(data stored in SCRATCH zone)

SWISSPROT: RHOA_HUMAN

ID   RHOA_HUMAN              Reviewed;         193 AA.
AC   P61586; P06749; Q53HM4; Q5U024; Q9UDJ0; Q9UEJ4;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   08-MAY-2019, entry version 185.
DE   RecName: Full=Transforming protein RhoA;
DE   AltName: Full=Rho cDNA clone 12;
DE            Short=h12;
DE   Flags: Precursor;
GN   Name=RHOA; Synonyms=ARH12, ARHA, RHO12;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3822842; DOI=10.1093/nar/15.4.1869;
RA   Yeramian P., Chardin P., Madaule P., Tavitian A.;
RT   "Nucleotide sequence of human rho cDNA clone 12.";
RL   Nucleic Acids Res. 15:1869-1869(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=7835413; DOI=10.1006/exer.1994.1102;
RA   Fagan K.P., Oliveira L., Pittler S.J.;
RT   "Sequence of rho small GTP-binding protein cDNAs from human retina and
RT   identification of novel 5' end cloning artifacts.";
RL   Exp. Eye Res. 59:235-237(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction
RT   sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adipose tissue;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Esophageal carcinoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-193.
RC   TISSUE=Mammary cancer;
RX   PubMed=8039707; DOI=10.1016/0378-1119(94)90382-4;
RA   Moscow J.A., He R., Gudas J.M., Cowan K.H.;
RT   "Utilization of multiple polyadenylation signals in the human RHOA
RT   protooncogene.";
RL   Gene 144:229-236(1994).
RN   [10]
RP   PROTEIN SEQUENCE OF 28-39; 45-57; 78-86; 130-144; 146-162 AND 165-184,
RP   AND ADP-RIBOSYLATION AT ASN-41 (MICROBIAL INFECTION).
RC   TISSUE=Platelet;
RX   PubMed=1328215;
RA   Nemoto Y., Namba T., Teru-uchi T., Ushikubi F., Morii N., Narumiya S.;
RT   "A rho gene product in human blood platelets. I. Identification of the
RT   platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA
RT   protein.";
RL   J. Biol. Chem. 267:20916-20920(1992).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-193.
RX   PubMed=1556108;
RA   Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.;
RT   "Structure and function of the 5'-flanking sequence of the human
RT   cytosolic selenium-dependent glutathione peroxidase gene (hgpx1).";
RL   J. Biol. Chem. 267:5949-5958(1992).
RN   [12]
RP   INTERACTION WITH ROCK1.
RX   PubMed=8617235;
RA   Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A.,
RA   Fujita A., Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S.;
RT   "The small GTP-binding protein Rho binds to and activates a 160 kDa
RT   Ser/Thr protein kinase homologous to myotonic dystrophy kinase.";
RL   EMBO J. 15:1885-1893(1996).
RN   [13]
RP   INTERACTION WITH ROCK2.
RX   PubMed=8641286;
RA   Matsui T., Amano M., Yamamoto T., Chihara K., Nakafuku M., Ito M.,
RA   Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.;
RT   "Rho-associated kinase, a novel serine/threonine kinase, as a putative
RT   target for small GTP binding protein Rho.";
RL   EMBO J. 15:2208-2216(1996).
RN   [14]
RP   FUNCTION.
RX   PubMed=8910519; DOI=10.1074/jbc.271.46.28772;
RA   Quilliam L.A., Lambert Q.T., Mickelson-Young L.A., Westwick J.K.,
RA   Sparks A.B., Kay B.K., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA   Der C.J.;
RT   "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein
RT   and potential effector of Rho protein signaling.";
RL   J. Biol. Chem. 271:28772-28776(1996).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH PKN2.
RX   PubMed=9121475; DOI=10.1128/MCB.17.4.2247;
RA   Vincent S., Settleman J.;
RT   "The PRK2 kinase is a potential effector target of both Rho and Rac
RT   GTPases and regulates actin cytoskeletal organization.";
RL   Mol. Cell. Biol. 17:2247-2256(1997).
RN   [16]
RP   FUNCTION, INTERACTION WITH KCNA2, AND SUBCELLULAR LOCATION.
RX   PubMed=9635436; DOI=10.1016/S0092-8674(00)81212-X;
RA   Cachero T.G., Morielli A.D., Peralta E.G.;
RT   "The small GTP-binding protein RhoA regulates a delayed rectifier
RT   potassium channel.";
RL   Cell 93:1077-1085(1998).
RN   [17]
RP   INTERACTION WITH ARHGEF2.
RX   PubMed=9857026; DOI=10.1074/jbc.273.52.34954;
RA   Ren Y., Li R., Zheng Y., Busch H.;
RT   "Cloning and characterization of GEF-H1, a microtubule-associated
RT   guanine nucleotide exchange factor for Rac and Rho GTPases.";
RL   J. Biol. Chem. 273:34954-34960(1998).
RN   [18]
RP   INTERACTION WITH DGKQ, AND MUTAGENESIS OF TYR-34.
RX   PubMed=10066731; DOI=10.1074/jbc.274.11.6820;
RA   Houssa B., de Widt J., Kranenburg O., Moolenaar W.H.,
RA   van Blitterswijk W.J.;
RT   "Diacylglycerol kinase theta binds to and is negatively regulated by
RT   active RhoA.";
RL   J. Biol. Chem. 274:6820-6822(1999).
RN   [19]
RP   INTERACTION WITH HRSV PROTEIN F (MICROBIAL INFECTION).
RX   PubMed=10438814;
RA   Pastey M.K., Crowe J.E. Jr., Graham B.S.;
RT   "RhoA interacts with the fusion glycoprotein of respiratory syncytial
RT   virus and facilitates virus-induced syncytium formation.";
RL   J. Virol. 73:7262-7270(1999).
RN   [20]
RP   INTERACTION WITH RTKN.
RX   PubMed=10940294; DOI=10.1074/jbc.M000465200;
RA   Reynaud C., Fabre S., Jalinot P.;
RT   "The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is
RT   involved in Rho signaling to the serum response element.";
RL   J. Biol. Chem. 275:33962-33968(2000).
RN   [21]
RP   PHOSPHORYLATION AT SER-188 BY PRKG1.
RX   PubMed=11162591; DOI=10.1006/bbrc.2000.4194;
RA   Sawada N., Itoh H., Yamashita J., Doi K., Inoue M., Masatsugu K.,
RA   Fukunaga Y., Sakaguchi S., Sone M., Yamahara K., Yurugi T., Nakao K.;
RT   "cGMP-dependent protein kinase phosphorylates and inactivates RhoA.";
RL   Biochem. Biophys. Res. Commun. 280:798-805(2001).
RN   [22]
RP   INTERACTION WITH AKAP13.
RX   PubMed=11696353; DOI=10.1016/S0014-5793(01)02995-7;
RA   Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V.,
RA   Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.;
RT   "Ht31: the first protein kinase A anchoring protein to integrate
RT   protein kinase A and Rho signaling.";
RL   FEBS Lett. 507:264-268(2001).
RN   [23]
RP   INTERACTION WITH ARHGEF3.
RX   PubMed=12221096; DOI=10.1074/jbc.M207401200;
RA   Arthur W.T., Ellerbroek S.M., Der C.J., Burridge K., Wennerberg K.;
RT   "XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not
RT   RhoC.";
RL   J. Biol. Chem. 277:42964-42972(2002).
RN   [24]
RP   INTERACTION WITH YERSINIA PESTIS YOPT, CLEAVAGE (MICROBIAL INFECTION),
RP   AND FUNCTION (MICROBIAL INFECTION).
RX   PubMed=12062101; DOI=10.1016/S0092-8674(02)00766-3;
RA   Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E.;
RT   "A Yersinia effector and a Pseudomonas avirulence protein define a
RT   family of cysteine proteases functioning in bacterial pathogenesis.";
RL   Cell 109:575-588(2002).
RN   [25]
RP   FUNCTION, AND INTERACTION WITH PLCE1.
RX   PubMed=12900402; DOI=10.1074/jbc.M306904200;
RA   Wing M.R., Snyder J.T., Sondek J., Harden T.K.;
RT   "Direct activation of phospholipase C-epsilon by Rho.";
RL   J. Biol. Chem. 278:41253-41258(2003).
RN   [26]
RP   INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPT, CLEAVAGE (MICROBIAL
RP   INFECTION), MUTAGENESIS OF LEU-193, AND FUNCTION (MICROBIAL
RP   INFECTION).
RX   PubMed=12538863; DOI=10.1073/pnas.252770599;
RA   Shao F., Vacratsis P.O., Bao Z., Bowers K.E., Fierke C.A., Dixon J.E.;
RT   "Biochemical characterization of the Yersinia YopT protease: cleavage
RT   site and recognition elements in Rho GTPases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:904-909(2003).
RN   [27]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16103226; DOI=10.1083/jcb.200501097;
RA   Yuce O., Piekny A., Glotzer M.;
RT   "An ECT2-centralspindlin complex regulates the localization and
RT   function of RhoA.";
RL   J. Cell Biol. 170:571-582(2005).
RN   [28]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16236794; DOI=10.1091/mbc.E05-06-0569;
RA   Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S.,
RA   Miki T.;
RT   "Dissecting the role of Rho-mediated signaling in contractile ring
RT   formation.";
RL   Mol. Biol. Cell 17:43-55(2006).
RN   [29]
RP   INTERACTION WITH PKP4, AND SUBCELLULAR LOCATION.
RX   PubMed=17115030; DOI=10.1038/ncb1504;
RA   Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M.,
RA   Huttelmaier S., Hatzfeld M.;
RT   "The armadillo protein p0071 regulates Rho signalling during
RT   cytokinesis.";
RL   Nat. Cell Biol. 8:1432-1440(2006).
RN   [30]
RP   FUNCTION.
RX   PubMed=19934221; DOI=10.1242/jcs.053728;
RA   Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L.,
RA   Webb D.J.;
RT   "The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin
RT   dynamics and thereby regulate cell migration.";
RL   J. Cell Sci. 122:4535-4546(2009).
RN   [31]
RP   FUNCTION.
RX   PubMed=19403695; DOI=10.1091/mbc.E08-10-1074;
RA   Stirling L., Williams M.R., Morielli A.D.;
RT   "Dual roles for RHOA/RHO-kinase in the regulated trafficking of a
RT   voltage-sensitive potassium channel.";
RL   Mol. Biol. Cell 20:2991-3002(2009).
RN   [32]
RP   AMPYLATION AT TYR-34 (MICROBIAL INFECTION), AND MUTAGENESIS OF TYR-34.
RX   PubMed=19362538; DOI=10.1016/j.molcel.2009.03.008;
RA   Worby C.A., Mattoo S., Kruger R.P., Corbeil L.B., Koller A.,
RA   Mendez J.C., Zekarias B., Lazar C., Dixon J.E.;
RT   "The fic domain: regulation of cell signaling by adenylylation.";
RL   Mol. Cell 34:93-103(2009).
RN   [33]
RP   UBIQUITINATION.
RX   PubMed=19782033; DOI=10.1016/j.molcel.2009.09.004;
RA   Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M.,
RA   Peng H.B., Shao F.;
RT   "Cullin mediates degradation of RhoA through evolutionarily conserved
RT   BTB adaptors to control actin cytoskeleton structure and cell
RT   movement.";
RL   Mol. Cell 35:841-855(2009).
RN   [34]
RP   AMPYLATION AT THR-37 (MICROBIAL INFECTION).
RX   PubMed=19039103; DOI=10.1126/science.1166382;
RA   Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.;
RT   "AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding
RT   and downstream signaling.";
RL   Science 323:269-272(2009).
