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Protein

Rho-related GTP-binding protein RhoB

Gene

Rhob

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi59 – 635GTPBy similarity
Nucleotide bindingi117 – 1204GTPBy similarity

GO - Molecular functioni

  1. GDP binding Source: MGI
  2. GTP binding Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell adhesion Source: UniProtKB
  3. cell differentiation Source: UniProtKB-KW
  4. cellular response to hydrogen peroxide Source: UniProtKB
  5. cellular response to ionizing radiation Source: UniProtKB
  6. cytokinesis Source: UniProtKB
  7. endosome to lysosome transport Source: UniProtKB
  8. intracellular protein transport Source: MGI
  9. negative regulation of cell cycle Source: UniProtKB
  10. positive regulation of angiogenesis Source: UniProtKB
  11. positive regulation of apoptotic process Source: UniProtKB
  12. small GTPase mediated signal transduction Source: InterPro
  13. transformed cell apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Apoptosis, Cell adhesion, Differentiation, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_297947. Rho GTPase cycle.
REACT_299052. G alpha (12/13) signalling events.
REACT_337915. GPVI-mediated activation cascade.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-related GTP-binding protein RhoB
Gene namesi
Name:Rhob
Synonyms:Arhb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:107949. Rhob.

Subcellular locationi

  1. Late endosome membrane 1 Publication; Lipid-anchor 1 Publication
  2. Cell membrane 1 Publication; Lipid-anchor 1 Publication
  3. Nucleus 1 Publication
  4. Cleavage furrow By similarity

  5. 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.By similarity

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB
  2. cytosol Source: Ensembl
  3. early endosome Source: MGI
  4. endosome membrane Source: UniProtKB
  5. extracellular vesicular exosome Source: MGI
  6. focal adhesion Source: MGI
  7. late endosome Source: MGI
  8. late endosome membrane Source: UniProtKB-SubCell
  9. membrane Source: MGI
  10. nucleus Source: UniProtKB
  11. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193Rho-related GTP-binding protein RhoBPRO_0000030419Add
BLAST
Propeptidei194 – 1963Removed in mature formBy similarityPRO_0000030420

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541Phosphotyrosine1 Publication
Lipidationi189 – 1891S-palmitoyl cysteineBy similarity
Lipidationi192 – 1921S-palmitoyl cysteineBy similarity
Modified residuei193 – 1931Cysteine methyl esterBy similarity
Lipidationi193 – 1931S-farnesyl cysteine; in plasma membrane formBy similarity
Lipidationi193 – 1931S-geranylgeranyl cysteine; in endosomal formBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Lipoprotein, Methylation, Palmitate, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP62746.
PaxDbiP62746.
PRIDEiP62746.

PTM databases

PhosphoSiteiP62746.

Expressioni

Inductioni

By UV irradiation, N-methyl-N-nitrosourea, cisplatin, cyclohexamide and serum stimulation.2 Publications

Gene expression databases

BgeeiP62746.
CleanExiMM_RHOB.
ExpressionAtlasiP62746. baseline and differential.
GenevestigatoriP62746.

Interactioni

Subunit structurei

Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts with ARHGEF3 and AKAP13 (By similarity). Interacts with RTKN.By similarity1 Publication

Protein-protein interaction databases

IntActiP62746. 2 interactions.
MINTiMINT-2982781.

Structurei

3D structure databases

ProteinModelPortaliP62746.
SMRiP62746. Positions 2-185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector regionSequence Analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP62746.
KOiK07856.
OMAiGKKHHCV.
OrthoDBiEOG73FQPD.
PhylomeDBiP62746.
TreeFamiTF300837.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62746-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG
60 70 80 90 100
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV
110 120 130 140 150
PEVKHFCPNV PIILVANKKD LRSDEHVRTE LARMKQEPVR TDDGRAMAVR
160 170 180 190
IQAYDYLECS AKTKEGVREV FETATRAALQ KRYGSQNGCI NCCKVL
Length:196
Mass (Da):22,123
Last modified:August 1, 1988 - v1
Checksum:iCCE6FD53AE00CD83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99963 Genomic DNA. Translation: CAA68228.1.
AF481943 mRNA. Translation: AAL89687.1.
BC018275 mRNA. Translation: AAH18275.1.
AK013784 mRNA. Translation: BAB28993.1.
CCDSiCCDS25799.1.
PIRiJC5075.
RefSeqiNP_031509.1. NM_007483.2.
UniGeneiMm.687.

Genome annotation databases

EnsembliENSMUST00000067384; ENSMUSP00000067013; ENSMUSG00000054364.
GeneIDi11852.
KEGGimmu:11852.
UCSCiuc007mzp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99963 Genomic DNA. Translation: CAA68228.1.
AF481943 mRNA. Translation: AAL89687.1.
BC018275 mRNA. Translation: AAH18275.1.
AK013784 mRNA. Translation: BAB28993.1.
CCDSiCCDS25799.1.
PIRiJC5075.
RefSeqiNP_031509.1. NM_007483.2.
UniGeneiMm.687.

3D structure databases

ProteinModelPortaliP62746.
SMRiP62746. Positions 2-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP62746. 2 interactions.
MINTiMINT-2982781.

PTM databases

PhosphoSiteiP62746.

Proteomic databases

MaxQBiP62746.
PaxDbiP62746.
PRIDEiP62746.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067384; ENSMUSP00000067013; ENSMUSG00000054364.
GeneIDi11852.
KEGGimmu:11852.
UCSCiuc007mzp.1. mouse.

Organism-specific databases

CTDi388.
MGIiMGI:107949. Rhob.

Phylogenomic databases

eggNOGiCOG1100.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP62746.
KOiK07856.
OMAiGKKHHCV.
OrthoDBiEOG73FQPD.
PhylomeDBiP62746.
TreeFamiTF300837.

Enzyme and pathway databases

ReactomeiREACT_297947. Rho GTPase cycle.
REACT_299052. G alpha (12/13) signalling events.
REACT_337915. GPVI-mediated activation cascade.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.

Miscellaneous databases

NextBioi1615.
PROiP62746.
SOURCEiSearch...

Gene expression databases

BgeeiP62746.
CleanExiMM_RHOB.
ExpressionAtlasiP62746. baseline and differential.
GenevestigatoriP62746.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRHOB_MOUSE
AccessioniPrimary (citable) accession number: P62746
Secondary accession number(s): P01121, Q9CUV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: April 1, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.