin and in
CC the nucleus. Translocates to the equatorial region before furrow
CC formation in a ECT2-dependent manner.
CC -!- INDUCTION: Up-regulated by DNA damaging agents like H(2)O(2) or
CC ionizing radiation (IR).
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 -!- 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
CC and cause mislocalization, leading to apoptosis and antineoplastic
CC effects.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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 PIR; A01372; TVHURH.
DR RefSeq; NP_004031.1; NM_004040.2.
DR UniGene; Hs.502876; -.
DR PDB; 2FV8; X-ray; 1.90 A; A=4-187.
DR PDBsum; 2FV8; -.
DR ProteinModelPortal; P62745; -.
DR SMR; P62745; 2-185.
DR IntAct; P62745; 22.
DR MINT; MINT-4824810; -.
DR STRING; 9606.ENSP00000272233; -.
DR ChEMBL; CHEMBL1795102; -.
DR PhosphoSite; P62745; -.
DR DMDM; 51338601; -.
DR PaxDb; P62745; -.
DR PeptideAtlas; P62745; -.
DR PRIDE; P62745; -.
DR DNASU; 388; -.
DR Ensembl; ENST00000272233; ENSP00000272233; ENSG00000143878.
DR GeneID; 388; -.
DR KEGG; hsa:388; -.
DR UCSC; uc002rdv.3; human.
DR CTD; 388; -.
DR GeneCards; GC02P020568; -.
DR HGNC; HGNC:668; RHOB.
DR HPA; CAB004560; -.
DR MIM; 165370; gene.
DR neXtProt; NX_P62745; -.
DR PharmGKB; PA24950; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233974; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P62745; -.
DR KO; K07856; -.
DR OMA; VWEVFET; -.
DR OrthoDB; EOG73FQPD; -.
DR PhylomeDB; P62745; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; P62745; -.
DR ChiTaRS; RHOB; human.
DR EvolutionaryTrace; P62745; -.
DR GeneWiki; RHOB; -.
DR GenomeRNAi; 388; -.
DR NextBio; 1615; -.
DR PRO; PR:P62745; -.
DR ArrayExpress; P62745; -.
DR Bgee; P62745; -.
DR CleanEx; HS_RHOB; -.
DR Genevestigator; P62745; -.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IDA: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; TAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; TAS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
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:0000910; P:cytokinesis; IMP:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:UniProtKB.
DR GO; GO:0006927; P:transformed cell apoptotic process; ISS:UniProtKB.
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 Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
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;
KW Cell adhesion; Cell membrane; Complete proteome;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Endosome; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport; Tumor suppressor.
FT CHAIN 1 193 Rho-related GTP-binding protein RhoB.
FT /FTId=PRO_0000030417.
FT PROPEP 194 196 Removed in mature form.
FT /FTId=PRO_0000030418.
FT NP_BIND 12 19 GTP (By similarity).
FT NP_BIND 59 63 GTP (By similarity).
FT NP_BIND 117 120 GTP (By similarity).
FT MOTIF 34 42 Effector region (Potential).
FT MOD_RES 41 41 ADP-ribosylasparagine; by botulinum toxin
FT (By similarity).
FT MOD_RES 154 154 Phosphotyrosine (By similarity).
FT MOD_RES 193 193 Cysteine methyl ester.
FT LIPID 189 189 S-palmitoyl cysteine.
FT LIPID 192 192 S-palmitoyl cysteine.
FT LIPID 193 193 S-farnesyl cysteine; in plasma membrane
FT form.
FT LIPID 193 193 S-geranylgeranyl cysteine; in endosomal
FT form.
FT MUTAGEN 14 14 G->V: No effect on internalization of EGF
FT receptor but decreases trafficking of
FT receptor to the lysosome with associated
FT accumulation in late endosomes.
FT MUTAGEN 39 39 F->G: Abolishes binding to PKN1 and
FT trafficking of EGF receptor.
FT MUTAGEN 189 189 C->S: No effect on prenylation. Reduced
FT palmitoylation. Abolishes palmitoylation;
FT when associated with S-192.
FT MUTAGEN 192 192 C->S: Reduced geranylgeranylation but no
FT effect on farnesylation. Reduced
FT palmitoylation. Abolishes palmitoylation;
FT when associated with S-189.
FT MUTAGEN 193 193 C->S: Abolishes methylation,
FT palmitoylation and prenylation.
FT MUTAGEN 194 194 K->L: No effect on palmitoylation or
FT prenylation.
