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P62745 (RHOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho-related GTP-binding protein RhoB
Alternative name(s):
Rho cDNA clone 6
Short name=h6
Gene names
Name:RHOB
Synonyms:ARH6, ARHB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.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 processAngiogenesis
Apoptosis
Cell adhesion
Differentiation
Protein transport
Transport
   Cellular componentCell membrane
Endosome
Membrane
Nucleus
   DiseaseTumor suppressor
   LigandGTP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
   PTMADP-ribosylation
Lipoprotein
Methylation
Palmitate
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Traceable author statement Ref.10. Source: GOC

Rho protein signal transduction

Traceable author statement Ref.10. Source: UniProtKB

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Traceable author statement PubMed 19637314. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Inferred from sequence or structural similarity. 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

cytokinesis

Inferred from mutant phenotype Ref.19. 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

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

transformed cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcleavage 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

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

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_functionGDP binding

Inferred from electronic annotation. Source: Ensembl

GTP binding

Traceable author statement Ref.15. Source: UniProtKB

GTPase activity

Traceable author statement Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 19637314. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TNFAIP1Q138295EBI-602647,EBI-2505861

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Rho-related GTP-binding protein RhoB
PRO_0000030417
Propeptide194 – 1963Removed in mature form
PRO_0000030418

Regions

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

Amino acid modifications

Modified residue411ADP-ribosylasparagine; by botulinum toxin By similarity
Modified residue1541Phosphotyrosine By similarity
Modified residue1931Cysteine methyl ester Ref.15
Lipidation1891S-palmitoyl cysteine Ref.15
Lipidation1921S-palmitoyl cysteine Ref.15
Lipidation1931S-farnesyl cysteine; in plasma membrane form Ref.15 Ref.16
Lipidation1931S-geranylgeranyl cysteine; in endosomal form Ref.15 Ref.16

Experimental info

Mutagenesis141G → V: No effect on internalization of EGF receptor but decreases trafficking of receptor to the lysosome with associated accumulation in late endosomes. Ref.13
Mutagenesis391F → G: Abolishes binding to PKN1 and trafficking of EGF receptor. Ref.12
Mutagenesis1891C → S: No effect on prenylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-192. Ref.15
Mutagenesis1921C → S: Reduced geranylgeranylation but no effect on farnesylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-189. Ref.15 Ref.16
Mutagenesis1931C → S: Abolishes methylation, palmitoylation and prenylation. Ref.15 Ref.16
Mutagenesis1941K → L: No effect on palmitoylation or prenylation. Ref.15

Secondary structure

................................ 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62745 [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]"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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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.

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.
CCDSCCDS1699.1.
PIRTVHURH. A01372.
RefSeqNP_004031.1. NM_004040.2.
UniGeneHs.502876.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FV8X-ray1.90A4-187[»]
ProteinModelPortalP62745.
SMRP62745. Positions 2-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106881. 12 interactions.
IntActP62745. 22 interactions.
MINTMINT-4824810.
STRING9606.ENSP00000272233.

Chemistry

ChEMBLCHEMBL1795102.

PTM databases

PhosphoSiteP62745.

Polymorphism databases

DMDM51338601.

Proteomic databases

MaxQBP62745.
PaxDbP62745.
PeptideAtlasP62745.
PRIDEP62745.

Protocols and materials databases

DNASU388.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272233; ENSP00000272233; ENSG00000143878.
GeneID388.
KEGGhsa:388.
UCSCuc002rdv.3. human.

Organism-specific databases

CTD388.
GeneCardsGC02P020568.
HGNCHGNC:668. RHOB.
HPACAB004560.
MIM165370. gene.
neXtProtNX_P62745.
PharmGKBPA24950.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233974.
HOVERGENHBG009351.
InParanoidP62745.
KOK07856.
OMAVWEVFET.
OrthoDBEOG73FQPD.
PhylomeDBP62745.
TreeFamTF300837.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
SignaLinkP62745.

Gene expression databases

ArrayExpressP62745.
BgeeP62745.
CleanExHS_RHOB.
GenevestigatorP62745.

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. human.
EvolutionaryTraceP62745.
GeneWikiRHOB.
GenomeRNAi388.
NextBio1615.
PROP62745.
SOURCESearch...

Entry information

Entry nameRHOB_HUMAN
AccessionPrimary (citable) accession number: P62745
Secondary accession number(s): B2R692 expand/collapse secondary AC list , P01121, Q5U0H6, Q7RTN5, Q7RTR9, Q9CUV7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM