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Transforming protein RhoA (Rho cDNA clone 12) (h12)

 RHOA_HUMAN              Reviewed;         193 AA.
P61586; P06749; Q53HM4; Q5U024; Q9UDJ0; Q9UEJ4;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
27-SEP-2017, entry version 167.
RecName: Full=Transforming protein RhoA;
AltName: Full=Rho cDNA clone 12;
Short=h12;
Flags: Precursor;
Name=RHOA; Synonyms=ARH12, ARHA, RHO12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3822842; DOI=10.1093/nar/15.4.1869;
Yeramian P., Chardin P., Madaule P., Tavitian A.;
"Nucleotide sequence of human rho cDNA clone 12.";
Nucleic Acids Res. 15:1869-1869(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Retina;
PubMed=7835413; DOI=10.1006/exer.1994.1102;
Fagan K.P., Oliveira L., Pittler S.J.;
"Sequence of rho small GTP-binding protein cDNAs from human retina and
identification of novel 5' end cloning artifacts.";
Exp. Eye Res. 59:235-237(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adipose tissue;
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Esophageal carcinoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
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., 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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-193.
TISSUE=Mammary cancer;
PubMed=8039707; DOI=10.1016/0378-1119(94)90382-4;
Moscow J.A., He R., Gudas J.M., Cowan K.H.;
"Utilization of multiple polyadenylation signals in the human RHOA
protooncogene.";
Gene 144:229-236(1994).
[10]
PROTEIN SEQUENCE OF 28-39; 45-57; 78-86; 130-144; 146-162 AND 165-184,
AND ADP-RIBOSYLATION AT ASN-41 (MICROBIAL INFECTION).
TISSUE=Platelet;
PubMed=1328215;
Nemoto Y., Namba T., Teru-uchi T., Ushikubi F., Morii N., Narumiya S.;
"A rho gene product in human blood platelets. I. Identification of the
platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA
protein.";
J. Biol. Chem. 267:20916-20920(1992).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-193.
PubMed=1556108;
Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.;
"Structure and function of the 5'-flanking sequence of the human
cytosolic selenium-dependent glutathione peroxidase gene (hgpx1).";
J. Biol. Chem. 267:5949-5958(1992).
[12]
INTERACTION WITH ROCK1.
PubMed=8617235;
Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A.,
Fujita A., Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S.;
"The small GTP-binding protein Rho binds to and activates a 160 kDa
Ser/Thr protein kinase homologous to myotonic dystrophy kinase.";
EMBO J. 15:1885-1893(1996).
[13]
INTERACTION WITH ROCK2.
PubMed=8641286;
Matsui T., Amano M., Yamamoto T., Chihara K., Nakafuku M., Ito M.,
Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.;
"Rho-associated kinase, a novel serine/threonine kinase, as a putative
target for small GTP binding protein Rho.";
EMBO J. 15:2208-2216(1996).
[14]
FUNCTION.
PubMed=8910519; DOI=10.1074/jbc.271.46.28772;
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.;
"Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein
and potential effector of Rho protein signaling.";
J. Biol. Chem. 271:28772-28776(1996).
[15]
FUNCTION, AND INTERACTION WITH PKN2.
PubMed=9121475; DOI=10.1128/MCB.17.4.2247;
Vincent S., Settleman J.;
"The PRK2 kinase is a potential effector target of both Rho and Rac
GTPases and regulates actin cytoskeletal organization.";
Mol. Cell. Biol. 17:2247-2256(1997).
[16]
FUNCTION, INTERACTION WITH KCNA2, AND SUBCELLULAR LOCATION.
PubMed=9635436; DOI=10.1016/S0092-8674(00)81212-X;
Cachero T.G., Morielli A.D., Peralta E.G.;
"The small GTP-binding protein RhoA regulates a delayed rectifier
potassium channel.";
Cell 93:1077-1085(1998).
[17]
INTERACTION WITH ARHGEF2.
PubMed=9857026; DOI=10.1074/jbc.273.52.34954;
Ren Y., Li R., Zheng Y., Busch H.;
"Cloning and characterization of GEF-H1, a microtubule-associated
guanine nucleotide exchange factor for Rac and Rho GTPases.";
J. Biol. Chem. 273:34954-34960(1998).
[18]
INTERACTION WITH DGKQ, AND MUTAGENESIS OF TYR-34.
