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Rho-related GTP-binding protein RhoB (Rho cDNA clone 6) (h6)

 RHOB_HUMAN              Reviewed;         196 AA.
P62745; B2R692; P01121; Q5U0H6; Q7RTN5; Q7RTR9; Q9CUV7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
30-AUG-2017, entry version 157.
RecName: Full=Rho-related GTP-binding protein RhoB;
AltName: Full=Rho cDNA clone 6;
Short=h6;
Flags: Precursor;
Name=RHOB; Synonyms=ARH6, ARHB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3283705; DOI=10.1093/nar/16.6.2717;
Chardin P., Madaule P., Tavitian A.;
"Coding sequence of human rho cDNAs clone 6 and clone 9.";
Nucleic Acids Res. 16:2717-2717(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 8-27; 52-68; 105-118 AND 151-162, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 29-196.
PubMed=3888408; DOI=10.1016/0092-8674(85)90058-3;
Madaule P., Axel R.;
"A novel ras-related gene family.";
Cell 41:31-40(1985).
[11]
FUNCTION, AND INTERACTION WITH PKN1.
PubMed=9478917; DOI=10.1074/jbc.273.9.4811;
Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J.;
"PRK1 is targeted to endosomes by the small GTPase, RhoB.";
J. Biol. Chem. 273:4811-4814(1998).
[12]
FUNCTION, AND MUTAGENESIS OF PHE-39.
PubMed=10508588; DOI=10.1016/S0960-9822(99)80422-9;
Gampel A., Parker P.J., Mellor H.;
"Regulation of epidermal growth factor receptor traffic by the small
GTPase rhoB.";
Curr. Biol. 9:955-958(1999).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-14.
PubMed=15226397; DOI=10.1242/jcs.01193;
Wherlock M., Gampel A., Futter C., Mellor H.;
"Farnesyltransferase inhibitors disrupt EGF receptor traffic through
modulation of the RhoB GTPase.";
J. Cell Sci. 117:3221-3231(2004).
[14]
SUBCELLULAR LOCATION.
PubMed=7537292; DOI=10.1177/43.5.7537292;
Robertson D., Paterson H.F., Adamson P., Hall A., Monaghan P.;
"Ultrastructural localization of ras-related proteins using epitope-
tagged plasmids.";
J. Histochem. Cytochem. 43:471-480(1995).
[15]
PALMITOYLATION AT CYS-189 AND CYS-192, ISOPRENYLATION AT CYS-193,
METHYLATION AT CYS-193, AND MUTAGENESIS OF CYS-189; CYS-192; CYS-193
AND LYS-194.
PubMed=1400319;
Adamson P., Marshall C.J., Hall A., Tilbrook P.A.;
"Post-translational modifications of p21rho proteins.";
J. Biol. Chem. 267:20033-20038(1992).
[16]
ISOPRENYLATION AT CYS-193, AND MUTAGENESIS OF CYS-192 AND CYS-193.
PubMed=7713879; DOI=10.1074/jbc.270.14.7864;
Armstrong S.A., Hannah V.C., Goldstein J.L., Brown M.S.;
"CAAX geranylgeranyl transferase transfers farnesyl as efficiently as
geranylgeranyl to RhoB.";
J. Biol. Chem. 270:7864-7868(1995).
[17]
INTERACTION WITH AKAP13.
PubMed=11546812; DOI=10.1074/jbc.M106629200;
Diviani D., Soderling J., Scott J.D.;
"AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective
Rho-mediated stress fiber formation.";
J. Biol. Chem. 276:44247-44257(2001).
[18]
INTERACTION WITH ARHGEF3.
PubMed=12221096; DOI=10.1074/jbc.M207401200;
Arthur W.T., Ellerbroek S.M., Der C.J., Burridge K., Wennerberg K.;
"XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not
RhoC.";
J. Biol. Chem. 277:42964-42972(2002).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16236794; DOI=10.1091/mbc.E05-06-0569;
Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S.,
Miki T.;
"Dissecting the role of Rho-mediated signaling in contractile ring
formation.";
Mol. Biol. Cell 17:43-55(2006).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
FUNCTION, AND INDUCTION.
PubMed=21373644; DOI=10.1371/journal.pone.0017108;
Srougi M.C., Burridge K.;
"The nuclear guanine nucleotide exchange factors Ect2 and Net1
regulate RhoB-mediated cell death after DNA damage.";
PLoS ONE 6:E17108-E17108(2011).
[22]
GLYCOSYLATION AT TYR-34 (MICROBIAL INFECTION).
PubMed=24141704; DOI=10.1038/nsmb.2688;
Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
Aktories K.;
"A bacterial toxin catalyzing tyrosine glycosylation of Rho and
deamidation of Gq and Gi proteins.";
Nat. Struct. Mol. Biol. 20:1273-1280(2013).
[23]
INTERACTION WITH RIPOR1.
PubMed=27807006; DOI=10.1242/jcs.198614;
Mardakheh F.K., Self A., Marshall C.J.;
"RHO binding to FAM65A regulates Golgi reorientation during cell
migration.";
J. Cell Sci. 129:4466-4479(2016).
-!- FUNCTION: Mediates apoptosis in neoplastically transformed cells
after DNA damage. Not essential for development but affects cell
adhesion and growth factor signaling in transformed cells. Plays a
negative role in tumorigenesis as deletion causes tumor formation.
Involved in intracellular protein trafficking of a number of
proteins. Targets PKN1 to endosomes and is involved in trafficking
of the EGF receptor from late endosomes to lysosomes. Also
required for stability and nuclear trafficking of AKT1/AKT which
promotes endothelial cell survival during vascular development.
Serves as a microtubule-dependent signal that is required for the
myosin contractile ring formation during cell cycle cytokinesis.
Required for genotoxic stress-induced cell death in breast cancer
cells. {ECO:0000269|PubMed:10508588, ECO:0000269|PubMed:15226397,
ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:21373644,
ECO:0000269|PubMed:9478917}.
-!- SUBUNIT: Binds ROCK1 and ROCK2 (By similarity). Also binds
PKN1/PRK1 (PubMed:9478917). Interacts with ARGGEF3
(PubMed:12221096). Interacts with RTKN (By similarity). Interacts
with AKAP13 (PubMed:11546812). Interacts with RIPOR1
(PubMed:27807006). {ECO:0000250|UniProtKB:P62746,
ECO:0000250|UniProtKB:P62747, ECO:0000269|PubMed:11546812,
ECO:0000269|PubMed:12221096, ECO:0000269|PubMed:27807006,
ECO:0000269|PubMed:9478917}.
-!- INTERACTION:
Q9HCE7-2:SMURF1; NbExp=3; IntAct=EBI-602647, EBI-9845742;
Q13829:TNFAIP1; NbExp=5; IntAct=EBI-602647, EBI-2505861;
-!- SUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor. Cell
membrane; Lipid-anchor. Nucleus. Cleavage furrow. Note=Late
endosomal membrane (geranylgeranylated form). Plasma membrane
(farnesylated form). Also detected at the nuclear margin and in
the nucleus. Translocates to the equatorial region before furrow
formation in a ECT2-dependent manner.
-!- INDUCTION: Up-regulated by DNA damaging agents like H(2)O(2) or
ionizing radiation (IR). {ECO:0000269|PubMed:21373644}.
-!- PTM: Prenylation specifies the subcellular location of RHOB. The
farnesylated form is localized to the plasma membrane while the
geranylgeranylated form is localized to the endosome.
{ECO:0000269|PubMed:1400319, ECO:0000269|PubMed:7713879}.
-!- PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus
asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230
inhibits downstream signaling by an impaired interaction with
diverse regulator and effector proteins of Rho and leads to actin
disassembly. {ECO:0000269|PubMed:24141704}.