RN   [35]
RP   MUTAGENESIS OF GLY-14.
RX   PubMed=19948726; DOI=10.1074/jbc.M109.088427;
RA   Chatterjee A., Wang L., Armstrong D.L., Rossie S.;
RT   "Activated Rac1 GTPase translocates protein phosphatase 5 to the cell
RT   membrane and stimulates phosphatase activity in vitro.";
RL   J. Biol. Chem. 285:3872-3882(2010).
RN   [36]
RP   INTERACTION WITH ARHGDIA.
RX   PubMed=20400958; DOI=10.1038/ncb2049;
RA   Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G.,
RA   Brennwald P.J., Burridge K.;
RT   "Regulation of Rho GTPase crosstalk, degradation and activity by
RT   RhoGDI1.";
RL   Nat. Cell Biol. 12:477-483(2010).
RN   [37]
RP   FUNCTION.
RX   PubMed=20937854; DOI=10.1073/pnas.1000975107;
RA   Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
RT   "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
RT   plasma membrane of migrating cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
RN   [38]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [39]
RP   ACTIVITY REGULATION.
RX   PubMed=21565175; DOI=10.1016/j.bbrc.2011.04.116;
RA   Naji L., Pacholsky D., Aspenstrom P.;
RT   "ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics
RT   and cell adhesion.";
RL   Biochem. Biophys. Res. Commun. 409:96-102(2011).
RN   [40]
RP   INTERACTION WITH RACK1.
RX   PubMed=20499158; DOI=10.1007/s10549-010-0955-3;
RA   Cao X.X., Xu J.D., Xu J.W., Liu X.L., Cheng Y.Y., Li Q.Q., Xu Z.D.,
RA   Liu X.P.;
RT   "RACK1 promotes breast carcinoma migration/metastasis via activation
RT   of the RhoA/Rho kinase pathway.";
RL   Breast Cancer Res. Treat. 126:555-563(2011).
RN   [41]
RP   FUNCTION, AND INTERACTION WITH PKN2.
RX   PubMed=20974804; DOI=10.1128/MCB.01001-10;
RA   Wallace S.W., Magalhaes A., Hall A.;
RT   "The Rho target PRK2 regulates apical junction formation in human
RT   bronchial epithelial cells.";
RL   Mol. Cell. Biol. 31:81-91(2011).
RN   [42]
RP   INTERACTION WITH DIAPH1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23325789; DOI=10.1091/mbc.E12-08-0597;
RA   Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
RT   "cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
RT   stability and interaction with binding partners in adrenocortical
RT   cells.";
RL   Mol. Biol. Cell 24:848-857(2013).
RN   [43]
RP   GLYCOSYLATION AT TYR-34 (MICROBIAL INFECTION).
RX   PubMed=24141704; DOI=10.1038/nsmb.2688;
RA   Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
RA   Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
RA   Aktories K.;
RT   "A bacterial toxin catalyzing tyrosine glycosylation of Rho and
RT   deamidation of Gq and Gi proteins.";
RL   Nat. Struct. Mol. Biol. 20:1273-1280(2013).
RN   [44]
RP   INTERACTION WITH RIPOR2.
RX   PubMed=25588844; DOI=10.1242/jcs.161497;
RA   Gao K., Tang W., Li Y., Zhang P., Wang D., Yu L., Wang C., Wu D.;
RT   "Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at
RT   leading edges polarizes neutrophils.";
RL   J. Cell Sci. 128:992-1000(2015).
RN   [45]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [46]
RP   INTERACTION WITH RIPOR1.
RX   PubMed=27807006; DOI=10.1242/jcs.198614;
RA   Mardakheh F.K., Self A., Marshall C.J.;
RT   "RHO binding to FAM65A regulates Golgi reorientation during cell
RT   migration.";
RL   J. Cell Sci. 129:4466-4479(2016).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=9302995; DOI=10.1038/nsb0997-699;
RA   Wei Y., Zhang Y., Derewenda U., Liu X., Minor W., Nakamoto R.K.,
RA   Somlyo A.V., Somlyo A.P., Derewenda Z.S.;
RT   "Crystal structure of RhoA-GDP and its functional implications.";
RL   Nat. Struct. Biol. 4:699-703(1997).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-181 OF MUTANT VAL-14.
RX   PubMed=9545299; DOI=10.1074/jbc.273.16.9656;
RA   Ihara K., Muraguchi S., Kato M., Shimizu T., Shirakawa M., Kuroda S.,
RA   Kaibuchi K., Hakoshima T.;
RT   "Crystal structure of human RhoA in a dominantly active form complexed
RT   with a GTP analogue.";
RL   J. Biol. Chem. 273:9656-9666(1998).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-181 IN COMPLEX WITH PRKCL1.
RX   PubMed=10388627; DOI=10.1006/jsbi.1999.4114;
RA   Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K.,
RA   Hakoshima T.;
RT   "Biochemical and crystallographic characterization of a Rho effector
RT   domain of the protein serine/threonine kinase N in a complex with
RT   RhoA.";
RL   J. Struct. Biol. 126:166-170(1999).
RN   [50]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-180 IN COMPLEX WITH GDP.
RX   PubMed=10748207; DOI=10.1074/jbc.M910274199;
RA   Shimizu T., Ihara K., Maesaki R., Kuroda S., Kaibuchi K.,
RA   Hakoshima T.;
RT   "An open conformation of switch I revealed by the crystal structure of
RT   a Mg2+-free form of RHOA complexed with GDP. Implications for the
RT   GDP/GTP exchange mechanism.";
RL   J. Biol. Chem. 275:18311-18317(2000).
RN   [51]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=11927263; DOI=10.1016/S1074-5521(02)00112-6;
RA   Graham D.L., Lowe P.N., Grime G.W., Marsh M., Rittinger K.,
RA   Smerdon S.J., Gamblin S.J., Eccleston J.F.;
RT   "MgF(3)(-) as a transition state analog of phosphoryl transfer.";
RL   Chem. Biol. 9:375-381(2002).
RN   [52]
RP   X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH MCF2.
RX   PubMed=12006984; DOI=10.1038/nsb796;
RA   Snyder J.T., Worthylake D.K., Rossman K.L., Betts L., Pruitt W.M.,
RA   Siderovski D.P., Der C.J., Sondek J.;
RT   "Structural basis for the selective activation of Rho GTPases by Dbl
RT   exchange factors.";
RL   Nat. Struct. Biol. 9:468-475(2002).
RN   [53]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF MUTANT LEU-63 IN COMPLEX WITH
RP   A GTP ANALOG AND MG(2+).
RX   PubMed=12777804; DOI=10.1107/S0907444903005390;
RA   Longenecker K., Read P., Lin S.-K., Somlyo A.P., Nakamoto R.K.,
RA   Derewenda Z.S.;
RT   "Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A
RT   resolution.";
RL   Acta Crystallogr. D 59:876-880(2003).
CC   -!- FUNCTION: Regulates a signal transduction pathway linking plasma
CC       membrane receptors to the assembly of focal adhesions and actin
CC       stress fibers. Involved in a microtubule-dependent signal that is
CC       required for the myosin contractile ring formation during cell
CC       cycle cytokinesis. Plays an essential role in cleavage furrow
CC       formation. Required for the apical junction formation of
CC       keratinocyte cell-cell adhesion. Stimulates PKN2 kinase activity.
CC       May be an activator of PLCE1. Activated by ARHGEF2, which promotes
CC       the exchange of GDP for GTP. Essential for the SPATA13-mediated
CC       regulation of cell migration and adhesion assembly and
CC       disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an
CC       important role in ERBB2-dependent stabilization of microtubules at
CC       the cell cortex. It controls the localization of APC and CLASP2 to
CC       the cell membrane, via the regulation of GSK3B activity. In turn,
CC       membrane-bound APC allows the localization of the MACF1 to the
CC       cell membrane, which is required for microtubule capture and
CC       stabilization. Regulates a signal transduction pathway linking
CC       plasma membrane receptors to the assembly of focal adhesions and
CC       actin stress fibers. Involved in a microtubule-dependent signal
CC       that is required for the myosin contractile ring formation during
CC       cell cycle cytokinesis. Plays an essential role in cleavage furrow
CC       formation. Required for the apical junction formation of
CC       keratinocyte cell-cell adhesion. May be an activator of PLCE1.
CC       Activated by ARHGEF2, which promotes the exchange of GDP for GTP.
CC       Essential for the SPATA13-mediated regulation of cell migration
CC       and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1
CC       signaling pathway plays an important role in ERBB2-dependent
CC       stabilization of microtubules at the cell cortex. It controls the
CC       localization of APC and CLASP2 to the cell membrane, via the
CC       regulation of GSK3B activity. In turn, membrane-bound APC allows
CC       the localization of the MACF1 to the cell membrane, which is
CC       required for microtubule capture and stabilization (By
CC       similarity). Regulates KCNA2 potassium channel activity by
CC       reducing its location at the cell surface in response to CHRM1
CC       activation; promotes KCNA2 endocytosis (PubMed:9635436,
CC       PubMed:19403695). {ECO:0000250, ECO:0000269|PubMed:12900402,
CC       ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794,
CC       ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20937854,
CC       ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519,
CC       ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9635436}.
CC   -!- FUNCTION: (Microbial infection) Serves as a target for the yopT
CC       cysteine peptidase from Yersinia pestis, vector of the plague.
CC       {ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12538863}.
CC   -!- FUNCTION: (Microbial infection) Serves as a target for the yopT
CC       cysteine peptidase from Yersinia pseudotuberculosis, which causes
CC       gastrointestinal disorders. {ECO:0000269|PubMed:12062101,
CC       ECO:0000269|PubMed:12538863}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:12777804};
CC   -!- ACTIVITY REGULATION: GTP hydrolysis is stimulated by ARHGAP30.
CC       {ECO:0000269|PubMed:21565175}.
CC   -!- SUBUNIT: Interacts with ARHGEF28 (By similarity). Interacts (via
CC       GTP-bound form) with RIPOR1 (via N-terminus); this interaction
CC       links RHOA to STK24 and STK26 kinases (PubMed:27807006). Interacts
CC       with RIPOR2 (via active GTP- or inactive GDP-bound forms) isoform
CC       1 and isoform 2; these interactions are direct, block the loading
CC       of GTP to RHOA and decrease upon chemokine CCL19 stimulation in
CC       primary T lymphocytes (PubMed:25588844). Binds PRKCL1, ROCK1 and
CC       ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts
CC       with PLCE1 and AKAP13. Interacts with DIAPH1 (PubMed:23325789).
CC       Interacts (in the constitutively activated, GTP-bound form) with
CC       DGKQ. Interacts with RACK1; enhances RHOA activation. Interacts
CC       with PKP4; the interaction is detected at the midbody. Interacts
CC       (GTP-bound form preferentially) with PKN2; the interaction
CC       stimulates autophosphorylation and phosphorylation of PKN2.
