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UniProtKB/Swiss-Prot entry P61586


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RHOA_HUMAN
Primary accession number P61586
Secondary accession numbers P06749 Q5U024 Q9UEJ4
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 72)
Name and origin of the protein
Protein name Transforming protein RhoA [Precursor]
Synonym H12
Gene name
Name: RHOA
Synonyms: ARH12, ARHA, RHO12
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/15.4.1869; PubMed=3822842 [NCBI, ExPASy, EBI, Israel, Japan]
Yeramian P., Chardin P., Madaule P., Tavitian A.;
"Nucleotide sequence of human rho cDNA clone 12.";
Nucleic Acids Res. 15:1869-1869(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Retina;
DOI=10.1006/exer.1994.1102; PubMed=7835413 [NCBI, ExPASy, EBI, Israel, Japan]
Fagan K.P., Oliveira L., Pittler S.J.;
"Sequence of rho small GTP-binding protein cDNAs from human retina and identification of novel 5' end cloning artifacts.";
Exp. Eye Res. 59:235-237(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Oesophageal carcinoma;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-193.
TISSUE=Mammary cancer;
DOI=10.1016/0378-1119(94)90382-4; PubMed=8039707 [NCBI, ExPASy, EBI, Israel, Japan]
Moscow J.A., He R., Gudas J.M., Cowan K.H.;
"Utilization of multiple polyadenylation signals in the human RHOA protooncogene.";
Gene 144:229-236(1994).
[8]
PROTEIN SEQUENCE OF 28-39; 45-57; 78-86; 130-144; 146-162 AND 165-184, AND ADP-RIBOSYLATION AT ASN-41.
PubMed=1328215 [NCBI, ExPASy, EBI, Israel, Japan]
Nemoto Y., Namba T., Teru-uchi T., Ushikubi F., Morii N., Narumiya S.;
"A rho gene product in human blood platelets. I. Identification of the platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA protein.";
J. Biol. Chem. 267:20916-20920(1992).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-193.
PubMed=1556108 [NCBI, ExPASy, EBI, Israel, Japan]
Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.;
"Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1).";
J. Biol. Chem. 267:5949-5958(1992).
[10]
INTERACTION WITH ROCK1.
PubMed=8617235 [NCBI, ExPASy, EBI, Israel, Japan]
Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A., Fujita A., Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S.;
"The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase.";
EMBO J. 15:1885-1893(1996).
[11]
INTERACTION WITH ROCK2.
PubMed=8641286 [NCBI, ExPASy, EBI, Israel, Japan]
Matsui T., Amano M., Yamamoto T., Chihara K., Nakafuku M., Ito M., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.;
"Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho.";
EMBO J. 15:2208-2216(1996).
[12]
INTERACTION WITH ARHGEF2.
DOI=10.1074/jbc.273.52.34954; PubMed=9857026 [NCBI, ExPASy, EBI, Israel, Japan]
Ren Y., Li R., Zheng Y., Busch H.;
"Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases.";
J. Biol. Chem. 273:34954-34960(1998).
[13]
INTERACTION WITH HRSV PROTEIN F.
PubMed=10438814 [NCBI, ExPASy, EBI, Israel, Japan]
Pastey M.K., Crowe J.E. Jr., Graham B.S.;
"RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation.";
J. Virol. 73:7262-7270(1999).
[14]
INTERACTION WITH RTKN.
DOI=10.1074/jbc.M000465200; PubMed=10940294 [NCBI, ExPASy, EBI, Israel, Japan]
Reynaud C., Fabre S., Jalinot P.;
"The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element.";
J. Biol. Chem. 275:33962-33968(2000).
[15]
INTERACTION WITH AKAP13.
DOI=10.1016/S0014-5793(01)02995-7; PubMed=11696353 [NCBI, ExPASy, EBI, Israel, Japan]
Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V., Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.;
"Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling.";
FEBS Lett. 507:264-268(2001).
[16]
INTERACTION WITH ARHGEF3.
DOI=10.1074/jbc.M207401200; PubMed=12221096 [NCBI, ExPASy, EBI, Israel, Japan]
Arthur W.T., Ellerbroek S.M., Der C.J., Burridge K., Wennerberg K.;
"XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC.";
J. Biol. Chem. 277:42964-42972(2002).
[17]
INTERACTION WITH YERSINIA PESTIS YOPT, AND CLEAVAGE.
DOI=10.1016/S0092-8674(02)00766-3; PubMed=12062101 [NCBI, ExPASy, EBI, Israel, Japan]
Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E.;
"A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis.";
Cell 109:575-588(2002).
[18]
FUNCTION, AND INTERACTION WITH PLCE1.
DOI=10.1074/jbc.M306904200; PubMed=12900402 [NCBI, ExPASy, EBI, Israel, Japan]
Wing M.R., Snyder J.T., Sondek J., Harden T.K.;
"Direct activation of phospholipase C-epsilon by Rho.";
J. Biol. Chem. 278:41253-41258(2003).
[19]
INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPT, CLEAVAGE, AND MUTAGENESIS OF LEU-193.
DOI=10.1073/pnas.252770599; PubMed=12538863 [NCBI, ExPASy, EBI, Israel, Japan]
Shao F., Vacratsis P.O., Bao Z., Bowers K.E., Fierke C.A., Dixon J.E.;
"Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases.";
Proc. Natl. Acad. Sci. U.S.A. 100:904-909(2003).
[20]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[21]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1038/nsb0997-699; PubMed=9302995 [NCBI, ExPASy, EBI, Israel, Japan]
Wei Y., Zhang Y., Derewenda U., Liu X., Minor W., Nakamoto R.K., Somlyo A.V., Somlyo A.P., Derewenda Z.S.;
"Crystal structure of RhoA-GDP and its functional implications.";
Nat. Struct. Biol. 4:699-703(1997).
[22]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-181 OF MUTANT VAL-14.
DOI=10.1074/jbc.273.16.9656; PubMed=9545299 [NCBI, ExPASy, EBI, Israel, Japan]
Ihara K., Muraguchi S., Kato M., Shimizu T., Shirakawa M., Kuroda S., Kaibuchi K., Hakoshima T.;
"Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue.";
J. Biol. Chem. 273:9656-9666(1998).
[23]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-181 IN COMPLEX WITH PRKCL1.
DOI=10.1006/jsbi.1999.4114; PubMed=10388627 [NCBI, ExPASy, EBI, Israel, Japan]
Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K., Hakoshima T.;
"Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA.";
J. Struct. Biol. 126:166-170(1999).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-180 IN COMPLEX WITH GDP.
DOI=10.1074/jbc.M910274199; PubMed=10748207 [NCBI, ExPASy, EBI, Israel, Japan]
Shimizu T., Ihara K., Maesaki R., Kuroda S., Kaibuchi K., Hakoshima T.;
"An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism.";
J. Biol. Chem. 275:18311-18317(2000).
[25]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1016/S1074-5521(02)00112-6; PubMed=11927263 [NCBI, ExPASy, EBI, Israel, Japan]
Graham D.L., Lowe P.N., Grime G.W., Marsh M., Rittinger K., Smerdon S.J., Gamblin S.J., Eccleston J.F.;
"MgF(3)(-) as a transition state analog of phosphoryl transfer.";
Chem. Biol. 9:375-381(2002).
[26]
X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH MCF2.
DOI=10.1038/nsb796; PubMed=12006984 [NCBI, ExPASy, EBI, Israel, Japan]
Snyder J.T., Worthylake D.K., Rossman K.L., Betts L., Pruitt W.M., Siderovski D.P., Der C.J., Sondek J.;
"Structural basis for the selective activation of Rho GTPases by Dbl exchange factors.";
Nat. Struct. Biol. 9:468-475(2002).
[27]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF MUTANT LEU-63 IN COMPLEX WITH A GTP ANALOG AND MG(2+).
DOI=10.1107/S0907444903005390; PubMed=12777804 [NCBI, ExPASy, EBI, Israel, Japan]
Longenecker K., Read P., Lin S.-K., Somlyo A.P., Nakamoto R.K., Derewenda Z.S.;
"Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution.";
Acta Crystallogr. D 59:876-880(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X05026; CAA28690.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L25080; AAC33178.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF498970; AAM21117.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019870; AAV38673.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX647063; CAE46190.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001360; AAH01360.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005976; AAH05976.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L09159; AAA50612.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M83094; AAA67539.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00478231; -.
PIR A26675; TVHU12.
RefSeq NP_001655.1; -.
UniGene Hs.247077
3D structure databases
PDB
1A2B; X-ray; 2.40 A; A=1-181.[ExPASy / RCSB / EBI]
1CC0; X-ray; 5.00 A; A/C=1-190.[ExPASy / RCSB / EBI]
1CXZ; X-ray; 2.20 A; A=1-181.[ExPASy / RCSB / EBI]
1DPF; X-ray; 2.00 A; A=1-180.[ExPASy / RCSB / EBI]
1FTN; X-ray; 2.10 A; A=1-193.[ExPASy / RCSB / EBI]
1KMQ; X-ray; 1.55 A; A=4-181.[ExPASy / RCSB / EBI]
1LB1; X-ray; 2.81 A; B/D/F/H=1-189.[ExPASy / RCSB / EBI]
1OW3; X-ray; 1.80 A; B=1-193.[ExPASy / RCSB / EBI]
1S1C; X-ray; 2.60 A; A/B=1-181.[ExPASy / RCSB / EBI]
1TX4; X-ray; 1.65 A; B=3-179.[ExPASy / RCSB / EBI]
1X86; X-ray; 3.22 A; B/D/F/H=1-193.[ExPASy / RCSB / EBI]
1XCG; X-ray; 2.50 A; B/F=3-180.[ExPASy / RCSB / EBI]
2RGN; X-ray; 3.50 A; C/F=1-193.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A2B; -.
1CC0; -.
1CXZ; -.
1DPF; -.
1FTN; -.
1KMQ; -.
1LB1; -.
1OW3; -.
1S1C; -.
1TX4; -.
1X86; -.
1XCG; -.
2RGN; -.
ModBase P61586.
Protein-protein interaction databases
IntAct P61586; 14.
PTM databases
PhosphoSite P61586; -.
Enzyme and pathway databases
Pathway_Interaction_DB amb2_neutrophils_pathway; amb2 Integrin signaling.
arf6downstreampathway; Arf6 downstream pathway.
aurora_b_pathway; Aurora B signaling.
pi3kcipathway; Class I PI3K signaling events.
endothelinpathway; Endothelins.
epha_fwdpathway; EPHA forward signaling.
epha2_fwdpathway; EPHA2 forward signaling.
ephbfwdpathway; EPHB forward signaling.
il2_1pathway; IL2-mediated signaling events.
avb3_integrin_pathway; Integrins in angiogenesis.
lis1pathway; Lissencephaly gene (LIS1) in neuronal migration and development.
lysophospholipid_pathway; LPA receptor mediated events.
trkrpathway; Neurotrophic factor-mediated Trk receptor signaling.
avb3_opn_pathway; Osteopontin-mediated events.
p75ntrpathway; p75(NTR)-mediated signaling.
a4b1_paxindep_pathway; Paxillin-independent events mediated by a4b1 and a4b7.
er_nongenomic_pathway; Plasma membrane estrogen receptor signaling.
s1p_s1p1_pathway; S1P1 pathway.
s1p_s1p2_pathway; S1P2 pathway.
s1p_s1p3_pathway; S1P3 pathway.
s1p_s1p4_pathway; S1P4 pathway.
s1p_s1p5_pathway; S1P5 pathway.
prlsignalingeventspathway; Signaling events mediated by PRL.
ptp1bpathway; Signaling events mediated by PTP1B.
vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway; Signaling events regulated by Ret tyrosine kinase.
syndecan_2_pathway; Syndecan-2-mediated signaling events.
syndecan_4_pathway; Syndecan-4-mediated signaling events.
tcrpathway; TCR signaling in naive CD4+ T cells.
tgfbrpathway; TGF-beta receptor signaling.
txa2pathway; Thromboxane A2 receptor signaling.
Reactome REACT_11044; Signaling by Rho GTPases.
REACT_11061; Signalling by NGF.
Organism-specific databases
GeneCards GC03M049371; -.
H-InvDB HIX0003297; -.
HGNC HGNC:667; RHOA.
GenAtlas RHOA.
HPA CAB005052; -.
MIM 165390; gene. [NCBI / EBI]
PharmGKB PA134865095; -.
Gene expression databases
ArrayExpress P61586; -.
Bgee P61586; -.
CleanEx HS_RHOA; -.
GermOnline ENSG00000067560; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005856; Cellular component: cytoskeleton (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003924; Molecular function: GTPase activity (traceable author statement from UniProtKB).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0017022; Molecular function: myosin binding (inferred from physical interaction from UniProtKB).
GO:0043123; Biological process: positive regulation of I-kappaB kinase/NF-kappaB cascade (inferred from expression pattern from UniProtKB).
GO:0045666; Biological process: positive regulation of neuron differentiation (inferred from mutant phenotype from MGI).
GO:0042346; Biological process: positive regulation of NF-kappaB import into nucleus (non-traceable author statement from UniProtKB).
GO:0051496; Biological process: positive regulation of stress fiber formation (inferred from direct assay from MGI).
GO:0007266; Biological process: Rho protein signal transduction (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR003578; GTPase_Rho.
IPR013753; Ras.
IPR001806; Ras_GTPase.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.
Pfam PF00071; Ras; 1.
Pfam graphical view of domain structure.
PRINTS PR00449; RASTRNSFRMNG.
SMART SM00174; RHO; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00231; small_GTP; 1.
PROSITE PS51420; RHO; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P61586; -.
PRIDE P61586; -.
Genome annotation databases
Ensembl ENSG00000067560; Homo sapiens. [Contig view]
GeneID 387; -.
KEGG hsa:387; -.
Phylogenomic databases
HOVERGEN P61586; -.
OMA P61586; QVRRGKK.
Other
DrugBank DB01076; Atorvastatin.
DB00641; Simvastatin.
NextBio 1611; -.
PMAP-CutDB P61586; -.
SOURCE RHOA; Homo sapiens.
ProtoNet P61586.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ADP-ribosylation; Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Host-virus interaction; Lipoprotein; Magnesium; Membrane; Methylation; Nucleotide-binding; Prenylation; Proto-oncogene.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   190  190     Transforming protein RhoA. PRO_0000030411
PROPEP   191   193  3     Removed in mature form. PRO_0000030412
NP_BIND   12    19  8     GTP. 
NP_BIND   59    63  5     GTP (By similarity). 
NP_BIND   117   120  4     GTP. 
MOTIF   34    42  9     Effector region (Potential). 
COMPBIAS   182   187  6     Arg/Lys-rich (basic). 
SITE   189   190  2     Cleavage; by yopT. 
MOD_RES   41    41        ADP-ribosylasparagine; by botulinum toxin (Probable). 
MOD_RES   190   190        Cysteine methyl ester. 
LIPID   190   190        S-geranylgeranyl cysteine. 
MUTAGEN   14    14        G->V: Causes constitutive activation. 
MUTAGEN   63    63        Q->L: Causes constitutive activation. 
MUTAGEN   193   193        L->M: Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT. 
STRAND   5    13  9      
HELIX   18    27  10      
STRAND   38    48  11      
STRAND   51    60  10      
HELIX   64    66  3      
TURN   67    69  3      
HELIX   70    72  3      
STRAND   78    87  10      
HELIX   90    97  8      
HELIX   99   106  8      
STRAND   112   117  6      
HELIX   119   122  4      
HELIX   125   133  9      
HELIX   141   150  10      
STRAND   154   158  5      
TURN   161   163  3      
HELIX   167   179  13      
Sequence information
Length: 193 AA [This is the length of the unprocessed precursor] Molecular weight: 21768 Da [This is the MW of the unprocessed precursor] CRC64: C4DA2DC31FF858BC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT 

        70         80         90        100        110        120 
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD 

       130        140        150        160        170        180 
LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ 

       190 
ARRGKKKSGC LVL 

P61586 in FASTA format

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