FT STRAND 4 12
FT HELIX 18 27
FT STRAND 41 48
FT STRAND 51 59
FT TURN 67 69
FT HELIX 70 73
FT STRAND 79 85
FT HELIX 89 97
FT HELIX 99 106
FT STRAND 112 117
FT HELIX 119 123
FT HELIX 125 133
FT HELIX 141 150
FT STRAND 154 158
FT TURN 161 163
FT HELIX 167 179
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
//
MIM
165370
*RECORD*
*FIELD* NO
165370
*FIELD* TI
*165370 RAS HOMOLOG GENE FAMILY, MEMBER B; RHOB
;;APLYSIA RAS-RELATED HOMOLOG 6; ARH6;;
read moreARHB;;
ONCOGENE RHO H6; RHOH6
*FIELD* TX
CLONING
A family of RAS proteins, originally designated RHO proteins, were
identified and isolated from protein products expressed in the marine
snail, Aplysia (Madaule and Axel, 1985). In humans, the products of
these genes, called ARH (Aplysia ras-related homologs), display striking
homology to the products of the classic RAS genes. Madaule and Axel
(1985) identified 3 classes of ARH genes, designated H6, H9 (RHOC;
165380), and H12 (RHOA; 165390). Chardin et al. (1988) reported the
complete H6 coding sequence and renamed the gene RhoB. The predicted
protein is 196 amino acids long.
GENE FUNCTION
Ridley and Hall (1992) showed that Rho stimulates actin stress fiber
production and the formation of focal adhesions when it is microinjected
into serum-starved Swiss 3T3 cells. Addition of serum or growth factors
such as PDGF also induced actin reorganization and stress fibers, but
when Rho was inhibited focal adhesion and stress fiber assembly were
impaired.
The actin cytoskeleton undergoes extensive remodeling during cell
morphogenesis and motility. The small guanosine triphosphatase Rho
regulates such remodeling. In their Figure 3C, Maekawa et al. (1999)
diagrammed proposed signaling pathways for Rho-induced remodeling of the
actin cytoskeleton. They demonstrated that LIM kinase (see 601329) is
phosphorylated and activated by ROCK (601702), a downstream effector of
Rho, and that LIM kinase, in turn, phosphorylates cofilin (601442).
Sandilands et al. (2004) found that RhoB colocalized with active Src
(190090) in the cytoplasm of mouse embryonic fibroblasts, and they
presented evidence that RhoB is a component of 'outside-in' signaling
pathways that coordinate Src activation with translocation to
transmembrane receptors.
MAPPING
By a combination of Southern analysis of somatic cell hybrid panels and
in situ hybridization, Cannizzaro et al. (1990) mapped the genes RHOB to
2pter-p12, ARH12 (RHOA) to 3p21, and ARH9 (RHOC) to 5q31-qter.
*FIELD* RF
1. Cannizzaro, L. A.; Madaule, P.; Hecht, F.; Axel, R.; Croce, C.
M.; Huebner, K.: Chromosome localization of human ARH genes, a ras-related
gene family. Genomics 6: 197-203, 1990.
2. Chardin, P.; Madaule, P.; Tavitian, A.: Coding sequence of human
rho cDNAs clone 6 and clone 9. Nucleic Acid Res. 16: 2717 only,
1988.
3. Madaule, P.; Axel, R.: A novel ras-related gene family. Cell 41:
31-40, 1985.
4. Maekawa, M.; Ishizaki, T.; Boku, S.; Watanabe, N.; Fujita, A.;
Iwamatsu, A.; Obinata, T.; Ohashi, K.; Mizuno, K.; Narumiya, S.:
Signaling from Rho to the actin cytoskeleton through protein kinases
ROCK and LIM-kinase. Science 285: 895-898, 1999.
5. Ridley, A. J.; Hall, A.: The small GTP-binding protein rho regulates
the assembly of focal adhesions and actin stress fibers in response
to growth factors. Cell 70: 389-399, 1992.
6. Sandilands, E.; Cans, C.; Fincham, V. J.; Brunton, V. G.; Mellor,
H.; Prendergast, G. C.; Norman, J. C.; Superti-Furga, G.; Frame, M.
C.: RhoB and actin polymerization coordinate Src activation with
endosome-mediated delivery to the membrane. Dev. Cell 7: 855-869,
2004.