CC       Interacts with ARHGDIA; this interaction inactivates and
CC       stabilizes RHOA. Interacts with ARHGDIB. Interacts (GTP-bound
CC       form) with KCNA2 (via cytoplasmic N-terminal domain)
CC       (PubMed:9635436). {ECO:0000250|UniProtKB:Q9QUI0,
CC       ECO:0000269|PubMed:10066731, ECO:0000269|PubMed:10388627,
CC       ECO:0000269|PubMed:10748207, ECO:0000269|PubMed:10940294,
CC       ECO:0000269|PubMed:11696353, ECO:0000269|PubMed:12006984,
CC       ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12221096,
CC       ECO:0000269|PubMed:12538863, ECO:0000269|PubMed:12777804,
CC       ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:17115030,
CC       ECO:0000269|PubMed:19403695, ECO:0000269|PubMed:20400958,
CC       ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20974804,
CC       ECO:0000269|PubMed:23325789, ECO:0000269|PubMed:25588844,
CC       ECO:0000269|PubMed:27807006, ECO:0000269|PubMed:8617235,
CC       ECO:0000269|PubMed:8641286, ECO:0000269|PubMed:9121475,
CC       ECO:0000269|PubMed:9857026, ECO:0000305|PubMed:9635436}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human respiratory
CC       syncytial virus (HRSV) protein F; this interaction facilitates
CC       virus-induced syncytium formation. {ECO:0000269|PubMed:10438814}.
CC   -!- INTERACTION:
CC       Q15109:AGER; NbExp=2; IntAct=EBI-446668, EBI-1646426;
CC       Q07960:ARHGAP1; NbExp=2; IntAct=EBI-446668, EBI-602762;
CC       P52565:ARHGDIA; NbExp=5; IntAct=EBI-446668, EBI-712693;
CC       O15085:ARHGEF11; NbExp=8; IntAct=EBI-446668, EBI-311099;
CC       Q9NZN5:ARHGEF12; NbExp=2; IntAct=EBI-446668, EBI-821440;
CC       Q8IW93:ARHGEF19; NbExp=2; IntAct=EBI-446668, EBI-7799822;
CC       P46527:CDKN1B; NbExp=3; IntAct=EBI-446668, EBI-519280;
CC       Q9Y4D1:DAAM1; NbExp=5; IntAct=EBI-446668, EBI-2817289;
CC       O60610:DIAPH1; NbExp=3; IntAct=EBI-446668, EBI-3959709;
CC       O08808:Diaph1 (xeno); NbExp=3; IntAct=EBI-446668, EBI-1026445;
CC       Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-446668, EBI-747204;
CC       Q6PDM6:Mcf2l (xeno); NbExp=3; IntAct=EBI-446668, EBI-602149;
CC       P19338:NCL; NbExp=3; IntAct=EBI-446668, EBI-346967;
CC       Q9Z0S9:Rabac1 (xeno); NbExp=2; IntAct=EBI-446668, EBI-476965;
CC       Q9Y4F9:RIPOR2; NbExp=4; IntAct=EBI-446668, EBI-2798942;
CC       Q13464:ROCK1; NbExp=4; IntAct=EBI-446668, EBI-876651;
CC       Q9BST9:RTKN; NbExp=6; IntAct=EBI-446668, EBI-446694;
CC       Q8C6B2:Rtkn (xeno); NbExp=4; IntAct=EBI-446668, EBI-1162441;
CC       Q15796:SMAD2; NbExp=2; IntAct=EBI-446668, EBI-1040141;
CC       Q9HCE7-2:SMURF1; NbExp=2; IntAct=EBI-446668, EBI-9845742;
CC       A0A0F6B1Q8:sseJ (xeno); NbExp=7; IntAct=EBI-446668, EBI-10760263;
CC       Q9FD10:sseJ (xeno); NbExp=3; IntAct=EBI-446668, EBI-10690199;
CC       Q15654:TRIP6; NbExp=3; IntAct=EBI-446668, EBI-742327;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell
CC       cortex {ECO:0000269|PubMed:9635436}. Midbody. Cell projection,
CC       lamellipodium {ECO:0000250}. Note=Localized to cell-cell contacts
CC       in calcium-treated keratinocytes (By similarity). Translocates to
CC       the equatorial region before furrow formation in a ECT2-dependent
CC       manner. Localizes to the equatorial cell cortex (at the site of
CC       the presumptive furrow) in early anaphase in an activated form and
CC       in a myosin- and actin-independent manner. {ECO:0000250}.
CC   -!- DOMAIN: The basic-rich region is essential for yopT recognition
CC       and cleavage.
CC   -!- PTM: (Microbial infection) Substrate for botulinum ADP-
CC       ribosyltransferase. {ECO:0000269|PubMed:1328215}.
CC   -!- PTM: (Microbial infection) Cleaved by yopT protease when the cell
CC       is infected by some Yersinia pathogens. This removes the lipid
CC       attachment, and leads to its displacement from plasma membrane and
CC       to subsequent cytoskeleton cleavage. {ECO:0000269|PubMed:12062101,
CC       ECO:0000269|PubMed:12538863}.
CC   -!- PTM: (Microbial infection) AMPylation at Tyr-34 and Thr-37 are
CC       mediated by bacterial enzymes in case of infection by H.somnus and
CC       V.parahaemolyticus, respectively. AMPylation occurs in the
CC       effector region and leads to inactivation of the GTPase activity
CC       by preventing the interaction with downstream effectors, thereby
CC       inhibiting actin assembly in infected cells. It is unclear whether
CC       some human enzyme mediates AMPylation; FICD has such ability in
CC       vitro but additional experiments remain to be done to confirm
CC       results in vivo. {ECO:0000269|PubMed:19039103,
CC       ECO:0000269|PubMed:19362538}.
CC   -!- PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus
CC       asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230
CC       inhibits downstream signaling by an impaired interaction with
CC       diverse regulator and effector proteins of Rho and leads to actin
CC       disassembly. {ECO:0000269|PubMed:24141704}.
CC   -!- PTM: Phosphorylation by PRKG1 at Ser-188 inactivates RHOA
CC       signaling (PubMed:11162591). Phosphorylation by SLK at Ser-188 in
CC       response to AGTR2 activation (By similarity).
CC       {ECO:0000250|UniProtKB:P61589, ECO:0000269|PubMed:11162591}.
