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 03-AUG-2022, entry version 205.
DE RecName: Full=Transforming protein RhoA {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000269|PubMed:21565175, ECO:0000269|PubMed:23940119};
DE AltName: Full=Rho cDNA clone 12;
DE Short=h12;
DE Flags: Precursor;
GN Name=RHOA {ECO:0000312|HGNC:HGNC:667}; Synonyms=ARH12, ARHA, RHO12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 sequenced by
RT 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 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., 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., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., 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 project:
RT 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, AND
RP ADP-RIBOSYLATION AT ASN-41 (MICROBIAL INFECTION).
RC TISSUE=Platelet;
RX PubMed=1328215; DOI=10.1016/s0021-9258(19)36775-4;
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 PROTEIN SEQUENCE OF 28-51, AND GLYCOSYLATION AT THR-37 (MICROBIAL
RP INFECTION).
RX PubMed=7777059; DOI=10.1038/375500a0;
RA Just I., Selzer J., Wilm M., von Eichel-Streiber C., Mann M., Aktories K.;
RT "Glucosylation of Rho proteins by Clostridium difficile toxin B.";
RL Nature 375:500-503(1995).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-193.
RX PubMed=1556108; DOI=10.1016/s0021-9258(18)42647-6;
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 cytosolic
RT selenium-dependent glutathione peroxidase gene (hgpx1).";
RL J. Biol. Chem. 267:5949-5958(1992).
RN [13]
RP GLYCOSYLATION AT THR-37 (MICROBIAL INFECTION), AND MUTAGENESIS OF THR-37.
RX PubMed=7775453; DOI=10.1074/jbc.270.23.13932;
RA Just I., Wilm M., Selzer J., Rex G., von Eichel-Streiber C., Mann M.,
RA Aktories K.;
RT "The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho
RT proteins.";
RL J. Biol. Chem. 270:13932-13936(1995).
RN [14]
RP INTERACTION WITH ROCK1.
RX PubMed=8617235; DOI=10.1002/j.1460-2075.1996.tb00539.x;
RA Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A., Fujita A.,
RA Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S.;
RT "The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr
RT protein kinase homologous to myotonic dystrophy kinase.";
RL EMBO J. 15:1885-1893(1996).
RN [15]
RP INTERACTION WITH ROCK2.
RX PubMed=8641286; DOI=10.1002/j.1460-2075.1996.tb00574.x;
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 [16]
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., Der C.J.;
RT "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and
RT potential effector of Rho protein signaling.";
RL J. Biol. Chem. 271:28772-28776(1996).
RN [17]
RP GLYCOSYLATION AT THR-37 (MICROBIAL INFECTION), AND MUTAGENESIS OF THR-37.
RX PubMed=8810274; DOI=10.1074/jbc.271.41.25173;
RA Selzer J., Hofmann F., Rex G., Wilm M., Mann M., Just I., Aktories K.;
RT "Clostridium novyi alpha-toxin-catalyzed incorporation of GlcNAc into Rho
RT subfamily proteins.";
RL J. Biol. Chem. 271:25173-25177(1996).
RN [18]
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 GTPases
RT and regulates actin cytoskeletal organization.";
RL Mol. Cell. Biol. 17:2247-2256(1997).
RN [19]
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 potassium
RT channel.";
RL Cell 93:1077-1085(1998).
RN [20]
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 guanine
RT nucleotide exchange factor for Rac and Rho GTPases.";
RL J. Biol. Chem. 273:34954-34960(1998).
RN [21]
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 active
RT RhoA.";
RL J. Biol. Chem. 274:6820-6822(1999).
RN [22]
RP INTERACTION WITH HRSV PROTEIN F (MICROBIAL INFECTION).
RX PubMed=10438814; DOI=10.1128/jvi.73.9.7262-7270.1999;
RA Pastey M.K., Crowe J.E. Jr., Graham B.S.;
RT "RhoA interacts with the fusion glycoprotein of respiratory syncytial virus
RT and facilitates virus-induced syncytium formation.";
RL J. Virol. 73:7262-7270(1999).
RN [23]
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 [24]
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 [25]
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., Klauschenz E.,
RA Hundsrucker C., Maric K., Rosenthal W.;
RT "Ht31: the first protein kinase A anchoring protein to integrate protein
RT kinase A and Rho signaling.";
RL FEBS Lett. 507:264-268(2001).
RN [26]
RP INTERACTION WITH ARHGEF3, AND ACTIVITY REGULATION.
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 [27]
RP INTERACTION WITH YERSINIA PESTIS YOPT (MICROBIAL INFECTION), CLEAVAGE
RP (MICROBIAL INFECTION), 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 family
RT of cysteine proteases functioning in bacterial pathogenesis.";
RL Cell 109:575-588(2002).
RN [28]
RP INTERACTION WITH RAP1GDS1, AND SUBCELLULAR LOCATION.
