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-AUG-2022, entry version 166.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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 of its
RT promoter region.";
RL Biochem. Biophys. Res. Commun. 226:688-694(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 8-27, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 susceptibility
RT to tumor formation as well as cell adhesion and growth factor signaling in
RT 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 cells
RT 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 endothelial
RT 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 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 domain.";
RL J. Biol. Chem. 271:13556-13560(1996).
RN [11]
RP INDUCTION.
RX 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 stability.";
RL Oncogene 22:6142-6150(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates apoptosis in neoplastically transformed cells after
CC DNA damage. Not essential for development but affects cell adhesion and
CC growth factor signaling in transformed cells. Plays a negative role in
CC tumorigenesis as deletion causes tumor formation. Involved in
CC intracellular protein trafficking of a number of proteins. Targets PKN1
CC to endosomes and is involved in trafficking of the EGF receptor from
CC late endosomes to lysosomes. Also required for stability and nuclear
CC trafficking of AKT1/AKT which promotes endothelial cell survival during
CC vascular development. Serves as a microtubule-dependent signal that is
CC required for the myosin contractile ring formation during cell cycle
CC cytokinesis. Required for genotoxic stress-induced cell death in breast
CC cancer cells. {ECO:0000269|PubMed:11353846,
CC ECO:0000269|PubMed:11564874, ECO:0000269|PubMed:14597666}.
CC -!- SUBUNIT: Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts with
CC ARGGEF3 (By similarity). Interacts with RTKN (PubMed:8662891).
CC Interacts with AKAP13. Interacts with RIPOR1 (By similarity).
CC {ECO:0000250|UniProtKB:P62745, ECO:0000250|UniProtKB:P62747,
CC ECO:0000269|PubMed:8662891}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:14597666}; Lipid-anchor
CC {ECO:0000269|PubMed:14597666}. Cell membrane
CC {ECO:0000269|PubMed:14597666}; Lipid-anchor
CC {ECO:0000269|PubMed:14597666}. Nucleus {ECO:0000269|PubMed:14597666}.
CC Cleavage furrow {ECO:0000250}. Note=Translocates to the equatorial
CC region before furrow formation in a ECT2-dependent manner (By
CC similarity). Late endosomal membrane (geranylgeranylated form). Plasma
CC membrane (farnesylated form). Also detected at the nuclear margin and
CC in the nucleus. {ECO:0000250}.
CC -!- INDUCTION: By UV irradiation, N-methyl-N-nitrosourea, cisplatin,
CC cyclohexamide and serum stimulation. {ECO:0000269|PubMed:13679852,
CC ECO:0000269|PubMed:7559652}.
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 similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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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 CCDS; CCDS25799.1; -.
DR PIR; JC5075; JC5075.
DR RefSeq; NP_031509.1; NM_007483.2.
DR AlphaFoldDB; P62746; -.
DR SMR; P62746; -.
DR BioGRID; 198196; 11.
DR IntAct; P62746; 4.
DR MINT; P62746; -.
DR STRING; 10090.ENSMUSP00000067013; -.
DR iPTMnet; P62746; -.
DR PhosphoSitePlus; P62746; -.
DR SwissPalm; P62746; -.
DR jPOST; P62746; -.
DR PaxDb; P62746; -.
DR PeptideAtlas; P62746; -.
DR PRIDE; P62746; -.
DR ProteomicsDB; 254975; -.
DR Antibodypedia; 3879; 225 antibodies from 34 providers.
DR DNASU; 11852; -.
DR Ensembl; ENSMUST00000067384; ENSMUSP00000067013; ENSMUSG00000054364.
DR GeneID; 11852; -.
DR KEGG; mmu:11852; -.
DR UCSC; uc007mzp.1; mouse.
DR CTD; 388; -.
DR MGI; MGI:107949; Rhob.
DR VEuPathDB; HostDB:ENSMUSG00000054364; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00950000182945; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; P62746; -.
DR OMA; WEVFETA; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; P62746; -.
DR TreeFam; TF300837; -.
DR BRENDA; 3.6.5.2; 3474.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5625900; RHO GTPases activate CIT.
DR Reactome; R-MMU-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR BioGRID-ORCS; 11852; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Rhob; mouse.
DR PRO; PR:P62746; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P62746; protein.
DR Bgee; ENSMUSG00000054364; Expressed in molar tooth and 281 other tissues.
DR ExpressionAtlas; P62746; baseline and differential.
DR Genevisible; P62746; MM.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0019003; F:GDP binding; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; 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:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0061154; P:endothelial tube morphogenesis; ISO:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW 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; Reference proteome; Transport; Tumor suppressor.
FT CHAIN 1..193
FT /note="Rho-related GTP-binding protein RhoB"
FT /id="PRO_0000030419"
FT PROPEP 194..196
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030420"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 154
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 193
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 189
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 192
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 193
FT /note="S-farnesyl cysteine; in plasma membrane form"
FT /evidence="ECO:0000250"
FT LIPID 193
FT /note="S-geranylgeranyl cysteine; in endosomal form"
FT /evidence="ECO:0000250"
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
