P62745 (RHOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho-related GTP-binding protein RhoB

Alternative name(s):
Rho cDNA clone 6
Short name=h6

Gene names

Name:	RHOB
Synonyms:	ARH6, ARHB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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.11 Ref.12 Ref.13 Ref.19 Ref.21
Subunit structure	Binds ROCK1 and ROCK2. Also binds PKN1/PRK1. Interacts with ARGGEF3, RTKN and AKAP13. Ref.11 Ref.17 Ref.18
Subcellular location	Late endosome membrane; Lipid-anchor. Cell membrane; Lipid-anchor. Nucleus. Cleavage furrow. Note: Late endosomal membrane (geranylgeranylated form). Plasma membrane (farnesylated form). Also detected at the nuclear margin and in the nucleus. Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Ref.13 Ref.14 Ref.19
Induction	Up-regulated by DNA damaging agents like H2O2 or ionizing radiation (IR). Ref.21
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.
Miscellaneous	RHOB is one of the targets of farnesyltransferase inhibitors which are currently under investigation as cancer therapeutics. These elevate the levels of geranylgeranylated RHOB and cause mislocalization, leading to apoptosis and antineoplastic effects.
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	ADP-ribosylation Lipoprotein Methylation Palmitate Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Traceable author statement Ref.10. Source: UniProtKB angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW axon guidance Traceable author statement. Source: Reactome cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB cell cycle cytokinesis Inferred from mutant phenotype Ref.19. Source: UniProtKB cellular response to hydrogen peroxide Inferred from direct assay Ref.21. Source: UniProtKB cellular response to ionizing radiation Inferred from direct assay Ref.21. Source: UniProtKB endosome to lysosome transport Inferred from direct assay Ref.12. Source: UniProtKB negative regulation of cell cycle Inferred from sequence or structural similarity. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome positive regulation of angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of apoptotic process Inferred from mutant phenotype Ref.21. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome transformed cell apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cleavage furrow Inferred from direct assay Ref.19. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endosome membrane Inferred from direct assay Ref.13PubMed 19637314. Source: UniProtKB late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from direct assay Ref.13PubMed 19637314. Source: UniProtKB
Molecular_function	GDP binding Inferred from electronic annotation. Source: Compara GTP binding Traceable author statement Ref.15. Source: UniProtKB GTPase activity Traceable author statement Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TNFAIP1	Q13829	5	EBI-602647,EBI-2505861

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_0000030417

Propeptide

194 – 196

3

Removed in mature form

PRO_0000030418

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

41

1

ADP-ribosylasparagine; by botulinum toxin By similarity

Modified residue

154

1

Phosphotyrosine By similarity

Modified residue

193

1

Cysteine methyl ester Ref.15

Lipidation

189

1

S-palmitoyl cysteine Ref.15

Lipidation

192

1

S-palmitoyl cysteine Ref.15

Lipidation

193

1

S-farnesyl cysteine; in plasma membrane form Ref.15 Ref.16

Lipidation

193

1

S-geranylgeranyl cysteine; in endosomal form Ref.15 Ref.16

Experimental info

Mutagenesis

14

1

G → V: No effect on internalization of EGF receptor but decreases trafficking of receptor to the lysosome with associated accumulation in late endosomes. Ref.13

Mutagenesis

39

1

F → G: Abolishes binding to PKN1 and trafficking of EGF receptor. Ref.12

Mutagenesis

189

1

C → S: No effect on prenylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-192. Ref.15

Mutagenesis

192

1

C → S: Reduced geranylgeranylation but no effect on farnesylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-189. Ref.15 Ref.16

Mutagenesis

193

1

C → S: Abolishes methylation, palmitoylation and prenylation. Ref.15 Ref.16

Mutagenesis

194

1

K → L: No effect on palmitoylation or prenylation. Ref.15

Secondary structure

1

.

.

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.

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196

Helix Strand Turn

Details...