PubMed=10066731; DOI=10.1074/jbc.274.11.6820;
Houssa B., de Widt J., Kranenburg O., Moolenaar W.H.,
van Blitterswijk W.J.;
"Diacylglycerol kinase theta binds to and is negatively regulated by
active RhoA.";
J. Biol. Chem. 274:6820-6822(1999).
[19]
INTERACTION WITH HRSV PROTEIN F.
PubMed=10438814;
Pastey M.K., Crowe J.E. Jr., Graham B.S.;
"RhoA interacts with the fusion glycoprotein of respiratory syncytial
virus and facilitates virus-induced syncytium formation.";
J. Virol. 73:7262-7270(1999).
[20]
INTERACTION WITH RTKN.
PubMed=10940294; DOI=10.1074/jbc.M000465200;
Reynaud C., Fabre S., Jalinot P.;
"The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is
involved in Rho signaling to the serum response element.";
J. Biol. Chem. 275:33962-33968(2000).
[21]
PHOSPHORYLATION AT SER-188 BY PRKG1.
PubMed=11162591; DOI=10.1006/bbrc.2000.4194;
Sawada N., Itoh H., Yamashita J., Doi K., Inoue M., Masatsugu K.,
Fukunaga Y., Sakaguchi S., Sone M., Yamahara K., Yurugi T., Nakao K.;
"cGMP-dependent protein kinase phosphorylates and inactivates RhoA.";
Biochem. Biophys. Res. Commun. 280:798-805(2001).
[22]
INTERACTION WITH AKAP13.
PubMed=11696353; DOI=10.1016/S0014-5793(01)02995-7;
Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V.,
Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.;
"Ht31: the first protein kinase A anchoring protein to integrate
protein kinase A and Rho signaling.";
FEBS Lett. 507:264-268(2001).
[23]
INTERACTION WITH ARHGEF3.
PubMed=12221096; DOI=10.1074/jbc.M207401200;
Arthur W.T., Ellerbroek S.M., Der C.J., Burridge K., Wennerberg K.;
"XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not
RhoC.";
J. Biol. Chem. 277:42964-42972(2002).
[24]
INTERACTION WITH YERSINIA PESTIS YOPT, CLEAVAGE (MICROBIAL INFECTION),
AND FUNCTION (MICROBIAL INFECTION).
PubMed=12062101; DOI=10.1016/S0092-8674(02)00766-3;
Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E.;
"A Yersinia effector and a Pseudomonas avirulence protein define a
family of cysteine proteases functioning in bacterial pathogenesis.";
Cell 109:575-588(2002).
[25]
FUNCTION, AND INTERACTION WITH PLCE1.
PubMed=12900402; DOI=10.1074/jbc.M306904200;
Wing M.R., Snyder J.T., Sondek J., Harden T.K.;
"Direct activation of phospholipase C-epsilon by Rho.";
J. Biol. Chem. 278:41253-41258(2003).
[26]
INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPT, CLEAVAGE (MICROBIAL
INFECTION), MUTAGENESIS OF LEU-193, AND FUNCTION (MICROBIAL
INFECTION).
PubMed=12538863; DOI=10.1073/pnas.252770599;
Shao F., Vacratsis P.O., Bao Z., Bowers K.E., Fierke C.A., Dixon J.E.;
"Biochemical characterization of the Yersinia YopT protease: cleavage
site and recognition elements in Rho GTPases.";
Proc. Natl. Acad. Sci. U.S.A. 100:904-909(2003).
[27]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16103226; DOI=10.1083/jcb.200501097;
Yuce O., Piekny A., Glotzer M.;
"An ECT2-centralspindlin complex regulates the localization and
function of RhoA.";
J. Cell Biol. 170:571-582(2005).
[28]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16236794; DOI=10.1091/mbc.E05-06-0569;
Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S.,
Miki T.;
"Dissecting the role of Rho-mediated signaling in contractile ring
formation.";
Mol. Biol. Cell 17:43-55(2006).
[29]
INTERACTION WITH PKP4, AND SUBCELLULAR LOCATION.
PubMed=17115030; DOI=10.1038/ncb1504;
Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M.,
Huttelmaier S., Hatzfeld M.;
"The armadillo protein p0071 regulates Rho signalling during
cytokinesis.";
Nat. Cell Biol. 8:1432-1440(2006).
[30]
FUNCTION.
PubMed=19934221; DOI=10.1242/jcs.053728;
Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L.,
Webb D.J.;
"The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin
dynamics and thereby regulate cell migration.";
J. Cell Sci. 122:4535-4546(2009).
[31]
FUNCTION.
PubMed=19403695; DOI=10.1091/mbc.E08-10-1074;
Stirling L., Williams M.R., Morielli A.D.;
"Dual roles for RHOA/RHO-kinase in the regulated trafficking of a
voltage-sensitive potassium channel.";
Mol. Biol. Cell 20:2991-3002(2009).
[32]
AMPYLATION AT TYR-34 (MICROBIAL INFECTION), AND MUTAGENESIS OF TYR-34.
PubMed=19362538; DOI=10.1016/j.molcel.2009.03.008;
Worby C.A., Mattoo S., Kruger R.P., Corbeil L.B., Koller A.,
Mendez J.C., Zekarias B., Lazar C., Dixon J.E.;
"The fic domain: regulation of cell signaling by adenylylation.";
Mol. Cell 34:93-103(2009).
[33]
UBIQUITINATION.
PubMed=19782033; DOI=10.1016/j.molcel.2009.09.004;
Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M.,
Peng H.B., Shao F.;
"Cullin mediates degradation of RhoA through evolutionarily conserved
BTB adaptors to control actin cytoskeleton structure and cell
movement.";
Mol. Cell 35:841-855(2009).
[34]
AMPYLATION AT THR-37 (MICROBIAL INFECTION).
PubMed=19039103; DOI=10.1126/science.1166382;
Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.;
"AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding
and downstream signaling.";
Science 323:269-272(2009).
[35]
MUTAGENESIS OF GLY-14.
PubMed=19948726; DOI=10.1074/jbc.M109.088427;
Chatterjee A., Wang L., Armstrong D.L., Rossie S.;
"Activated Rac1 GTPase translocates protein phosphatase 5 to the cell
membrane and stimulates phosphatase activity in vitro.";
J. Biol. Chem. 285:3872-3882(2010).
[36]
INTERACTION WITH ARHGDIA.
PubMed=20400958; DOI=10.1038/ncb2049;
Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G.,
Brennwald P.J., Burridge K.;
"Regulation of Rho GTPase crosstalk, degradation and activity by
RhoGDI1.";
Nat. Cell Biol. 12:477-483(2010).
[37]
FUNCTION.
PubMed=20937854; DOI=10.1073/pnas.1000975107;
Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
"ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
plasma membrane of migrating cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[39]
ENZYME REGULATION.
PubMed=21565175; DOI=10.1016/j.bbrc.2011.04.116;
Naji L., Pacholsky D., Aspenstrom P.;
"ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics
and cell adhesion.";
Biochem. Biophys. Res. Commun. 409:96-102(2011).
[40]
INTERACTION WITH RACK1.
PubMed=20499158; DOI=10.1007/s10549-010-0955-3;
Cao X.X., Xu J.D., Xu J.W., Liu X.L., Cheng Y.Y., Li Q.Q., Xu Z.D.,
Liu X.P.;
"RACK1 promotes breast carcinoma migration/metastasis via activation
of the RhoA/Rho kinase pathway.";
Breast Cancer Res. Treat. 126:555-563(2011).
[41]
FUNCTION, AND INTERACTION WITH PKN2.
PubMed=20974804; DOI=10.1128/MCB.01001-10;
Wallace S.W., Magalhaes A., Hall A.;
"The Rho target PRK2 regulates apical junction formation in human
bronchial epithelial cells.";
Mol. Cell. Biol. 31:81-91(2011).
[42]
INTERACTION WITH DIAPH1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23325789; DOI=10.1091/mbc.E12-08-0597;
Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
"cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
stability and interaction with binding partners in adrenocortical
cells.";
Mol. Biol. Cell 24:848-857(2013).
[43]
GLYCOSYLATION AT TYR-34 (MICROBIAL INFECTION).
PubMed=24141704; DOI=10.1038/nsmb.2688;
Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
Aktories K.;
"A bacterial toxin catalyzing tyrosine glycosylation of Rho and
deamidation of Gq and Gi proteins.";
Nat. Struct. Mol. Biol. 20:1273-1280(2013).
[44]
INTERACTION WITH RIPOR2.
PubMed=25588844; DOI=10.1242/jcs.161497;
Gao K., Tang W., Li Y., Zhang P., Wang D., Yu L., Wang C., Wu D.;
"Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at
leading edges polarizes neutrophils.";
J. Cell Sci. 128:992-1000(2015).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[46]
INTERACTION WITH RIPOR1.
PubMed=27807006; DOI=10.1242/jcs.198614;
Mardakheh F.K., Self A., Marshall C.J.;
"RHO binding to FAM65A regulates Golgi reorientation during cell
migration.";
J. Cell Sci. 129:4466-4479(2016).
[47]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=9302995; DOI=10.1038/nsb0997-699;
Wei Y., Zhang Y., Derewenda U., Liu X., Minor W., Nakamoto R.K.,
Somlyo A.V., Somlyo A.P., Derewenda Z.S.;
"Crystal structure of RhoA-GDP and its functional implications.";
Nat. Struct. Biol. 4:699-703(1997).
[48]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-181 OF MUTANT VAL-14.
PubMed=9545299; DOI=10.1074/jbc.273.16.9656;
Ihara K., Muraguchi S., Kato M., Shimizu T., Shirakawa M., Kuroda S.,
Kaibuchi K., Hakoshima T.;
"Crystal structure of human RhoA in a dominantly active form complexed
with a GTP analogue.";
J. Biol. Chem. 273:9656-9666(1998).
[49]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-181 IN COMPLEX WITH PRKCL1.
PubMed=10388627; DOI=10.1006/jsbi.1999.4114;
Maesaki R., Shimizu T., Ihara K., Kuroda S., Kaibuchi K.,
Hakoshima T.;
"Biochemical and crystallographic characterization of a Rho effector
domain of the protein serine/threonine kinase N in a complex with
RhoA.";
J. Struct. Biol. 126:166-170(1999).
[50]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-180 IN COMPLEX WITH GDP.
PubMed=10748207; DOI=10.1074/jbc.M910274199;
Shimizu T., Ihara K., Maesaki R., Kuroda S., Kaibuchi K.,
Hakoshima T.;
"An open conformation of switch I revealed by the crystal structure of
a Mg2+-free form of RHOA complexed with GDP. Implications for the
GDP/GTP exchange mechanism.";
J. Biol. Chem. 275:18311-18317(2000).
[51]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=11927263; DOI=10.1016/S1074-5521(02)00112-6;
Graham D.L., Lowe P.N., Grime G.W., Marsh M., Rittinger K.,
Smerdon S.J., Gamblin S.J., Eccleston J.F.;
"MgF(3)(-) as a transition state analog of phosphoryl transfer.";
Chem. Biol. 9:375-381(2002).
[52]
X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH MCF2.
PubMed=12006984; DOI=10.1038/nsb796;
Snyder J.T., Worthylake D.K., Rossman K.L., Betts L., Pruitt W.M.,
Siderovski D.P., Der C.J., Sondek J.;
"Structural basis for the selective activation of Rho GTPases by Dbl
exchange factors.";
Nat. Struct. Biol. 9:468-475(2002).
[53]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF MUTANT LEU-63 IN COMPLEX WITH
A GTP ANALOG AND MG(2+).
PubMed=12777804; DOI=10.1107/S0907444903005390;
Longenecker K., Read P., Lin S.-K., Somlyo A.P., Nakamoto R.K.,
Derewenda Z.S.;
"Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A
resolution.";
Acta Crystallogr. D 59:876-880(2003).
-!- 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. 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. 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. 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 (By
similarity). Regulates KCNA2 potassium channel activity by
reducing its location at the cell surface in response to CHRM1
activation; promotes KCNA2 endocytosis (PubMed:9635436,
PubMed:19403695). {ECO:0000250, ECO:0000269|PubMed:12900402,
ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794,
ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20937854,
ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519,
ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9635436}.
-!- FUNCTION: (Microbial infection) Serves as a target for the yopT
cysteine peptidase from Yersinia pestis, vector of the plague, and
Yersinia pseudotuberculosis, which causes gastrointestinal
disorders. {ECO:0000269|PubMed:12062101,
ECO:0000269|PubMed:12538863}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12777804};
-!- ENZYME REGULATION: GTP hydrolysis is stimulated by ARHGAP30.
{ECO:0000269|PubMed:21565175}.
-!- SUBUNIT: Interacts with ARHGEF28 (By similarity). Interacts (via
GTP-bound form) with RIPOR1 (via N-terminus); this interaction
links RHOA to STK24 and STK26 kinases (PubMed:27807006). Interacts
with RIPOR2 (via active GTP- or inactive GDP-bound forms) isoform
1 and isoform 2; these interactions are direct, block the loading
of GTP to RHOA and decrease upon chemokine CCL19 stimulation in
primary T lymphocytes (PubMed:25588844). Binds PRKCL1, ROCK1 and
ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts
with PLCE1 and AKAP13. Interacts with DIAPH1 (PubMed:23325789).
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 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. Interacts (GTP-bound
form) with KCNA2 (via cytoplasmic N-terminal domain)
(PubMed:9635436). {ECO:0000250|UniProtKB:P61589,
ECO:0000250|UniProtKB:Q9QUI0, ECO:0000269|PubMed:10066731,
ECO:0000269|PubMed:10388627, ECO:0000269|PubMed:10438814,
ECO:0000269|PubMed:10748207, ECO:0000269|PubMed:10940294,
ECO:0000269|PubMed:11696353, ECO:0000269|PubMed:12006984,
ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12221096,
ECO:0000269|PubMed:12538863, ECO:0000269|PubMed:12777804,
ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:17115030,
ECO:0000269|PubMed:19403695, ECO:0000269|PubMed:20400958,
ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20974804,
ECO:0000269|PubMed:23325789, ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:27807006, ECO:0000269|PubMed:8617235,
ECO:0000269|PubMed:8641286, ECO:0000269|PubMed:9121475,
ECO:0000269|PubMed:9857026, ECO:0000305|PubMed:9635436}.
-!- INTERACTION:
Q15109:AGER; NbExp=2; IntAct=EBI-446668, EBI-1646426;
Q07960:ARHGAP1; NbExp=2; IntAct=EBI-446668, EBI-602762;
P52565:ARHGDIA; NbExp=6; IntAct=EBI-446668, EBI-712693;
O15085:ARHGEF11; NbExp=6; IntAct=EBI-446668, EBI-311099;
Q9NZN5:ARHGEF12; NbExp=2; IntAct=EBI-446668, EBI-821440;
Q8IW93:ARHGEF19; NbExp=2; IntAct=EBI-446668, EBI-7799822;
Q969H4:CNKSR1; NbExp=4; IntAct=EBI-446668, EBI-741671;
Q9Y4D1:DAAM1; NbExp=5; IntAct=EBI-446668, EBI-2817289;
O60610:DIAPH1; NbExp=3; IntAct=EBI-446668, EBI-3959709;
O08808:Diaph1 (xeno); NbExp=3; IntAct=EBI-446668, EBI-1026445;
Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-446668, EBI-747204;
Q6PDM6:Mcf2l (xeno); NbExp=3; IntAct=EBI-446668, EBI-602149;
P19338:NCL; NbExp=3; IntAct=EBI-446668, EBI-346967;
Q9Z0S9:Rabac1 (xeno); NbExp=3; IntAct=EBI-446668, EBI-476965;
Q9Y4F9:RIPOR2; NbExp=4; IntAct=EBI-446668, EBI-2798942;
Q13464:ROCK1; NbExp=4; IntAct=EBI-446668, EBI-876651;
Q9BST9:RTKN; NbExp=5; IntAct=EBI-446668, EBI-446694;
Q8C6B2:Rtkn (xeno); NbExp=3; IntAct=EBI-446668, EBI-1162441;
Q15796:SMAD2; NbExp=2; IntAct=EBI-446668, EBI-1040141;
Q9HCE7-2:SMURF1; NbExp=2; IntAct=EBI-446668, EBI-9845742;
A0A0F6B1Q8:sseJ (xeno); NbExp=7; IntAct=EBI-446668, EBI-10760263;
Q9FD10:sseJ (xeno); NbExp=3; IntAct=EBI-446668, EBI-10690199;
Q15654:TRIP6; NbExp=3; IntAct=EBI-446668, EBI-742327;
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell
cortex {ECO:0000269|PubMed:9635436}. Midbody. Cell projection,
lamellipodium {ECO:0000250}. 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. {ECO:0000250}.
-!- DOMAIN: The basic-rich region is essential for yopT recognition
and cleavage.
-!- PTM: (Microbial infection) Substrate for botulinum ADP-
ribosyltransferase. {ECO:0000269|PubMed:1328215}.
-!- PTM: (Microbial infection) 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. {ECO:0000269|PubMed:12062101,
ECO:0000269|PubMed:12538863}.
-!- PTM: (Microbial infection) 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. {ECO:0000269|PubMed:19039103,
ECO:0000269|PubMed:19362538}.
-!- PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus
asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230
inhibits downstream signaling by an impaired interaction with
diverse regulator and effector proteins of Rho and leads to actin
disassembly. {ECO:0000269|PubMed:24141704}.
-!- PTM: Phosphorylation by PRKG1 at Ser-188 inactivates RHOA
signaling (PubMed:11162591). Phosphorylation by SLK at Ser-188 in
response to AGTR2 activation (By similarity).
{ECO:0000250|UniProtKB:P61589, ECO:0000269|PubMed:11162591}.
-!- PTM: 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. {ECO:0000269|PubMed:19782033}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RHOAID42107ch3p21.html";
-----------------------------------------------------------------------
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EMBL; X05026; CAA28690.1; -; mRNA.
EMBL; L25080; AAC33178.1; -; mRNA.
EMBL; AF498970; AAM21117.1; -; mRNA.
EMBL; BT019870; AAV38673.1; -; mRNA.
EMBL; AK222556; BAD96276.1; -; mRNA.
EMBL; BX647063; CAE46190.1; -; mRNA.
EMBL; AC104452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001360; AAH01360.1; -; mRNA.
EMBL; BC005976; AAH05976.1; -; mRNA.
EMBL; L09159; AAA50612.1; -; mRNA.
EMBL; M83094; AAA67539.1; -; Genomic_DNA.
CCDS; CCDS2795.1; -.
PIR; A26675; TVHU12.
RefSeq; NP_001300870.1; NM_001313941.1.
RefSeq; NP_001655.1; NM_001664.3.
UniGene; Hs.247077; -.
PDB; 1A2B; X-ray; 2.40 A; A=1-181.
PDB; 1CC0; X-ray; 5.00 A; A/C=1-190.
PDB; 1CXZ; X-ray; 2.20 A; A=1-181.
PDB; 1DPF; X-ray; 2.00 A; A=1-180.
PDB; 1FTN; X-ray; 2.10 A; A=1-193.
PDB; 1KMQ; X-ray; 1.55 A; A=4-181.
PDB; 1LB1; X-ray; 2.81 A; B/D/F/H=1-190.
PDB; 1OW3; X-ray; 1.80 A; B=1-193.
PDB; 1S1C; X-ray; 2.60 A; A/B=1-181.
PDB; 1TX4; X-ray; 1.65 A; B=3-179.
PDB; 1X86; X-ray; 3.22 A; B/D/F/H=1-193.
PDB; 1XCG; X-ray; 2.50 A; B/F=3-180.
PDB; 2RGN; X-ray; 3.50 A; C/F=1-193.
PDB; 3KZ1; X-ray; 2.70 A; E/F=1-181.
PDB; 3LW8; X-ray; 1.85 A; A/B/C/D=2-181.
PDB; 3LWN; X-ray; 2.28 A; A/B=2-181.
PDB; 3LXR; X-ray; 1.68 A; A=2-181.
PDB; 3MSX; X-ray; 1.65 A; A=1-180.
PDB; 3T06; X-ray; 2.84 A; B/F=3-180.
PDB; 4D0N; X-ray; 2.10 A; A=1-184.
PDB; 4XH9; X-ray; 2.00 A; B/E=2-180.
PDB; 4XOI; X-ray; 2.09 A; A/C=1-180.
PDB; 4XSG; X-ray; 1.80 A; A=1-179.
PDB; 4XSH; X-ray; 2.50 A; A=1-179.
PDB; 5A0F; X-ray; 2.00 A; A=1-181.
PDB; 5BWM; X-ray; 2.50 A; A=1-179.
PDB; 5C2K; X-ray; 1.42 A; A=1-193.
PDB; 5C4M; X-ray; 1.30 A; A=1-193.
PDB; 5EZ6; X-ray; 1.80 A; B=1-181.
PDB; 5FR1; X-ray; 2.75 A; A=1-193.
PDB; 5FR2; X-ray; 3.35 A; A=1-193.
PDB; 5HPY; X-ray; 2.40 A; B/F=3-181.
PDB; 5IRC; X-ray; 1.72 A; D/F=2-181.
PDB; 5JCP; X-ray; 2.10 A; A/B=1-181.
PDB; 5JHG; X-ray; 2.50 A; B/F=1-181.
PDB; 5JHH; X-ray; 2.30 A; B/F=1-181.
PDB; 5M6X; X-ray; 2.40 A; B/I=2-193.
PDB; 5M70; X-ray; 2.20 A; B/G=2-193.
PDBsum; 1A2B; -.
PDBsum; 1CC0; -.
PDBsum; 1CXZ; -.
PDBsum; 1DPF; -.
PDBsum; 1FTN; -.
PDBsum; 1KMQ; -.
PDBsum; 1LB1; -.
PDBsum; 1OW3; -.
PDBsum; 1S1C; -.
PDBsum; 1TX4; -.
PDBsum; 1X86; -.
PDBsum; 1XCG; -.
PDBsum; 2RGN; -.
PDBsum; 3KZ1; -.