*FIELD* CN
Patricia A. Hartz - updated: 1/6/2005
Ada Hamosh - updated: 8/5/1999
Rebekah S. Rasooly - updated: 9/30/1998
Alan F. Scott - updated: 3/27/1996
*FIELD* CD
Victor A. McKusick: 10/27/1989
*FIELD* ED
alopez: 04/04/2007
mgross: 1/7/2005
terry: 1/6/2005
alopez: 8/5/1999
alopez: 9/30/1998
alopez: 9/9/1998
terry: 8/28/1998
alopez: 8/3/1998
terry: 4/17/1996
mark: 3/27/1996
supermim: 3/16/1992
carol: 9/8/1990
carol: 6/18/1990
carol: 6/13/1990
supermim: 3/20/1990
supermim: 2/8/1990
*RECORD*
*FIELD* NO
165370
*FIELD* TI
*165370 RAS HOMOLOG GENE FAMILY, MEMBER B; RHOB
;;APLYSIA RAS-RELATED HOMOLOG 6; ARH6;;
read moreARHB;;
ONCOGENE RHO H6; RHOH6
*FIELD* TX
CLONING
A family of RAS proteins, originally designated RHO proteins, were
identified and isolated from protein products expressed in the marine
snail, Aplysia (Madaule and Axel, 1985). In humans, the products of
these genes, called ARH (Aplysia ras-related homologs), display striking
homology to the products of the classic RAS genes. Madaule and Axel
(1985) identified 3 classes of ARH genes, designated H6, H9 (RHOC;
165380), and H12 (RHOA; 165390). Chardin et al. (1988) reported the
complete H6 coding sequence and renamed the gene RhoB. The predicted
protein is 196 amino acids long.
GENE FUNCTION
Ridley and Hall (1992) showed that Rho stimulates actin stress fiber
production and the formation of focal adhesions when it is microinjected
into serum-starved Swiss 3T3 cells. Addition of serum or growth factors
such as PDGF also induced actin reorganization and stress fibers, but
when Rho was inhibited focal adhesion and stress fiber assembly were
impaired.
The actin cytoskeleton undergoes extensive remodeling during cell
morphogenesis and motility. The small guanosine triphosphatase Rho
regulates such remodeling. In their Figure 3C, Maekawa et al. (1999)
diagrammed proposed signaling pathways for Rho-induced remodeling of the
actin cytoskeleton. They demonstrated that LIM kinase (see 601329) is
phosphorylated and activated by ROCK (601702), a downstream effector of
Rho, and that LIM kinase, in turn, phosphorylates cofilin (601442).
Sandilands et al. (2004) found that RhoB colocalized with active Src
(190090) in the cytoplasm of mouse embryonic fibroblasts, and they
presented evidence that RhoB is a component of 'outside-in' signaling
pathways that coordinate Src activation with translocation to
transmembrane receptors.
MAPPING
By a combination of Southern analysis of somatic cell hybrid panels and
in situ hybridization, Cannizzaro et al. (1990) mapped the genes RHOB to
2pter-p12, ARH12 (RHOA) to 3p21, and ARH9 (RHOC) to 5q31-qter.
*FIELD* RF
1. Cannizzaro, L. A.; Madaule, P.; Hecht, F.; Axel, R.; Croce, C.
M.; Huebner, K.: Chromosome localization of human ARH genes, a ras-related
gene family. Genomics 6: 197-203, 1990.
2. Chardin, P.; Madaule, P.; Tavitian, A.: Coding sequence of human
rho cDNAs clone 6 and clone 9. Nucleic Acid Res. 16: 2717 only,
1988.
3. Madaule, P.; Axel, R.: A novel ras-related gene family. Cell 41:
31-40, 1985.
4. Maekawa, M.; Ishizaki, T.; Boku, S.; Watanabe, N.; Fujita, A.;
Iwamatsu, A.; Obinata, T.; Ohashi, K.; Mizuno, K.; Narumiya, S.:
Signaling from Rho to the actin cytoskeleton through protein kinases
ROCK and LIM-kinase. Science 285: 895-898, 1999.
5. Ridley, A. J.; Hall, A.: The small GTP-binding protein rho regulates
the assembly of focal adhesions and actin stress fibers in response
to growth factors. Cell 70: 389-399, 1992.
6. Sandilands, E.; Cans, C.; Fincham, V. J.; Brunton, V. G.; Mellor,
H.; Prendergast, G. C.; Norman, J. C.; Superti-Furga, G.; Frame, M.
C.: RhoB and actin polymerization coordinate Src activation with
endosome-mediated delivery to the membrane. Dev. Cell 7: 855-869,
2004.
*FIELD* CN
Patricia A. Hartz - updated: 1/6/2005
Ada Hamosh - updated: 8/5/1999
Rebekah S. Rasooly - updated: 9/30/1998
Alan F. Scott - updated: 3/27/1996
*FIELD* CD
Victor A. McKusick: 10/27/1989
*FIELD* ED
alopez: 04/04/2007
mgross: 1/7/2005
terry: 1/6/2005
alopez: 8/5/1999
alopez: 9/30/1998
alopez: 9/9/1998
terry: 8/28/1998
alopez: 8/3/1998
terry: 4/17/1996
mark: 3/27/1996
supermim: 3/16/1992
carol: 9/8/1990
carol: 6/18/1990
carol: 6/13/1990
supermim: 3/20/1990
supermim: 2/8/1990