Beta strand

4 – 12

9

Helix

18 – 27

10

Beta strand

41 – 48

8

Beta strand

51 – 59

9

Turn

67 – 69

3

Helix

70 – 73

4

Beta strand

79 – 85

7

Helix

89 – 97

9

Helix

99 – 106

8

Beta strand

112 – 117

6

Helix

119 – 123

5

Helix

125 – 133

9

Helix

141 – 150

10

Beta strand

154 – 158

5

Turn

161 – 163

3

Helix

167 – 179

13

Sequences

	Sequence		Length	Mass (Da)
	P62745 [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]	"Coding sequence of human rho cDNAs clone 6 and clone 9." Chardin P., Madaule P., Tavitian A. Nucleic Acids Res. 16:2717-2717(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Hippocampus.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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]. Tissue: Brain.
[9]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 8-27; 52-68; 105-118 AND 151-162, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[10]	"A novel ras-related gene family." Madaule P., Axel R. Cell 41:31-40(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-196.
[11]	"PRK1 is targeted to endosomes by the small GTPase, RhoB." Mellor H., Flynn P., Nobes C.D., Hall A., Parker P.J. J. Biol. Chem. 273:4811-4814(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PKN1.
[12]	"Regulation of epidermal growth factor receptor traffic by the small GTPase rhoB." Gampel A., Parker P.J., Mellor H. Curr. Biol. 9:955-958(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PHE-39.
[13]	"Farnesyltransferase inhibitors disrupt EGF receptor traffic through modulation of the RhoB GTPase." Wherlock M., Gampel A., Futter C., Mellor H. J. Cell Sci. 117:3221-3231(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-14.
[14]	"Ultrastructural localization of ras-related proteins using epitope-tagged plasmids." Robertson D., Paterson H.F., Adamson P., Hall A., Monaghan P. J. Histochem. Cytochem. 43:471-480(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"Post-translational modifications of p21rho proteins." Adamson P., Marshall C.J., Hall A., Tilbrook P.A. J. Biol. Chem. 267:20033-20038(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-189 AND CYS-192, ISOPRENYLATION AT CYS-193, METHYLATION AT CYS-193, MUTAGENESIS OF CYS-189; CYS-192; CYS-193 AND LYS-194.
[16]	"CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB." Armstrong S.A., Hannah V.C., Goldstein J.L., Brown M.S. J. Biol. Chem. 270:7864-7868(1995) [PubMed] [Europe PMC] [Abstract] Cited for: ISOPRENYLATION AT CYS-193, MUTAGENESIS OF CYS-192 AND CYS-193.
[17]	"AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation." Diviani D., Soderling J., Scott J.D. J. Biol. Chem. 276:44247-44257(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AKAP13.
[18]	"XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC." Arthur W.T., Ellerbroek S.M., Der C.J., Burridge K., Wennerberg K. J. Biol. Chem. 277:42964-42972(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGEF3.
[19]	"Dissecting the role of Rho-mediated signaling in contractile ring formation." Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T. Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"The nuclear guanine nucleotide exchange factors Ect2 and Net1 regulate RhoB-mediated cell death after DNA damage." Srougi M.C., Burridge K. PLoS ONE 6:E17108-E17108(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06820 mRNA. Translation: CAA29968.1.
AF498971 mRNA. Translation: AAM21118.1.
CR542272 mRNA. Translation: CAG47068.1.
AK124398 mRNA. Translation: BAG54035.1.
AK312487 mRNA. Translation: BAG35389.1.
BT019546 mRNA. Translation: AAV38353.1.
BT019547 mRNA. Translation: AAV38354.1.
AC023137 Genomic DNA. Translation: AAY24345.1.
CH471053 Genomic DNA. Translation: EAX00819.1.
CH471053 Genomic DNA. Translation: EAX00820.1.
BC066954 mRNA. Translation: AAH66954.1.
M12174 mRNA. Translation: AAA36565.1.
BK001232 mRNA. Translation: DAA01138.1.
BK001671 Genomic DNA. Translation: DAA01912.1.

IPI

IPI00000041.

PIR

TVHURH. A01372.

RefSeq

NP_004031.1. NM_004040.2.

UniGene

Hs.502876.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FV8	X-ray	1.90	A	4-187	[»]

ProteinModelPortal

P62745.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62745. 20 interactions.

MINT

MINT-4824810.

STRING

9606.ENSP00000272233.

PTM databases

PhosphoSite

P62745.

Polymorphism databases

DMDM

51338601.

Proteomic databases

PaxDb

P62745.

PeptideAtlas

P62745.

PRIDE

P62745.

Protocols and materials databases

DNASU

388.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000272233; ENSP00000272233; ENSG00000143878.

GeneID

388.

KEGG

hsa:388.

UCSC

uc002rdv.3. human.

Organism-specific databases

CTD

388.

GeneCards

GC02P020568.

HGNC

HGNC:668. RHOB.

HPA

CAB004560.

MIM

165370. gene.

neXtProt

NX_P62745.

PharmGKB

PA24950.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233974.

HOVERGEN

HBG009351.

InParanoid

P62745.

KO

K07856.

OMA

DGRAMAM.

PhylomeDB

P62745.

Enzyme and pathway databases

Pathway_Interaction_DB

p75ntrpathway. p75(NTR)-mediated signaling.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P62745.

Bgee

P62745.

CleanEx

HS_RHOB.

Genevestigator

P62745.

GermOnline

ENSG00000143878. Homo sapiens.

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

ChEMBL

CHEMBL1795102.

ChiTaRS

RHOB. human.

EvolutionaryTrace

P62745.

GenomeRNAi

388.

NextBio

1615.

SOURCE

Search...

Entry information

Entry name

RHOB_HUMAN

Accession

Primary (citable) accession number: P62745
Secondary accession number(s): B2R692 , P01121, Q5U0H6, Q7RTN5, Q7RTR9, 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 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.