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P61586 (RHOA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. 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:
Transforming protein RhoA
Alternative name(s):
Rho cDNA clone 12
Short name=h12
Gene names
Name:RHOA
Synonyms:ARH12, ARHA, RHO12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Ref.14 Ref.15 Ref.24 Ref.26 Ref.27 Ref.29 Ref.35 Ref.39

Cofactor

Magnesium.

Enzyme regulation

GTP hydrolysis is stimulated by ARHGAP30. Ref.37

Subunit structure

Interacts with ARHGEF28 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. Interacts with GNB2L1/RACK1; enhances RHOA activation. Interacts with PKP4; the interaction is detected at the midbody. Interacts (GTP-bound form preferentially) with PKN2; the interaction stimulates autophosphorylation and phosphorylation of PKN2. Interacts with ARHGDIA; this interaction inactivates and stabilizes RHOA. Interacts with ARHGDIB. Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28 Ref.34 Ref.38 Ref.39

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmcytoskeleton. Cleavage furrow. Cytoplasmcell cortex. Midbody. Cell projectionlamellipodium By similarity. Note: Localized to cell-cell contacts in calcium-treated keratinocytes By similarity. Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Localizes to the equatorial cell cortex (at the site of the presumptive furrow) in early anaphase in a activated form and in a myosin- and actin-independent manner. Ref.26 Ref.27 Ref.28

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.

Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling.

Ubiquitinated by the BCR(BACURD1) and BCR(BACURD2) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Ref.31

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Host-virus interaction
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   DiseaseProto-oncogene
   LigandGTP-binding
Magnesium
Nucleotide-binding
   PTMADP-ribosylation
Lipoprotein
Methylation
Phosphoprotein
Prenylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Traceable author statement PubMed 10436159. Source: GOC

Rho protein signal transduction

Traceable author statement PubMed 10436159. Source: UniProtKB

actin cytoskeleton organization

Traceable author statement PubMed 10436159. Source: UniProtKB

apical junction assembly

Inferred from mutant phenotype Ref.39. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cleavage furrow formation

Inferred from direct assay Ref.26. Source: UniProtKB

negative regulation of axonogenesis

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

ossification involved in bone maturation

Inferred from sequence or structural similarity. Source: BHF-UCL

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

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

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of NF-kappaB import into nucleus

Non-traceable author statement PubMed 12761501. Source: UniProtKB

positive regulation of axonogenesis

Traceable author statement. Source: Reactome

positive regulation of cytokinesis

Inferred from mutant phenotype Ref.26Ref.28. Source: UniProtKB

positive regulation of neuron differentiation

Inferred from mutant phenotype PubMed 17488780. Source: MGI

positive regulation of stress fiber assembly

Inferred from direct assay PubMed 15467718. Source: MGI

regulation of axonogenesis

Traceable author statement. Source: Reactome

regulation of cell migration

Inferred from mutant phenotype Ref.29. Source: UniProtKB

regulation of osteoblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

spindle assembly involved in mitosis

Inferred from mutant phenotype PubMed 19635168. Source: BHF-UCL

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

trabecula morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapical junction complex

Inferred from direct assay Ref.39. Source: UniProtKB

cell cortex

Inferred from direct assay Ref.26. Source: UniProtKB

cell junction

Traceable author statement. Source: Reactome

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Traceable author statement PubMed 10436159. Source: UniProtKB

myosin binding

Inferred from physical interaction PubMed 15644318. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17PubMed 15644318Ref.28Ref.39. Source: UniProtKB

Complete GO annotation...

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 IbpA
Modified residue371O-AMP-threonine; by Vibrio VopS
Modified residue411ADP-ribosylasparagine; by botulinum toxin Probable
Modified residue1881Phosphoserine; by PKG/PRKG1 Ref.20
Modified residue1901Cysteine methyl ester By similarity
Lipidation1901S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis141G → V: Causes constitutive activation. Ref.33
Mutagenesis341Y → A: Abolishes interaction with DGKQ. Ref.17 Ref.30
Mutagenesis341Y → F: Abolishes AMPylation by Haemophilus IbpA. Ref.17 Ref.30
Mutagenesis631Q → L: Causes constitutive activation.
Mutagenesis1931L → M: Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT. Ref.25
Sequence conflict231I → T in BAD96276. Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P61586 [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

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] [Europe PMC] [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] [Europe PMC] [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]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adipose tissue.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Esophageal carcinoma.
[7]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
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 and Colon.
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-193.
Tissue: Mammary cancer.
[10]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-39; 45-57; 78-86; 130-144; 146-162 AND 165-184, ADP-RIBOSYLATION AT ASN-41.
Tissue: Platelet.
[11]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-193.
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ROCK1.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ROCK2.
[14]"Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling."
Quilliam L.A., Lambert Q.T., Mickelson-Young L.A., Westwick J.K., Sparks A.B., Kay B.K., Jenkins N.A., Gilbert D.J., Copeland N.G., Der C.J.
J. Biol. Chem. 271:28772-28776(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization."
Vincent S., Settleman J.
Mol. Cell. Biol. 17:2247-2256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PKN2.
[16]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF2.
[17]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DGKQ, MUTAGENESIS OF TYR-34.
[18]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRSV PROTEIN F.
[19]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTKN.
[20]"cGMP-dependent protein kinase phosphorylates and inactivates RhoA."
Sawada N., Itoh H., Yamashita J., Doi K., Inoue M., Masatsugu K., Fukunaga Y., Sakaguchi S., Sone M., Yamahara K., Yurugi T., Nakao K.
Biochem. Biophys. Res. Commun. 280:798-805(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-188 BY PRKG1.
[21]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AKAP13.
[22]"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.
[23]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YERSINIA PESTIS YOPT, CLEAVAGE.
[24]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PLCE1.
[25]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPT, CLEAVAGE, MUTAGENESIS OF LEU-193.
[26]"An ECT2-centralspindlin complex regulates the localization and function of RhoA."
Yuce O., Piekny A., Glotzer M.
J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[27]"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.
[28]"The armadillo protein p0071 regulates Rho signalling during cytokinesis."
Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M., Huttelmaier S., Hatzfeld M.
Nat. Cell Biol. 8:1432-1440(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKP4, SUBCELLULAR LOCATION.
[29]"The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin dynamics and thereby regulate cell migration."
Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L., Webb D.J.
J. Cell Sci. 122:4535-4546(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"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] [Europe PMC] [Abstract]
Cited for: AMPYLATION AT TYR-34, MUTAGENESIS OF TYR-34.
[31]"Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement."
Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M., Peng H.B., Shao F.
Mol. Cell 35:841-855(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[32]"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] [Europe PMC] [Abstract]
Cited for: AMPYLATION AT THR-37.
[33]"Activated Rac1 GTPase translocates protein phosphatase 5 to the cell membrane and stimulates phosphatase activity in vitro."
Chatterjee A., Wang L., Armstrong D.L., Rossie S.
J. Biol. Chem. 285:3872-3882(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-14.
[34]"Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1."
Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G., Brennwald P.J., Burridge K.
Nat. Cell Biol. 12:477-483(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGDIA.
[35]"ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[36]"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].
[37]"ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and cell adhesion."
Naji L., Pacholsky D., Aspenstrom P.
Biochem. Biophys. Res. Commun. 409:96-102(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[38]"RACK1 promotes breast carcinoma migration/metastasis via activation of the RhoA/Rho kinase pathway."
Cao X.X., Xu J.D., Xu J.W., Liu X.L., Cheng Y.Y., Li Q.Q., Xu Z.D., Liu X.P.
Breast Cancer Res. Treat. 126:555-563(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GNB2L1.
[39]"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
Wallace S.W., Magalhaes A., Hall A.
Mol. Cell. Biol. 31:81-91(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PKN2.
[40]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[41]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-181 OF MUTANT VAL-14.
[42]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-181 IN COMPLEX WITH PRKCL1.
[43]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-180 IN COMPLEX WITH GDP.
[44]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[45]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH MCF2.
[46]"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] [Europe PMC] [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.

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.
AK222556 mRNA. Translation: BAD96276.1.
BX647063 mRNA. Translation: CAE46190.1.
AC104452 Genomic DNA. No translation available.
AC121247 Genomic DNA. No translation available.
AC137114 Genomic DNA. No translation available.
BC001360 mRNA. Translation: AAH01360.1.
BC005976 mRNA. Translation: AAH05976.1.
L09159 mRNA. Translation: AAA50612.1.
M83094 Genomic DNA. Translation: AAA67539.1.
CCDSCCDS2795.1.
PIRTVHU12. A26675.
RefSeqNP_001655.1. NM_001664.2.
UniGeneHs.247077.

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/H1-190[»]
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[»]
3KZ1X-ray2.70E/F1-181[»]
3LW8X-ray1.85A/B/C/D2-181[»]
3LWNX-ray2.28A/B2-181[»]
3LXRX-ray1.68A2-181[»]
3MSXX-ray1.65A1-180[»]
3T06X-ray2.84B/F3-180[»]
4D0NX-ray2.10A1-184[»]
ProteinModelPortalP61586.
SMRP61586. Positions 2-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106880. 110 interactions.
DIPDIP-29642N.
IntActP61586. 44 interactions.
MINTMINT-4999683.
STRING9606.ENSP00000400175.

Chemistry

BindingDBP61586.
ChEMBLCHEMBL6052.
DrugBankDB01076. Atorvastatin.
DB00641. Simvastatin.

PTM databases

PhosphoSiteP61586.

Polymorphism databases

DMDM47606458.

Proteomic databases

MaxQBP61586.
PaxDbP61586.
PeptideAtlasP61586.
PRIDEP61586.

Protocols and materials databases

DNASU387.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000418115; ENSP00000400175; ENSG00000067560.
GeneID387.
KEGGhsa:387.
UCSCuc003cwu.3. human.

Organism-specific databases

CTD387.
GeneCardsGC03M049371.
HGNCHGNC:667. RHOA.
HPACAB005052.
MIM165390. gene.
neXtProtNX_P61586.
PharmGKBPA134865095.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233974.
HOVERGENHBG009351.
InParanoidP61586.
KOK04513.
OMARNDPHTI.
OrthoDBEOG73FQPD.
PhylomeDBP61586.
TreeFamTF300837.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
SignaLinkP61586.

Gene expression databases

ArrayExpressP61586.
BgeeP61586.
CleanExHS_RHOA.
GenevestigatorP61586.

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

ChiTaRSRHOA. human.
EvolutionaryTraceP61586.
GeneWikiRHOA.
GenomeRNAi387.
NextBio1611.
PMAP-CutDBP61586.
PROP61586.
SOURCESearch...

Entry information

Entry nameRHOA_HUMAN
AccessionPrimary (citable) accession number: P61586
Secondary accession number(s): P06749 expand/collapse secondary AC list , Q53HM4, Q5U024, Q9UDJ0, Q9UEJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 9, 2014
This is version 131 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 3

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