(data stored in ACNUC8465 zone)

SWISSPROT: 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   08-MAY-2019, entry version 170.
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
RP   IDENTIFICATION BY 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
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; 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-
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).
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
RT   deamidation of Gq and Gi proteins.";
RL   Nat. Struct. Mol. Biol. 20:1273-1280(2013).
RN   [23]
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
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. {ECO:0000269|PubMed:10508588, ECO:0000269|PubMed:15226397,
CC       ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:21373644,
CC       ECO:0000269|PubMed:9478917}.
CC   -!- SUBUNIT: Binds ROCK1 and ROCK2 (By similarity). Also binds
CC       PKN1/PRK1 (PubMed:9478917). Interacts with ARGGEF3
CC       (PubMed:12221096). Interacts with RTKN (By similarity). Interacts
CC       with AKAP13 (PubMed:11546812). Interacts with RIPOR1
CC       (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       Q9HCE7-2:SMURF1; NbExp=3; IntAct=EBI-602647, EBI-9845742;
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). {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
CC       inhibits downstream signaling by an impaired interaction with
CC       diverse regulator and effector proteins of Rho and leads to actin
CC       disassembly. {ECO:0000269|PubMed:24141704}.
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       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/RHOBID42108ch2p24.html";
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   PDBsum; 2FV8; -.
DR   SMR; P62745; -.
DR   BioGrid; 106881; 22.
DR   IntAct; P62745; 25.
DR   MINT; P62745; -.
DR   STRING; 9606.ENSP00000272233; -.
DR   ChEMBL; CHEMBL1795102; -.
DR   DrugBank; DB00083; Botulinum Toxin Type A.
DR   iPTMnet; P62745; -.
DR   PhosphoSitePlus; P62745; -.
DR   SwissPalm; P62745; -.
DR   BioMuta; RHOB; -.
DR   DMDM; 51338601; -.
DR   EPD; P62745; -.
DR   jPOST; P62745; -.
DR   MaxQB; P62745; -.
DR   PaxDb; P62745; -.
DR   PeptideAtlas; P62745; -.
DR   PRIDE; P62745; -.
DR   ProteomicsDB; 57420; -.
DR   TopDownProteomics; P62745; -.
DR   DNASU; 388; -.
DR   Ensembl; ENST00000272233; ENSP00000272233; ENSG00000143878.
DR   GeneID; 388; -.
DR   KEGG; hsa:388; -.
DR   UCSC; uc002rdv.4; human.
DR   CTD; 388; -.
DR   DisGeNET; 388; -.
DR   GeneCards; RHOB; -.
DR   HGNC; HGNC:668; RHOB.
DR   MIM; 165370; gene.
DR   neXtProt; NX_P62745; -.
DR   OpenTargets; ENSG00000143878; -.
DR   PharmGKB; PA24950; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   eggNOG; COG1100; LUCA.
DR   GeneTree; ENSGT00950000182945; -.
DR   HOGENOM; HOG000233974; -.
DR   InParanoid; P62745; -.
DR   KO; K07856; -.
DR   OMA; WEVFETA; -.
DR   OrthoDB; 1166960at2759; -.
DR   PhylomeDB; P62745; -.
DR   TreeFam; TF300837; -.
DR   Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR   Reactome; R-HSA-194840; Rho GTPase cycle.
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   SignaLink; P62745; -.
DR   SIGNOR; P62745; -.
DR   ChiTaRS; RHOB; human.
DR   EvolutionaryTrace; P62745; -.
DR   GeneWiki; RHOB; -.
DR   GenomeRNAi; 388; -.
DR   PRO; PR:P62745; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000143878; Expressed in 236 organ(s), highest expression level in tibial artery.
DR   Genevisible; P62745; HS.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; 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:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0051017; P:actin filament bundle assembly; 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:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
DR   GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
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:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
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   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P62745.
DR   SWISS-2DPAGE; P62745.
KW   3D-structure; ADP-ribosylation; Angiogenesis; Apoptosis;
KW   Cell adhesion; Cell membrane; Complete proteome;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Endosome; Glycoprotein; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein;
KW   Prenylation; Protein transport; Reference proteome; Transport;
KW   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. {ECO:0000250}.
FT   NP_BIND      59     63       GTP. {ECO:0000250}.
FT   NP_BIND     117    120       GTP. {ECO:0000250}.
FT   MOTIF        34     42       Effector region. {ECO:0000255}.
FT   MOD_RES      41     41       ADP-ribosylasparagine; by botulinum
FT                                toxin. {ECO:0000250}.
FT   MOD_RES     154    154       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P62746}.
FT   MOD_RES     193    193       Cysteine methyl ester.
FT                                {ECO:0000269|PubMed:1400319}.
FT   LIPID       189    189       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:1400319}.
FT   LIPID       192    192       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:1400319}.
FT   LIPID       193    193       S-farnesyl cysteine; in plasma membrane
FT                                form. {ECO:0000269|PubMed:1400319,
FT                                ECO:0000269|PubMed:7713879}.
FT   LIPID       193    193       S-geranylgeranyl cysteine; in endosomal
FT                                form. {ECO:0000269|PubMed:1400319,
FT                                ECO:0000269|PubMed:7713879}.
FT   CARBOHYD     34     34       O-linked (GlcNAc) tyrosine; by
FT                                Photorhabdus PAU_02230.
FT                                {ECO:0000269|PubMed:24141704}.
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                                {ECO:0000269|PubMed:15226397}.
FT   MUTAGEN      39     39       F->G: Abolishes binding to PKN1 and
FT                                trafficking of EGF receptor.
FT                                {ECO:0000269|PubMed:10508588}.
FT   MUTAGEN     189    189       C->S: No effect on prenylation. Reduced
FT                                palmitoylation. Abolishes palmitoylation;
FT                                when associated with S-192.
FT                                {ECO:0000269|PubMed:1400319}.
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                                {ECO:0000269|PubMed:1400319,
FT                                ECO:0000269|PubMed:7713879}.
FT   MUTAGEN     193    193       C->S: Abolishes methylation,
FT                                palmitoylation and prenylation.
FT                                {ECO:0000269|PubMed:1400319,
FT                                ECO:0000269|PubMed:7713879}.
FT   MUTAGEN     194    194       K->L: No effect on palmitoylation or
FT                                prenylation.
FT                                {ECO:0000269|PubMed:1400319}.
FT   STRAND        4     12       {ECO:0000244|PDB:2FV8}.
FT   HELIX        18     27       {ECO:0000244|PDB:2FV8}.
FT   STRAND       41     48       {ECO:0000244|PDB:2FV8}.
FT   STRAND       51     59       {ECO:0000244|PDB:2FV8}.
FT   TURN         67     69       {ECO:0000244|PDB:2FV8}.
FT   HELIX        70     73       {ECO:0000244|PDB:2FV8}.
FT   STRAND       79     85       {ECO:0000244|PDB:2FV8}.
FT   HELIX        89     97       {ECO:0000244|PDB:2FV8}.
FT   HELIX        99    106       {ECO:0000244|PDB:2FV8}.
FT   STRAND      112    117       {ECO:0000244|PDB:2FV8}.
FT   HELIX       119    123       {ECO:0000244|PDB:2FV8}.
FT   HELIX       125    133       {ECO:0000244|PDB:2FV8}.
FT   HELIX       141    150       {ECO:0000244|PDB:2FV8}.
FT   STRAND      154    158       {ECO:0000244|PDB:2FV8}.
FT   TURN        161    163       {ECO:0000244|PDB:2FV8}.
FT   HELIX       167    179       {ECO:0000244|PDB:2FV8}.
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
//

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