PDBsum; 3LW8; -.
PDBsum; 3LWN; -.
PDBsum; 3LXR; -.
PDBsum; 3MSX; -.
PDBsum; 3T06; -.
PDBsum; 4D0N; -.
PDBsum; 4XH9; -.
PDBsum; 4XOI; -.
PDBsum; 4XSG; -.
PDBsum; 4XSH; -.
PDBsum; 5A0F; -.
PDBsum; 5BWM; -.
PDBsum; 5C2K; -.
PDBsum; 5C4M; -.
PDBsum; 5EZ6; -.
PDBsum; 5FR1; -.
PDBsum; 5FR2; -.
PDBsum; 5HPY; -.
PDBsum; 5IRC; -.
PDBsum; 5JCP; -.
PDBsum; 5JHG; -.
PDBsum; 5JHH; -.
PDBsum; 5M6X; -.
PDBsum; 5M70; -.
ProteinModelPortal; P61586; -.
SMR; P61586; -.
BioGrid; 106880; 171.
CORUM; P61586; -.
DIP; DIP-29642N; -.
IntAct; P61586; 73.
MINT; MINT-4999683; -.
STRING; 9606.ENSP00000400175; -.
BindingDB; P61586; -.
ChEMBL; CHEMBL6052; -.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
iPTMnet; P61586; -.
PhosphoSitePlus; P61586; -.
SwissPalm; P61586; -.
BioMuta; RHOA; -.
DMDM; 47606458; -.
EPD; P61586; -.
MaxQB; P61586; -.
PaxDb; P61586; -.
PeptideAtlas; P61586; -.
PRIDE; P61586; -.
TopDownProteomics; P61586; -.
DNASU; 387; -.
Ensembl; ENST00000418115; ENSP00000400175; ENSG00000067560.
GeneID; 387; -.
KEGG; hsa:387; -.
UCSC; uc003cwu.4; human.
CTD; 387; -.
DisGeNET; 387; -.
EuPathDB; HostDB:ENSG00000067560.10; -.
GeneCards; RHOA; -.
HGNC; HGNC:667; RHOA.
HPA; CAB005052; -.
MIM; 165390; gene.
neXtProt; NX_P61586; -.
OpenTargets; ENSG00000067560; -.
PharmGKB; PA134865095; -.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000119020; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; P61586; -.
KO; K04513; -.
OMA; QKIGARH; -.
OrthoDB; EOG091G0QVS; -.
PhylomeDB; P61586; -.
TreeFam; TF300837; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-198203; PI3K/AKT activation.
Reactome; R-HSA-209563; Axonal growth stimulation.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-4086400; PCP/CE pathway.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5625900; RHO GTPases activate CIT.
Reactome; R-HSA-5625970; RHO GTPases activate KTN1.
Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLink; P61586; -.
SIGNOR; P61586; -.
ChiTaRS; RHOA; human.
EvolutionaryTrace; P61586; -.
GeneWiki; RHOA; -.
GenomeRNAi; 387; -.
PMAP-CutDB; P61586; -.
PRO; PR:P61586; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000067560; -.
CleanEx; HS_RHOA; -.
ExpressionAtlas; P61586; baseline and differential.
Genevisible; P61586; HS.
GO; GO:0043296; C:apical junction complex; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; TAS:Reactome.
GO; GO:0071944; C:cell periphery; IMP:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:SynGO.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IMP:AgBase.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0031982; C:vesicle; IDA:AgBase.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; TAS:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0043297; P:apical junction assembly; IMP:UniProtKB.
GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:1990869; P:cellular response to chemokine; IMP:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0036089; P:cleavage furrow formation; IDA:UniProtKB.
GO; GO:0043542; P:endothelial cell migration; IGI:MGI.
GO; GO:0097498; P:endothelial tube lumen extension; IGI:MGI.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:1903673; P:mitotic cleavage furrow formation; IMP:UniProtKB.
GO; GO:0090307; P:mitotic spindle assembly; IMP:BHF-UCL.
GO; GO:0050919; P:negative chemotaxis; IMP:UniProtKB.
GO; GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IGI:MGI.
GO; GO:0045792; P:negative regulation of cell size; IMP:CAFA.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043931; P:ossification involved in bone maturation; ISS:BHF-UCL.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0050772; P:positive regulation of axonogenesis; TAS:Reactome.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0060193; P:positive regulation of lipase activity; IDA:AgBase.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; NAS:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:MGI.
GO; GO:2000406; P:positive regulation of T cell migration; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; TAS:Reactome.