CC   -!- PTM: Ubiquitinated by the BCR(KCTD13) and BCR(TNFAIP1) E3
CC       ubiquitin ligase complexes, leading to its degradation by the
CC       proteasome, thereby regulating the actin cytoskeleton and synaptic
CC       transmission in neurons. {ECO:0000269|PubMed:19782033}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/RHOAID42107ch3p21.html";
DR   EMBL; X05026; CAA28690.1; -; mRNA.
DR   EMBL; L25080; AAC33178.1; -; mRNA.
DR   EMBL; AF498970; AAM21117.1; -; mRNA.
DR   EMBL; BT019870; AAV38673.1; -; mRNA.
DR   EMBL; AK222556; BAD96276.1; -; mRNA.
DR   EMBL; BX647063; CAE46190.1; -; mRNA.
DR   EMBL; AC104452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC137114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001360; AAH01360.1; -; mRNA.
DR   EMBL; BC005976; AAH05976.1; -; mRNA.
DR   EMBL; L09159; AAA50612.1; -; mRNA.
DR   EMBL; M83094; AAA67539.1; -; Genomic_DNA.
DR   CCDS; CCDS2795.1; -.
DR   PIR; A26675; TVHU12.
DR   RefSeq; NP_001300870.1; NM_001313941.1.
DR   RefSeq; NP_001655.1; NM_001664.3.
DR   PDB; 1A2B; X-ray; 2.40 A; A=1-181.
DR   PDB; 1CC0; X-ray; 5.00 A; A/C=1-190.
DR   PDB; 1CXZ; X-ray; 2.20 A; A=1-181.
DR   PDB; 1DPF; X-ray; 2.00 A; A=1-180.
DR   PDB; 1FTN; X-ray; 2.10 A; A=1-193.
DR   PDB; 1KMQ; X-ray; 1.55 A; A=4-181.
DR   PDB; 1LB1; X-ray; 2.81 A; B/D/F/H=1-190.
DR   PDB; 1OW3; X-ray; 1.80 A; B=1-193.
DR   PDB; 1S1C; X-ray; 2.60 A; A/B=1-181.
DR   PDB; 1TX4; X-ray; 1.65 A; B=3-179.
DR   PDB; 1X86; X-ray; 3.22 A; B/D/F/H=1-193.
DR   PDB; 1XCG; X-ray; 2.50 A; B/F=3-180.
DR   PDB; 2RGN; X-ray; 3.50 A; C/F=1-193.
DR   PDB; 3KZ1; X-ray; 2.70 A; E/F=1-181.
DR   PDB; 3LW8; X-ray; 1.85 A; A/B/C/D=2-181.
DR   PDB; 3LWN; X-ray; 2.28 A; A/B=2-181.
DR   PDB; 3LXR; X-ray; 1.68 A; A=2-181.
DR   PDB; 3MSX; X-ray; 1.65 A; A=1-180.
DR   PDB; 3T06; X-ray; 2.84 A; B/F=3-180.
DR   PDB; 4D0N; X-ray; 2.10 A; A=1-184.
DR   PDB; 4XH9; X-ray; 2.00 A; B/E=2-180.
DR   PDB; 4XOI; X-ray; 2.09 A; A/C=1-180.
DR   PDB; 4XSG; X-ray; 1.80 A; A=1-179.
DR   PDB; 4XSH; X-ray; 2.50 A; A=1-179.
DR   PDB; 5A0F; X-ray; 2.00 A; A=1-181.
DR   PDB; 5BWM; X-ray; 2.50 A; A=1-179.
DR   PDB; 5C2K; X-ray; 1.42 A; A=1-193.
DR   PDB; 5C4M; X-ray; 1.30 A; A=1-193.
DR   PDB; 5EZ6; X-ray; 1.80 A; B=1-181.
DR   PDB; 5FR1; X-ray; 2.75 A; A=1-193.
DR   PDB; 5FR2; X-ray; 3.35 A; A=1-193.
DR   PDB; 5HPY; X-ray; 2.40 A; B/F=3-181.
DR   PDB; 5IRC; X-ray; 1.72 A; D/F=2-181.
DR   PDB; 5JCP; X-ray; 2.10 A; A/B=1-181.
DR   PDB; 5JHG; X-ray; 2.50 A; B/F=1-181.
DR   PDB; 5JHH; X-ray; 2.30 A; B/F=1-181.
DR   PDB; 5M6X; X-ray; 2.40 A; B/I=2-193.
DR   PDB; 5M70; X-ray; 2.20 A; B/G=2-193.
DR   PDB; 5ZHX; X-ray; 3.50 A; e/f/g/h=1-193.
DR   PDB; 6BC0; X-ray; 2.20 A; F=1-181.
DR   PDB; 6BCA; X-ray; 2.00 A; C/F=1-181.
DR   PDB; 6BCB; X-ray; 1.40 A; F=1-181.
DR   PDBsum; 1A2B; -.
DR   PDBsum; 1CC0; -.
DR   PDBsum; 1CXZ; -.
DR   PDBsum; 1DPF; -.
DR   PDBsum; 1FTN; -.
DR   PDBsum; 1KMQ; -.
DR   PDBsum; 1LB1; -.
DR   PDBsum; 1OW3; -.
DR   PDBsum; 1S1C; -.
DR   PDBsum; 1TX4; -.
DR   PDBsum; 1X86; -.
DR   PDBsum; 1XCG; -.
DR   PDBsum; 2RGN; -.
DR   PDBsum; 3KZ1; -.
DR   PDBsum; 3LW8; -.
DR   PDBsum; 3LWN; -.
DR   PDBsum; 3LXR; -.
DR   PDBsum; 3MSX; -.
DR   PDBsum; 3T06; -.
DR   PDBsum; 4D0N; -.
DR   PDBsum; 4XH9; -.
DR   PDBsum; 4XOI; -.
DR   PDBsum; 4XSG; -.
DR   PDBsum; 4XSH; -.
DR   PDBsum; 5A0F; -.
DR   PDBsum; 5BWM; -.
DR   PDBsum; 5C2K; -.
DR   PDBsum; 5C4M; -.
DR   PDBsum; 5EZ6; -.
DR   PDBsum; 5FR1; -.
DR   PDBsum; 5FR2; -.
DR   PDBsum; 5HPY; -.
DR   PDBsum; 5IRC; -.
DR   PDBsum; 5JCP; -.
DR   PDBsum; 5JHG; -.
DR   PDBsum; 5JHH; -.
DR   PDBsum; 5M6X; -.
DR   PDBsum; 5M70; -.
DR   PDBsum; 5ZHX; -.
DR   PDBsum; 6BC0; -.
DR   PDBsum; 6BCA; -.
DR   PDBsum; 6BCB; -.
DR   SMR; P61586; -.
DR   BioGrid; 106880; 186.
DR   CORUM; P61586; -.
DR   DIP; DIP-29642N; -.
DR   IntAct; P61586; 84.
DR   MINT; P61586; -.
DR   STRING; 9606.ENSP00000400175; -.
DR   BindingDB; P61586; -.
DR   ChEMBL; CHEMBL6052; -.
DR   DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR   iPTMnet; P61586; -.
DR   PhosphoSitePlus; P61586; -.
DR   SwissPalm; P61586; -.
DR   BioMuta; RHOA; -.
DR   DMDM; 47606458; -.
DR   EPD; P61586; -.
DR   jPOST; P61586; -.
DR   MaxQB; P61586; -.
DR   PaxDb; P61586; -.
DR   PeptideAtlas; P61586; -.
DR   PRIDE; P61586; -.
DR   ProteomicsDB; 57321; -.
DR   TopDownProteomics; P61586; -.
DR   DNASU; 387; -.
DR   Ensembl; ENST00000418115; ENSP00000400175; ENSG00000067560.
DR   GeneID; 387; -.
DR   KEGG; hsa:387; -.
DR   UCSC; uc003cwu.4; human.
DR   CTD; 387; -.
DR   DisGeNET; 387; -.
DR   GeneCards; RHOA; -.
DR   HGNC; HGNC:667; RHOA.
DR   HPA; CAB005052; -.
DR   MIM; 165390; gene.
DR   neXtProt; NX_P61586; -.
DR   OpenTargets; ENSG00000067560; -.
DR   PharmGKB; PA134865095; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   eggNOG; COG1100; LUCA.
DR   GeneTree; ENSGT00950000182945; -.
DR   HOGENOM; HOG000233974; -.
DR   InParanoid; P61586; -.
DR   KO; K04513; -.
DR   OMA; DLRFDQK; -.
DR   OrthoDB; 1166960at2759; -.
DR   PhylomeDB; P61586; -.
DR   TreeFam; TF300837; -.
DR   Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR   Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
DR   Reactome; R-HSA-194840; Rho GTPase cycle.
DR   Reactome; R-HSA-198203; PI3K/AKT activation.
DR   Reactome; R-HSA-209563; Axonal growth stimulation.
DR   Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR   Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-HSA-4086400; PCP/CE pathway.
DR   Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR   Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration.
DR   Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR   Reactome; R-HSA-5625970; RHO GTPases activate KTN1.
DR   Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR   Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR   Reactome; R-HSA-8985586; SLIT2:ROBO1 increases RHOA activity.
DR   SignaLink; P61586; -.
DR   SIGNOR; P61586; -.
DR   ChiTaRS; RHOA; human.
DR   EvolutionaryTrace; P61586; -.
DR   GeneWiki; RHOA; -.
DR   GenomeRNAi; 387; -.
DR   PMAP-CutDB; P61586; -.
DR   PRO; PR:P61586; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000067560; Expressed in 243 organ(s), highest expression level in metanephric glomerulus.
DR   ExpressionAtlas; P61586; baseline and differential.
DR   Genevisible; P61586; HS.
DR   GO; GO:0043296; C:apical junction complex; IDA:UniProtKB.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0030054; C:cell junction; TAS:Reactome.
DR   GO; GO:0071944; C:cell periphery; IMP:UniProtKB.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IDA:SynGO.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005768; C:endosome; IMP:AgBase.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR   GO; GO:0031982; C:vesicle; IDA:AgBase.
DR   GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR   GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IEA:Ensembl.
DR   GO; GO:0030036; P:actin cytoskeleton organization; TAS:UniProtKB.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR   GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0002363; P:alpha-beta T cell lineage commitment; IEA:Ensembl.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
DR   GO; GO:0043297; P:apical junction assembly; IMP:UniProtKB.
DR   GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0043366; P:beta selection; IEA:Ensembl.
DR   GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:1990869; P:cellular response to chemokine; IMP:UniProtKB.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:ARUK-UCL.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR   GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
DR   GO; GO:0036089; P:cleavage furrow formation; IDA:UniProtKB.
DR   GO; GO:0043542; P:endothelial cell migration; IGI:MGI.
DR   GO; GO:0097498; P:endothelial tube lumen extension; IGI:MGI.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IBA:GO_Central.
DR   GO; GO:0021861; P:forebrain radial glial cell differentiation; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0046039; P:GTP metabolic process; IEA:Ensembl.
DR   GO; GO:1903673; P:mitotic cleavage furrow formation; IMP:UniProtKB.
DR   GO; GO:0090307; P:mitotic spindle assembly; IMP:BHF-UCL.
DR   GO; GO:0050919; P:negative chemotaxis; IMP:UniProtKB.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome.
DR   GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IGI:MGI.
DR   GO; GO:0045792; P:negative regulation of cell size; IMP:CAFA.
DR   GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISS:ARUK-UCL.
DR   GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR   GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IEA:Ensembl.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR   GO; GO:0043931; P:ossification involved in bone maturation; ISS:BHF-UCL.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR   GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; TAS:Reactome.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
DR   GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IMP:ARUK-UCL.
DR   GO; GO:0060193; P:positive regulation of lipase activity; IDA:AgBase.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:ARUK-UCL.
DR   GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:MGI.
DR   GO; GO:2000406; P:positive regulation of T cell migration; IMP:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR   GO; GO:1904695; P:positive regulation of vascular smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:2000145; P:regulation of cell motility; TAS:Reactome.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl.
DR   GO; GO:0051893; P:regulation of focal adhesion assembly; TAS:ARUK-UCL.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; EXP:SynGO.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl.
DR   GO; GO:0033688; P:regulation of osteoblast proliferation; ISS:BHF-UCL.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
DR   GO; GO:0035385; P:Roundabout signaling pathway; IDA:UniProtKB.
DR   GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR   GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR   GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IEA:Ensembl.
DR   GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR   GO; GO:0061383; P:trabecula morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   Pfam; PF00071; Ras; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P61586.
DR   SWISS-2DPAGE; P61586.
KW   3D-structure; ADP-ribosylation; Cell cycle; Cell division;
KW   Cell membrane; Cell projection; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Glycoprotein; GTP-binding;
KW   Host-virus interaction; Lipoprotein; Magnesium; Membrane; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Proto-oncogene;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN         1    190       Transforming protein RhoA.
FT                                /FTId=PRO_0000030411.
FT   PROPEP      191    193       Removed in mature form.
FT                                /FTId=PRO_0000030412.
FT   NP_BIND      12     19       GTP. {ECO:0000269|PubMed:10748207,
FT                                ECO:0000269|PubMed:12777804}.
FT   NP_BIND      59     63       GTP. {ECO:0000250}.
FT   NP_BIND     117    120       GTP. {ECO:0000269|PubMed:10748207,
FT                                ECO:0000269|PubMed:12777804}.
FT   MOTIF        34     42       Effector region. {ECO:0000255}.
FT   COMPBIAS    182    187       Arg/Lys-rich (basic).
FT   SITE        189    190       Cleavage; by yopT.
FT   MOD_RES      34     34       O-AMP-tyrosine; by Haemophilus IbpA;
FT                                alternate. {ECO:0000269|PubMed:19362538}.
FT   MOD_RES      37     37       O-AMP-threonine; by Vibrio VopS.
FT                                {ECO:0000269|PubMed:19039103}.
FT   MOD_RES      41     41       ADP-ribosylasparagine; by botulinum
FT                                toxin. {ECO:0000305|PubMed:1328215}.
FT   MOD_RES     188    188       Phosphoserine; by PKG/PRKG1.
FT                                {ECO:0000269|PubMed:11162591}.
FT   MOD_RES     190    190       Cysteine methyl ester.
FT                                {ECO:0000250|UniProtKB:P62745}.
FT   LIPID       190    190       S-geranylgeranyl cysteine.
FT                                {ECO:0000250|UniProtKB:P62745}.
FT   CARBOHYD     34     34       O-linked (GlcNAc) tyrosine; by
FT                                Photorhabdus PAU_02230; alternate.
FT                                {ECO:0000269|PubMed:24141704}.
FT   MUTAGEN      14     14       G->V: Causes constitutive activation.
FT                                {ECO:0000269|PubMed:19948726}.
FT   MUTAGEN      34     34       Y->A: Abolishes interaction with DGKQ.
FT                                {ECO:0000269|PubMed:10066731,
FT                                ECO:0000269|PubMed:19362538}.
FT   MUTAGEN      34     34       Y->F: Abolishes AMPylation by Haemophilus
FT                                IbpA. {ECO:0000269|PubMed:10066731,
FT                                ECO:0000269|PubMed:19362538}.
FT   MUTAGEN      63     63       Q->L: Causes constitutive activation.
FT   MUTAGEN     193    193       L->M: Converts geranyl-geranylation to
FT                                farnesylation; does not prevent the
FT                                cleavage by yopT.
FT                                {ECO:0000269|PubMed:12538863}.
FT   CONFLICT     23     23       I -> T (in Ref. 5; BAD96276).
FT                                {ECO:0000305}.
FT   STRAND        4     13       {ECO:0000244|PDB:5C4M}.
FT   HELIX        14     16       {ECO:0000244|PDB:4XH9}.
FT   HELIX        18     27       {ECO:0000244|PDB:5C4M}.
FT   STRAND       43     47       {ECO:0000244|PDB:5C4M}.
FT   STRAND       52     58       {ECO:0000244|PDB:5C4M}.
FT   HELIX        63     69       {ECO:0000244|PDB:5C4M}.
FT   HELIX        70     73       {ECO:0000244|PDB:5C4M}.
FT   STRAND       78     85       {ECO:0000244|PDB:5C4M}.
FT   HELIX        89     97       {ECO:0000244|PDB:5C4M}.
FT   HELIX        99    106       {ECO:0000244|PDB:5C4M}.
FT   STRAND      107    109       {ECO:0000244|PDB:5FR2}.
FT   STRAND      112    117       {ECO:0000244|PDB:5C4M}.
FT   HELIX       119    121       {ECO:0000244|PDB:5C4M}.
FT   HELIX       125    132       {ECO:0000244|PDB:5C4M}.
FT   TURN        133    135       {ECO:0000244|PDB:5C4M}.
FT   HELIX       141    151       {ECO:0000244|PDB:5C4M}.
FT   STRAND      154    158       {ECO:0000244|PDB:5C4M}.
FT   TURN        161    163       {ECO:0000244|PDB:5C4M}.
FT   HELIX       167    179       {ECO:0000244|PDB:5C4M}.
FT   TURN        182    184       {ECO:0000244|PDB:5ZHX}.
FT   STRAND      185    187       {ECO:0000244|PDB:5ZHX}.
FT   STRAND      190    193       {ECO:0000244|PDB:5FR1}.
SQ   SEQUENCE   193 AA;  21768 MW;  C4DA2DC31FF858BC CRC64;
     MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT
     AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
     LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ
     ARRGKKKSGC LVL
//

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