RX PubMed=12551911; DOI=10.1074/jbc.m211286200;
RA Lanning C.C., Ruiz-Velasco R., Williams C.L.;
RT "Novel mechanism of the co-regulation of nuclear transport of SmgGDS and
RT Rac1.";
RL J. Biol. Chem. 278:12495-12506(2003).
RN [29]
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 [30]
RP INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPT (MICROBIAL INFECTION),
RP CLEAVAGE (MICROBIAL INFECTION), MUTAGENESIS OF LEU-193, AND FUNCTION
RP (MICROBIAL 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 site
RT and recognition elements in Rho GTPases.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:904-909(2003).
RN [31]
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 function of
RT RhoA.";
RL J. Cell Biol. 170:571-582(2005).
RN [32]
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., Miki T.;
RT "Dissecting the role of Rho-mediated signaling in contractile ring
RT formation.";
RL Mol. Biol. Cell 17:43-55(2006).
RN [33]
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 cytokinesis.";
RL Nat. Cell Biol. 8:1432-1440(2006).
RN [34]
RP FUNCTION.
RX PubMed=19934221; DOI=10.1242/jcs.053728;
RA Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L., 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 [35]
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 voltage-
RT sensitive potassium channel.";
RL Mol. Biol. Cell 20:2991-3002(2009).
RN [36]
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., Mendez J.C.,
RA 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 [37]
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 BTB
RT adaptors to control actin cytoskeleton structure and cell movement.";
RL Mol. Cell 35:841-855(2009).
RN [38]
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 and
RT downstream signaling.";
RL Science 323:269-272(2009).
RN [39]
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 [40]
RP INTERACTION WITH RAP1GDS1.
RX PubMed=20709748; DOI=10.1074/jbc.m110.129916;
RA Berg T.J., Gastonguay A.J., Lorimer E.L., Kuhnmuench J.R., Li R.,
RA Fields A.P., Williams C.L.;
RT "Splice variants of SmgGDS control small GTPase prenylation and membrane
RT localization.";
RL J. Biol. Chem. 285:35255-35266(2010).
RN [41]
RP INTERACTION WITH ARHGDIA, AND ACTIVITY REGULATION.
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 RhoGDI1.";
RL Nat. Cell Biol. 12:477-483(2010).
RN [42]
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 [43]
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., Buerckstuemmer T.,
RA 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 [44]
RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
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 and
RT cell adhesion.";
RL Biochem. Biophys. Res. Commun. 409:96-102(2011).
RN [45]
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 of the
RT RhoA/Rho kinase pathway.";
RL Breast Cancer Res. Treat. 126:555-563(2011).
RN [46]
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 bronchial
RT epithelial cells.";
RL Mol. Cell. Biol. 31:81-91(2011).
RN [47]
RP FUNCTION, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=23940119; DOI=10.1083/jcb.201304133;
RA Dubash A.D., Koetsier J.L., Amargo E.V., Najor N.A., Harmon R.M.,
RA Green K.J.;
RT "The GEF Bcr activates RhoA/MAL signaling to promote keratinocyte
RT differentiation via desmoglein-1.";
RL J. Cell Biol. 202:653-666(2013).
RN [48]
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 cells.";
RL Mol. Biol. Cell 24:848-857(2013).
RN [49]
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 deamidation
RT of Gq and Gi proteins.";
RL Nat. Struct. Mol. Biol. 20:1273-1280(2013).
RN [50]
RP GLYCOSYLATION AT THR-37 (MICROBIAL INFECTION).
RX PubMed=24905543; DOI=10.1111/cmi.12321;
RA Genth H., Pauillac S., Schelle I., Bouvet P., Bouchier C.,
RA Varela-Chavez C., Just I., Popoff M.R.;
RT "Haemorrhagic toxin and lethal toxin from Clostridium sordellii strain
RT vpi9048: molecular characterization and comparative analysis of substrate
RT specificity of the large clostridial glucosylating toxins.";
RL Cell. Microbiol. 16:1706-1721(2014).
RN [51]
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 [52]
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., Ayoub D.,
RA 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 [53]
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 [54]
RP INTERACTION WITH RAP1GDS1.
RX PubMed=28630045; DOI=10.1074/jbc.m117.792556;
RA Shimizu H., Toma-Fukai S., Saijo S., Shimizu N., Kontani K., Katada T.,
RA Shimizu T.;
RT "Structure-based analysis of the guanine nucleotide exchange factor SmgGDS
RT reveals armadillo-repeat motifs and key regions for activity and GTPase
RT binding.";
RL J. Biol. Chem. 292:13441-13448(2017).
RN [55]
RP FUNCTION, AND INTERACTION WITH ECT2.
RX PubMed=31888991; DOI=10.1073/pnas.1913054117;
RA Chen M., Pan H., Sun L., Shi P., