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P62746 (RHOB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho-related GTP-binding protein RhoB
Gene names
Name:Rhob
Synonyms:Arhb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.7 Ref.8

Subunit structure

Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts with ARHGEF3 and AKAP13 By similarity. Interacts with RTKN. Ref.10

Subcellular location

Late endosome membrane; Lipid-anchor. Cell membrane; Lipid-anchor. Nucleus. Cleavage furrow By similarity. Note: Translocates to the equatorial region before furrow formation in a ECT2-dependent manner By similarity. Late endosomal membrane (geranylgeranylated form). Plasma membrane (farnesylated form). Also detected at the nuclear margin and in the nucleus. Ref.8

Induction

By UV irradiation, N-methyl-N-nitrosourea, cisplatin, cyclohexamide and serum stimulation. Ref.9 Ref.11

Post-translational modification

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 By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
   Biological processAngiogenesis
Apoptosis
Cell adhesion
Differentiation
Protein transport
Transport
   Cellular componentCell membrane
Endosome
Membrane
Nucleus
   DiseaseTumor suppressor
   LigandGTP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
   PTMLipoprotein
Methylation
Palmitate
Phosphoprotein
Prenylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from direct assay Ref.6. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to hydrogen peroxide

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to ionizing radiation

Inferred from sequence or structural similarity. Source: UniProtKB

cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

endosome to lysosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell cycle

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

transformed cell apoptotic process

Inferred from direct assay Ref.7. Source: UniProtKB

   Cellular_componentcleavage furrow

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 8939998. Source: MGI

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGDP binding

Inferred from direct assay PubMed 8939998. Source: MGI

GTP binding

Traceable author statement PubMed 1400319. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Rho-related GTP-binding protein RhoB
PRO_0000030419
Propeptide194 – 1963Removed in mature form By similarity
PRO_0000030420

Regions

Nucleotide binding12 – 198GTP By similarity
Nucleotide binding59 – 635GTP By similarity
Nucleotide binding117 – 1204GTP By similarity
Motif34 – 429Effector region Potential

Amino acid modifications

Modified residue1541Phosphotyrosine Ref.12
Modified residue1931Cysteine methyl ester By similarity
Lipidation1891S-palmitoyl cysteine By similarity
Lipidation1921S-palmitoyl cysteine By similarity
Lipidation1931S-farnesyl cysteine; in plasma membrane form By similarity
Lipidation1931S-geranylgeranyl cysteine; in endosomal form By similarity

Sequences

Sequence LengthMass (Da)Tools
P62746 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: CCE6FD53AE00CD83

FASTA19622,123
        10         20         30         40         50         60 
MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG KQVELALWDT 

        70         80         90        100        110        120 
AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV PEVKHFCPNV PIILVANKKD 

       130        140        150        160        170        180 
LRSDEHVRTE LARMKQEPVR TDDGRAMAVR IQAYDYLECS AKTKEGVREV FETATRAALQ 

       190 
KRYGSQNGCI NCCKVL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the RhoB gene from the mouse genome and characterization of its promoter region."
Nakamura T., Asano M., Shindo-Okada N., Nishimura S., Monden Y.
Biochem. Biophys. Res. Commun. 226:688-694(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"RhoB mRNA is stabilized by HuR after UV light."
Westmark C.J., Bartleson V.B., Malter J.S.
Oncogene 24:502-511(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Hippocampus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Salivary gland.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 8-27, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-196.
Strain: C57BL/6J.
Tissue: Hippocampus.
[6]"RhoB is dispensable for mouse development, but it modifies susceptibility to tumor formation as well as cell adhesion and growth factor signaling in transformed cells."
Liu A.-X., Rane N., Liu J.-P., Prendergast G.C.
Mol. Cell. Biol. 21:6906-6912(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"RhoB is required to mediate apoptosis in neoplastically transformed cells after DNA damage."
Liu A.-X., Cerniglia G.J., Bernhard E.J., Prendergast G.C.
Proc. Natl. Acad. Sci. U.S.A. 98:6192-6197(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"RhoB controls Akt trafficking and stage-specific survival of endothelial cells during vascular development."
Adini I., Rabinovitz I., Sun J.F., Prendergast G.C., Benjamin L.E.
Genes Dev. 17:2721-2732(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"The ras-related small GTP-binding protein RhoB is immediate-early inducible by DNA damaging treatments."
Fritz G., Kaina B., Aktories K.
J. Biol. Chem. 270:25172-25177(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain."
Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N., Fujisawa K., Morii N., Madaule P., Narumiya S.
J. Biol. Chem. 271:13556-13560(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTKN.
[11]"Mitogen-responsive expression of RhoB is regulated by RNA stability."
Malcolm T., Ettehadieh E., Sadowski I.
Oncogene 22:6142-6150(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[12]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99963 Genomic DNA. Translation: CAA68228.1.
AF481943 mRNA. Translation: AAL89687.1.
BC018275 mRNA. Translation: AAH18275.1.
AK013784 mRNA. Translation: BAB28993.1.
PIRJC5075.
RefSeqNP_031509.1. NM_007483.2.
UniGeneMm.687.

3D structure databases

ProteinModelPortalP62746.
SMRP62746. Positions 2-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP62746. 2 interactions.
MINTMINT-2982781.

PTM databases

PhosphoSiteP62746.

Proteomic databases

PaxDbP62746.
PRIDEP62746.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067384; ENSMUSP00000067013; ENSMUSG00000054364.
GeneID11852.
KEGGmmu:11852.
UCSCuc007mzp.1. mouse.

Organism-specific databases

CTD388.
MGIMGI:107949. Rhob.

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233974.
HOVERGENHBG009351.
InParanoidP62746.
KOK07856.
OMAVWEVFET.
OrthoDBEOG73FQPD.
PhylomeDBP62746.
TreeFamTF300837.

Gene expression databases

ArrayExpressP62746.
BgeeP62746.
CleanExMM_RHOB.
GenevestigatorP62746.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRHOB. mouse.
NextBio1615.
PROP62746.
SOURCESearch...

Entry information

Entry nameRHOB_MOUSE
AccessionPrimary (citable) accession number: P62746
Secondary accession number(s): P01121, Q9CUV7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot