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Reviewed, UniProtKB/Swiss-Prot P61586 (RHOA_HUMAN)

Last modified February 9, 2010. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Transforming protein RhoA
Alternative name(s):
    H12
Gene names
Name: RHOA
Synonyms: ARH12, ARHA, RHO12
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Ref.19

Cofactor

Magnesium.

Subunit structure

Interacts with RGNEF By similarity. Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts with PLCE1 and AKAP13. Interacts (in the constitutively activated, GTP-bound form) with DGKQ. Interacts with human respiratory syncytial virus (HRSV) protein F; this interaction facilitates virus-induced syncytium formation. Ref.19 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm › cytoskeleton.

Domain

The basic-rich region is essential for yopT recognition and cleavage.

Post-translational modification

Substrate for botulinum ADP-ribosyltransferase.

Cleaved by yopT protease when the cell is infected by some Yersinia pathogens. This removes the lipid attachment, and leads to its displacement from plasma membrane and to subsequent cytoskeleton cleavage.

AMPylation at Tyr-34 and Thr-37 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

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Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   DiseaseProto-oncogene
   LigandGTP-binding
Magnesium
Nucleotide-binding
   PTMADP-ribosylation
Lipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processRho protein signal transduction

Traceable author statement. Source: UniProtKB

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of axonogenesis

Inferred from Experiment. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB cascade

Inferred from expression pattern. Source: UniProtKB

positive regulation of NF-kappaB import into nucleus

Non-traceable author statement. Source: UniProtKB

positive regulation of axonogenesis

Inferred from Experiment. Source: Reactome

positive regulation of neuron differentiation

Inferred from mutant phenotype. Source: MGI

positive regulation of stress fiber assembly

Inferred from direct assay. Source: MGI

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane Ref.10

Inferred from Experiment. Source: Reactome

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Traceable author statement. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARHGAP1Q079601EBI-446668,EBI-602762
ARHGDIAP525651EBI-446668,EBI-712693
ARHGEF5Q127741EBI-446668,EBI-602199
CNKSR1Q969H42EBI-446668,EBI-741671
Mcf2lQ6PDM63EBI-446668,EBI-602149From a different organism.
PKN1Q165121EBI-446668,EBI-602382
Rabac1Q9Z0S91EBI-446668,EBI-476965From a different organism.
RTKNQ9BST91EBI-446668,EBI-446694

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Transforming protein RhoA
PRO_0000030411
Propeptide191 – 1933Removed in mature form
PRO_0000030412

Regions

Nucleotide binding12 – 198GTP
Nucleotide binding59 – 635GTP By similarity
Nucleotide binding117 – 1204GTP
Motif34 – 429Effector region Potential
Compositional bias182 – 1876Arg/Lys-rich (basic)

Sites

Site189 – 1902Cleavage; by yopT

Amino acid modifications

Modified residue341O-AMP-tyrosine; by Haemophilus vopS
Modified residue371O-AMP-threonine; by Vibrio ibpA
Modified residue411ADP-ribosylasparagine; by botulinum toxin Probable
Modified residue1561Phosphotyrosine Ref.22
Modified residue1901Cysteine methyl ester
Lipidation1901S-geranylgeranyl cysteine

Experimental info

Mutagenesis141G → V: Causes constitutive activation.
Mutagenesis341Y → A: Abolishes interaction with DGKQ. Ref.13 Ref.23
Mutagenesis341Y → F: Abolishes AMPylation by Haemophilus vopS. Ref.13 Ref.23
Mutagenesis631Q → L: Causes constitutive activation.
Mutagenesis1931L → M: Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT. Ref.20

Secondary structure

1 ................................. 193
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P61586-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: C4DA2DC31FF858BC

FASTA19321,768
        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

« Hide

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References

« Hide 'large scale' references
[1]"Nucleotide sequence of human rho cDNA clone 12."
Yeramian P., Chardin P., Madaule P., Tavitian A.
Nucleic Acids Res. 15:1869-1869(1987) [PubMed: 3822842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence of rho small GTP-binding protein cDNAs from human retina and identification of novel 5' end cloning artifacts."
Fagan K.P., Oliveira L., Pittler S.J.
Exp. Eye Res. 59:235-237(1994) [PubMed: 7835413] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[3]"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.
[4]"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].
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Oesophageal carcinoma.
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Colon.
[7]"Utilization of multiple polyadenylation signals in the human RHOA protooncogene."
Moscow J.A., He R., Gudas J.M., Cowan K.H.
Gene 144:229-236(1994) [PubMed: 8039707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-193.
Tissue: Mammary cancer.
[8]"A rho gene product in human blood platelets. I. Identification of the platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA protein."
Nemoto Y., Namba T., Teru-uchi T., Ushikubi F., Morii N., Narumiya S.
J. Biol. Chem. 267:20916-20920(1992) [PubMed: 1328215] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-39; 45-57; 78-86; 130-144; 146-162 AND 165-184, ADP-RIBOSYLATION AT ASN-41.
[9]"Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1)."
Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.
J. Biol. Chem. 267:5949-5958(1992) [PubMed: 1556108] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-193.
[10]"The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase."
Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A., Fujita A., Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S.
EMBO J. 15:1885-1893(1996) [PubMed: 8617235] [Abstract]
Cited for: INTERACTION WITH ROCK1.
[11]"Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho."
Matsui T., Amano M., Yamamoto T., Chihara K., Nakafuku M., Ito M., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.
EMBO J. 15:2208-2216(1996) [PubMed: 8641286] [Abstract]
Cited for: INTERACTION WITH ROCK2.
[12]"Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases."
Ren Y., Li R., Zheng Y., Busch H.
J. Biol. Chem. 273:34954-34960(1998) [PubMed: 9857026] [Abstract]
Cited for: INTERACTION WITH ARHGEF2.
[13]"Diacylglycerol kinase theta binds to and is negatively regulated by active RhoA."
Houssa B., de Widt J., Kranenburg O., Moolenaar W.H., van Blitterswijk W.J.
J. Biol. Chem. 274:6820-6822(1999) [PubMed: 10066731] [Abstract]
Cited for: INTERACTION WITH DGKQ, MUTAGENESIS OF TYR-34.
[14]"RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation."
Pastey M.K., Crowe J.E. Jr., Graham B.S.
J. Virol. 73:7262-7270(1999) [PubMed: 10438814] [Abstract]
Cited for: INTERACTION WITH HRSV PROTEIN F.
[15]"The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element."
Reynaud C., Fabre S., Jalinot P.
J. Biol. Chem. 275:33962-33968(2000) [PubMed: 10940294] [Abstract]
Cited for: INTERACTION WITH RTKN.
[16]"Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling."
Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V., Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.
FEBS Lett. 507:264-268(2001) [PubMed: 11696353] [Abstract]
Cited for: INTERACTION WITH AKAP13.
[17]"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: 12221096] [Abstract]
Cited for: INTERACTION WITH ARHGEF3.
[18]"A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis."
Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E.
Cell 109:575-588(2002) [PubMed: 12062101] [Abstract]
Cited for: INTERACTION WITH YERSINIA PESTIS YOPT, CLEAVAGE.
[19]"Direct activation of phospholipase C-epsilon by Rho."
Wing M.R., Snyder J.T., Sondek J., Harden T.K.
J. Biol. Chem. 278:41253-41258(2003) [PubMed: 12900402] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PLCE1.
[20]"Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases."
Shao F., Vacratsis P.O., Bao Z., Bowers K.E., Fierke C.A., Dixon J.E.
Proc. Natl. Acad. Sci. U.S.A. 100:904-909(2003) [PubMed: 12538863] [Abstract]
Cited for: INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPT, CLEAVAGE, MUTAGENESIS OF LEU-193.
[21]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[22]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-156, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[23]"The fic domain: regulation of cell signaling by adenylylation."
Worby C.A., Mattoo S., Kruger R.P., Corbeil L.B., Koller A., Mendez J.C., Zekarias B., Lazar C., Dixon J.E.
Mol. Cell 34:93-103(2009) [PubMed: 19362538] [Abstract]
Cited for: AMPYLATION AT TYR-34, MUTAGENESIS OF TYR-34.
[24]"AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling."
Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.
Science 323:269-272(2009) [PubMed: 19039103] [Abstract]
Cited for: AMPYLATION AT THR-37.
[25]"Crystal structure of RhoA-GDP and its functional implications."
Wei Y., Zhang Y., Derewenda U., Liu X., Minor W., Nakamoto R.K., Somlyo A.V., Somlyo A.P., Derewenda Z.S.
Nat. Struct. Biol. 4:699-703(1997) [PubMed: 9302995] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[26]"Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue."
Ihara K., Muraguchi S., Kato M., Shimizu T., Shirakawa M., Kuroda S., Kaibuchi K., Hakoshima T.
J. Biol. Chem. 273:9656-9666(1998) [PubMed: 9545299] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-181 OF MUTANT VAL-14.
[27]"Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA."
Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K., Hakoshima T.
J. Struct. Biol. 126:166-170(1999) [PubMed: 10388627] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-181 IN COMPLEX WITH PRKCL1.
[28]"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."
Shimizu T., Ihara K., Maesaki R., Kuroda S., Kaibuchi K., Hakoshima T.
J. Biol. Chem. 275:18311-18317(2000) [PubMed: 10748207] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-180 IN COMPLEX WITH GDP.
[29]"MgF(3)(-) as a transition state analog of phosphoryl transfer."
Graham D.L., Lowe P.N., Grime G.W., Marsh M., Rittinger K., Smerdon S.J., Gamblin S.J., Eccleston J.F.
Chem. Biol. 9:375-381(2002) [PubMed: 11927263] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[30]"Structural basis for the selective activation of Rho GTPases by Dbl exchange factors."
Snyder J.T., Worthylake D.K., Rossman K.L., Betts L., Pruitt W.M., Siderovski D.P., Der C.J., Sondek J.
Nat. Struct. Biol. 9:468-475(2002) [PubMed: 12006984] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH MCF2.
[31]"Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution."
Longenecker K., Read P., Lin S.-K., Somlyo A.P., Nakamoto R.K., Derewenda Z.S.
Acta Crystallogr. D 59:876-880(2003) [PubMed: 12777804] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF MUTANT LEU-63 IN COMPLEX WITH A GTP ANALOG AND MG(2+).
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X05026 mRNA. Translation: CAA28690.1.
L25080 mRNA. Translation: AAC33178.1.
AF498970 mRNA. Translation: AAM21117.1.
BT019870 mRNA. Translation: AAV38673.1.
BX647063 mRNA. Translation: CAE46190.1.
BC001360 mRNA. Translation: AAH01360.1.
BC005976 mRNA. Translation: AAH05976.1.
L09159 mRNA. Translation: AAA50612.1.
M83094 Genomic DNA. Translation: AAA67539.1.
IPIIPI00478231.
PIRTVHU12. A26675.
RefSeqNP_001655.1.
UniGeneHs.247077
Hs.709788