GO; GO:0033688; P:regulation of osteoblast proliferation; ISS:BHF-UCL.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0035385; P:Roundabout signaling pathway; IDA:UniProtKB.
GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
GO; GO:0061383; P:trabecula morphogenesis; ISS:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Cell cycle; Cell division;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Glycoprotein; GTP-binding;
Host-virus interaction; Lipoprotein; Magnesium; Membrane; Methylation;
Nucleotide-binding; Phosphoprotein; Prenylation; Proto-oncogene;
Reference proteome; Ubl conjugation.
CHAIN 1 190 Transforming protein RhoA.
/FTId=PRO_0000030411.
PROPEP 191 193 Removed in mature form.
/FTId=PRO_0000030412.
NP_BIND 12 19 GTP. {ECO:0000269|PubMed:10748207,
ECO:0000269|PubMed:12777804}.
NP_BIND 59 63 GTP. {ECO:0000250}.
NP_BIND 117 120 GTP. {ECO:0000269|PubMed:10748207,
ECO:0000269|PubMed:12777804}.
MOTIF 34 42 Effector region. {ECO:0000255}.
COMPBIAS 182 187 Arg/Lys-rich (basic).
SITE 189 190 Cleavage; by yopT.
MOD_RES 34 34 O-AMP-tyrosine; by Haemophilus IbpA;
alternate. {ECO:0000269|PubMed:19362538}.
MOD_RES 37 37 O-AMP-threonine; by Vibrio VopS.
{ECO:0000269|PubMed:19039103}.
MOD_RES 41 41 ADP-ribosylasparagine; by botulinum
toxin. {ECO:0000305|PubMed:1328215}.
MOD_RES 188 188 Phosphoserine; by PKG/PRKG1.
{ECO:0000269|PubMed:11162591}.
MOD_RES 190 190 Cysteine methyl ester.
{ECO:0000250|UniProtKB:P62745}.
LIPID 190 190 S-geranylgeranyl cysteine.
{ECO:0000250|UniProtKB:P62745}.
CARBOHYD 34 34 O-linked (GlcNAc) tyrosine; by
Photorhabdus PAU_02230; alternate.
{ECO:0000269|PubMed:24141704}.
MUTAGEN 14 14 G->V: Causes constitutive activation.
{ECO:0000269|PubMed:19948726}.
MUTAGEN 34 34 Y->A: Abolishes interaction with DGKQ.
{ECO:0000269|PubMed:10066731,
ECO:0000269|PubMed:19362538}.
MUTAGEN 34 34 Y->F: Abolishes AMPylation by Haemophilus
IbpA. {ECO:0000269|PubMed:10066731,
ECO:0000269|PubMed:19362538}.
MUTAGEN 63 63 Q->L: Causes constitutive activation.
MUTAGEN 193 193 L->M: Converts geranyl-geranylation to
farnesylation; does not prevent the
cleavage by yopT.
{ECO:0000269|PubMed:12538863}.
CONFLICT 23 23 I -> T (in Ref. 5; BAD96276).
{ECO:0000305}.
STRAND 4 13 {ECO:0000244|PDB:5C4M}.
HELIX 14 16 {ECO:0000244|PDB:4XH9}.
HELIX 18 27 {ECO:0000244|PDB:5C4M}.
STRAND 43 47 {ECO:0000244|PDB:5C4M}.
STRAND 52 58 {ECO:0000244|PDB:5C4M}.
HELIX 63 69 {ECO:0000244|PDB:5C4M}.
HELIX 70 73 {ECO:0000244|PDB:5C4M}.
STRAND 78 85 {ECO:0000244|PDB:5C4M}.
HELIX 89 97 {ECO:0000244|PDB:5C4M}.
HELIX 99 106 {ECO:0000244|PDB:5C4M}.
STRAND 107 109 {ECO:0000244|PDB:5FR2}.
STRAND 112 117 {ECO:0000244|PDB:5C4M}.
HELIX 119 121 {ECO:0000244|PDB:5C4M}.
HELIX 125 132 {ECO:0000244|PDB:5C4M}.
TURN 133 135 {ECO:0000244|PDB:5C4M}.
HELIX 141 151 {ECO:0000244|PDB:5C4M}.
STRAND 154 158 {ECO:0000244|PDB:5C4M}.
TURN 161 163 {ECO:0000244|PDB:5C4M}.
HELIX 167 179 {ECO:0000244|PDB:5C4M}.
STRAND 190 193 {ECO:0000244|PDB:5FR1}.
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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