(data stored in ACNUC4266 zone)

HOVERGEN: RHOB_MOUSE

ID   RHOB_MOUSE              Reviewed;         196 AA.
AC   P62746; P01121; Q9CUV7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-NOV-2009, entry version 70.
DE   RecName: Full=Rho-related GTP-binding protein RhoB;
DE   Flags: Precursor;
GN   Name=Rhob; Synonyms=Arhb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96428574; PubMed=8831676; DOI=10.1006/bbrc.1996.1415;
RA   Nakamura T., Asano M., Shindo-Okada N., Nishimura S., Monden Y.;
RT   "Cloning of the RhoB gene from the mouse genome and characterization
RT   of its promoter region.";
RL   Biochem. Biophys. Res. Commun. 226:688-694(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Hippocampus;
RX   PubMed=15543229; DOI=10.1038/sj.onc.1208224;
RA   Westmark C.J., Bartleson V.B., Malter J.S.;
RT   "RhoB mRNA is stabilized by HuR after UV light.";
RL   Oncogene 24:502-511(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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   [4]
RP   PROTEIN SEQUENCE OF 8-27, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-196.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=11564874; DOI=10.1128/MCB.21.20.6906-6912.2001;
RA   Liu A.-X., Rane N., Liu J.-P., Prendergast G.C.;
RT   "RhoB is dispensable for mouse development, but it modifies
RT   susceptibility to tumor formation as well as cell adhesion and growth
RT   factor signaling in transformed cells.";
RL   Mol. Cell. Biol. 21:6906-6912(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=11353846; DOI=10.1073/pnas.111137198;
RA   Liu A.-X., Cerniglia G.J., Bernhard E.J., Prendergast G.C.;
RT   "RhoB is required to mediate apoptosis in neoplastically transformed
RT   cells after DNA damage.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:6192-6197(2001).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14597666; DOI=10.1101/gad.1134603;
RA   Adini I., Rabinovitz I., Sun J.F., Prendergast G.C., Benjamin L.E.;
RT   "RhoB controls Akt trafficking and stage-specific survival of
RT   endothelial cells during vascular development.";
RL   Genes Dev. 17:2721-2732(2003).
RN   [9]
RP   INDUCTION.
RX   PubMed=7559652; DOI=10.1074/jbc.270.42.25172;
RA   Fritz G., Kaina B., Aktories K.;
RT   "The ras-related small GTP-binding protein RhoB is immediate-early
RT   inducible by DNA damaging treatments.";
RL   J. Biol. Chem. 270:25172-25177(1995).
RN   [10]
RP   INTERACTION WITH RTKN.
RX   MEDLINE=96278781; PubMed=8662891; DOI=10.1074/jbc.271.23.13556;
RA   Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N.,
RA   Fujisawa K., Morii N., Madaule P., Narumiya S.;
RT   "Rhotekin, a new putative target for Rho bearing homology to a
RT   serine/threonine kinase, PKN, and rhophilin in the rho-binding
RT   domain.";
RL   J. Biol. Chem. 271:13556-13560(1996).
RN   [11]
RP   INDUCTION.
RX   MEDLINE=22860510; PubMed=13679852; DOI=10.1038/sj.onc.1206638;
RA   Malcolm T., Ettehadieh E., Sadowski I.;
RT   "Mitogen-responsive expression of RhoB is regulated by RNA
RT   stability.";
RL   Oncogene 22:6142-6150(2003).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
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   -!- SUBUNIT: Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts
CC       with ARHGEF3 and AKAP13 (By similarity). Interacts with RTKN.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor. Cell
CC       membrane; Lipid-anchor. Nucleus. Note=Late endosomal membrane
CC       (geranylgeranylated form). Plasma membrane (farnesylated form).
CC       Also detected at the nuclear margin and in the nucleus.
CC   -!- INDUCTION: By UV irradiation, N-methyl-N-nitrosourea, cisplatin,
CC       cyclohexamide and serum stimulation.
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 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
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CC   -!- GENE_FAMILY: HBG009351 [ FAMILY / ALN / TREE ]
DR   EMBL; X99963; CAA68228.1; -; Genomic_DNA.
DR   EMBL; AF481943; AAL89687.1; -; mRNA.
DR   EMBL; BC018275; AAH18275.1; -; mRNA.
DR   EMBL; AK013784; BAB28993.1; -; mRNA.
DR   IPI; IPI00404182; -.
DR   PIR; JC5075; JC5075.
DR   RefSeq; NP_031509.1; -.
DR   UniGene; Mm.687; -.
DR   HSSP; P06749; 1CXZ.
DR   SMR; P62746; 2-185.
DR   STRING; P62746; -.
DR   PhosphoSite; P62746; -.
DR   PRIDE; P62746; -.
DR   Ensembl; ENSMUST00000067384; ENSMUSP00000067013; ENSMUSG00000054364; Mus musculus.
DR   GeneID; 11852; -.
DR   KEGG; mmu:11852; -.
DR   UCSC; uc007mzp.1; mouse.
DR   CTD; 11852; -.
DR   MGI; MGI:107949; Rhob.
DR   HOGENOM; P62746; -.
DR   HOVERGEN; P62746; -.
DR   OMA; RNELARM; -.
DR   NextBio; 279825; -.
DR   ArrayExpress; P62746; -.
DR   Bgee; P62746; -.
DR   CleanEx; MM_RHOB; -.
DR   Genevestigator; P62746; -.
DR   GermOnline; ENSMUSG00000054364; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0019003; F:GDP binding; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; TAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IMP:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0006927; P:transformed cell apoptosis; IDA:UniProtKB.
DR   InterPro; IPR003578; GTPase_Rho.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP_bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00174; RHO; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P62746.
DR   SWISS-2DPAGE; P62746.
KW   Angiogenesis; Apoptosis; Cell adhesion; Cell membrane;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Endosome; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Prenylation;
KW   Protein transport; Transport; Tumor suppressor.
FT   DOMAIN        7    182       PRODOM:2005.1:PD000015  2217
FT   CHAIN         1    193       Rho-related GTP-binding protein RhoB.
FT                                /FTId=PRO_0000030419.
FT   PROPEP      194    196       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000030420.
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     154    154       Phosphotyrosine.
FT   MOD_RES     193    193       Cysteine methyl ester (By similarity).
FT   LIPID       189    189       S-palmitoyl cysteine (By similarity).
FT   LIPID       192    192       S-palmitoyl cysteine (By similarity).
FT   LIPID       193    193       S-farnesyl cysteine; in plasma membrane
FT                                form (By similarity).
FT   LIPID       193    193       S-geranylgeranyl cysteine; in endosomal
FT                                form (By similarity).
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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