P62746 (RHOB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho-related GTP-binding protein RhoB

Gene names

Name:	Rhob
Synonyms:	Arhb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Angiogenesis Apoptosis Cell adhesion Differentiation Protein transport Transport
Cellular component	Cell membrane Endosome Membrane Nucleus
Disease	Tumor suppressor
Ligand	GTP-binding Nucleotide-binding
Molecular function	Developmental protein
PTM	Lipoprotein Methylation Palmitate Phosphoprotein Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cell adhesion Inferred from direct assay Ref.6. Source: UniProtKB cell cycle cytokinesis Inferred from sequence or structural similarity. 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 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_component	cleavage furrow Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.8. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	GDP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 193	193	Rho-related GTP-binding protein RhoB		PRO_0000030419
	Propeptide	194 – 196	3	Removed in mature form By similarity		PRO_0000030420
Regions
	Nucleotide binding	12 – 19	8	GTP By similarity
	Nucleotide binding	59 – 63	5	GTP By similarity
	Nucleotide binding	117 – 120	4	GTP By similarity
	Motif	34 – 42	9	Effector region Potential
Amino acid modifications
	Modified residue	154	1	Phosphotyrosine Ref.12
	Modified residue	193	1	Cysteine methyl ester By similarity
	Lipidation	189	1	S-palmitoyl cysteine By similarity
	Lipidation	192	1	S-palmitoyl cysteine By similarity
	Lipidation	193	1	S-farnesyl cysteine; in plasma membrane form By similarity
	Lipidation	193	1	S-geranylgeranyl cysteine; in endosomal form By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62746 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: CCE6FD53AE00CD83	FASTA	196	22,123
	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

References

	« Hide 'large scale' referencesShow '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, 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, MASS SPECTROMETRY. 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.
IPI	IPI00404182.
PIR	JC5075.
RefSeq	NP_031509.1. NM_007483.2.
UniGene	Mm.687.
3D structure databases
ProteinModelPortal	P62746.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-2982781.
PTM databases
PhosphoSite	P62746.
Proteomic databases
PaxDb	P62746.
PRIDE	P62746.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000067384; ENSMUSP00000067013; ENSMUSG00000054364.
GeneID	11852.
KEGG	mmu:11852.
Organism-specific databases
CTD	388.
MGI	MGI:107949. Rhob.
Phylogenomic databases
eggNOG	COG1100.
HOGENOM	HOG000233974.
HOVERGEN	HBG009351.
InParanoid	P62746.
KO	K07856.
OMA	DGRAMAM.
OrthoDB	EOG4G4GRD.
Gene expression databases
ArrayExpress	P62746.
Bgee	P62746.
CleanEx	MM_RHOB.
Genevestigator	P62746.
GermOnline	ENSMUSG00000054364. Mus musculus.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003578. Small_GTPase_Rho. [Graphical view]
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00174. RHO. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51420. RHO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RHOB. mouse.
NextBio	1615.
SOURCE	Search...

Entry information

Entry name

RHOB_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program