-!- MISCELLANEOUS: RHOB is one of the targets of farnesyltransferase
inhibitors which are currently under investigation as cancer
therapeutics. These elevate the levels of geranylgeranylated RHOB
and cause mislocalization, leading to apoptosis and antineoplastic
effects.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RHOBID42108ch2p24.html";
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EMBL; X06820; CAA29968.1; -; mRNA.
EMBL; AF498971; AAM21118.1; -; mRNA.
EMBL; CR542272; CAG47068.1; -; mRNA.
EMBL; AK124398; BAG54035.1; -; mRNA.
EMBL; AK312487; BAG35389.1; -; mRNA.
EMBL; BT019546; AAV38353.1; -; mRNA.
EMBL; BT019547; AAV38354.1; -; mRNA.
EMBL; AC023137; AAY24345.1; -; Genomic_DNA.
EMBL; CH471053; EAX00819.1; -; Genomic_DNA.
EMBL; CH471053; EAX00820.1; -; Genomic_DNA.
EMBL; BC066954; AAH66954.1; -; mRNA.
EMBL; M12174; AAA36565.1; -; mRNA.
EMBL; BK001232; DAA01138.1; -; mRNA.
EMBL; BK001671; DAA01912.1; -; Genomic_DNA.
CCDS; CCDS1699.1; -.
PIR; A01372; TVHURH.
RefSeq; NP_004031.1; NM_004040.3.
UniGene; Hs.502876; -.
PDB; 2FV8; X-ray; 1.90 A; A=4-187.
PDBsum; 2FV8; -.
ProteinModelPortal; P62745; -.
SMR; P62745; -.
BioGrid; 106881; 20.
IntAct; P62745; 24.
MINT; MINT-4824810; -.
STRING; 9606.ENSP00000272233; -.
ChEMBL; CHEMBL1795102; -.
DrugBank; DB00083; Botulinum Toxin Type A.
iPTMnet; P62745; -.
PhosphoSitePlus; P62745; -.
SwissPalm; P62745; -.
BioMuta; RHOB; -.
DMDM; 51338601; -.
EPD; P62745; -.
MaxQB; P62745; -.
PaxDb; P62745; -.
PeptideAtlas; P62745; -.
PRIDE; P62745; -.
TopDownProteomics; P62745; -.
DNASU; 388; -.
Ensembl; ENST00000272233; ENSP00000272233; ENSG00000143878.
GeneID; 388; -.
KEGG; hsa:388; -.
UCSC; uc002rdv.4; human.
CTD; 388; -.
DisGeNET; 388; -.
GeneCards; RHOB; -.
HGNC; HGNC:668; RHOB.
MIM; 165370; gene.
neXtProt; NX_P62745; -.
OpenTargets; ENSG00000143878; -.
PharmGKB; PA24950; -.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000119020; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; P62745; -.
KO; K07856; -.
OMA; WEVFETA; -.
OrthoDB; EOG091G0QVS; -.
PhylomeDB; P62745; -.
TreeFam; TF300837; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5625900; RHO GTPases activate CIT.
Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
SignaLink; P62745; -.
SIGNOR; P62745; -.
ChiTaRS; RHOB; human.
EvolutionaryTrace; P62745; -.
GeneWiki; RHOB; -.
GenomeRNAi; 388; -.
PRO; PR:P62745; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000143878; -.
CleanEx; HS_RHOB; -.
Genevisible; P62745; HS.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0019003; F:GDP binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; TAS:UniProtKB.
GO; GO:0003924; F:GTPase activity; TAS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB.
GO; GO:0000910; P:cytokinesis; IMP:UniProtKB.
GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL.
GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
GO; GO:0030334; P:regulation of cell migration; IGI:BHF-UCL.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007266; P:Rho protein signal transduction; TAS:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Angiogenesis; Apoptosis;
Cell adhesion; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
Endosome; Glycoprotein; GTP-binding; Lipoprotein; Membrane;
Methylation; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein;
Prenylation; Protein transport; Reference proteome; Transport;
Tumor suppressor.
CHAIN 1 193 Rho-related GTP-binding protein RhoB.
/FTId=PRO_0000030417.
PROPEP 194 196 Removed in mature form.
/FTId=PRO_0000030418.
NP_BIND 12 19 GTP. {ECO:0000250}.
NP_BIND 59 63 GTP. {ECO:0000250}.
NP_BIND 117 120 GTP. {ECO:0000250}.
MOTIF 34 42 Effector region. {ECO:0000255}.
MOD_RES 41 41 ADP-ribosylasparagine; by botulinum
toxin. {ECO:0000250}.
MOD_RES 154 154 Phosphotyrosine.
{ECO:0000250|UniProtKB:P62746}.
MOD_RES 193 193 Cysteine methyl ester.
{ECO:0000269|PubMed:1400319}.
LIPID 189 189 S-palmitoyl cysteine.
{ECO:0000269|PubMed:1400319}.
LIPID 192 192 S-palmitoyl cysteine.
{ECO:0000269|PubMed:1400319}.
LIPID 193 193 S-farnesyl cysteine; in plasma membrane
form. {ECO:0000269|PubMed:1400319,
ECO:0000269|PubMed:7713879}.
LIPID 193 193 S-geranylgeranyl cysteine; in endosomal
form. {ECO:0000269|PubMed:1400319,
ECO:0000269|PubMed:7713879}.
CARBOHYD 34 34 O-linked (GlcNAc) tyrosine; by
Photorhabdus PAU_02230.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 14 14 G->V: No effect on internalization of EGF
receptor but decreases trafficking of
receptor to the lysosome with associated
accumulation in late endosomes.
{ECO:0000269|PubMed:15226397}.
MUTAGEN 39 39 F->G: Abolishes binding to PKN1 and
trafficking of EGF receptor.
{ECO:0000269|PubMed:10508588}.
MUTAGEN 189 189 C->S: No effect on prenylation. Reduced
palmitoylation. Abolishes palmitoylation;
when associated with S-192.
{ECO:0000269|PubMed:1400319}.
MUTAGEN 192 192 C->S: Reduced geranylgeranylation but no
effect on farnesylation. Reduced
palmitoylation. Abolishes palmitoylation;
when associated with S-189.
{ECO:0000269|PubMed:1400319,
ECO:0000269|PubMed:7713879}.
MUTAGEN 193 193 C->S: Abolishes methylation,
palmitoylation and prenylation.
{ECO:0000269|PubMed:1400319,
ECO:0000269|PubMed:7713879}.
MUTAGEN 194 194 K->L: No effect on palmitoylation or
prenylation.
{ECO:0000269|PubMed:1400319}.
STRAND 4 12 {ECO:0000244|PDB:2FV8}.
HELIX 18 27 {ECO:0000244|PDB:2FV8}.
STRAND 41 48 {ECO:0000244|PDB:2FV8}.
STRAND 51 59 {ECO:0000244|PDB:2FV8}.
TURN 67 69 {ECO:0000244|PDB:2FV8}.
HELIX 70 73 {ECO:0000244|PDB:2FV8}.
STRAND 79 85 {ECO:0000244|PDB:2FV8}.
HELIX 89 97 {ECO:0000244|PDB:2FV8}.
HELIX 99 106 {ECO:0000244|PDB:2FV8}.
STRAND 112 117 {ECO:0000244|PDB:2FV8}.
HELIX 119 123 {ECO:0000244|PDB:2FV8}.
HELIX 125 133 {ECO:0000244|PDB:2FV8}.
HELIX 141 150 {ECO:0000244|PDB:2FV8}.
STRAND 154 158 {ECO:0000244|PDB:2FV8}.
TURN 161 163 {ECO:0000244|PDB:2FV8}.
HELIX 167 179 {ECO:0000244|PDB:2FV8}.
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


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