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2BX-ray2.40A1-181[»]
1CC0X-ray5.00A/C1-190[»]
1CXZX-ray2.20A1-181[»]
1DPFX-ray2.00A1-180[»]
1FTNX-ray2.10A1-193[»]
1KMQX-ray1.55A4-181[»]
1LB1X-ray2.81B/D/F/H1-189[»]
1OW3X-ray1.80B1-193[»]
1S1CX-ray2.60A/B1-181[»]
1TX4X-ray1.65B3-179[»]
1X86X-ray3.22B/D/F/H1-193[»]
1XCGX-ray2.50B/F3-180[»]
2RGNX-ray3.50C/F1-193[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29642N.
IntActP61586. 14 interactions.
STRINGP61586.

PTM databases

PhosphoSiteP61586.

Proteomic databases

PeptideAtlasP61586.
PRIDEP61586.

Genome annotation databases

EnsemblENST00000418115; ENSP00000400175; ENSG00000067560; Homo sapiens. [Genome view]
GeneID387.
KEGGhsa:387.
UCSCuc003cwu.1. human.

Organism-specific databases

CTD387.
GeneCardsGC03M049371.
H-InvDBHIX0003297.
HGNCHGNC:667. RHOA.
HPACAB005052.
MIM165390. gene.
PharmGKBPA134865095.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09468.
HOGENOMHBG745225.
HOVERGENP61586.
InParanoidP61586.
OMAKWIAEVL.
PhylomeDBP61586.

Enzyme and pathway databases

Pathway_Interaction_DBamb2_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.
ReactomeREACT_11044. Signaling by Rho GTPases.
REACT_11061. Signalling by NGF.
REACT_14797. Signaling by GPCR.
REACT_18266. Axon guidance.

Gene expression databases

ArrayExpressP61586.
BgeeP61586.
CleanExHS_RHOA.
GenevestigatorP61586.
GermOnlineENSG00000067560. Homo sapiens.

Family and domain databases

InterProIPR003578. GTPase_Rho.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01076. Atorvastatin.
DB00641. Simvastatin.
NextBio1611.
PMAP-CutDBP61586.
SOURCESearch...

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Entry information

Entry nameRHOA_HUMAN
AccessionPrimary (citable) accession number: P61586
Secondary accession number(s): P06749, Q5U024, Q9UEJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: February 9, 2010
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents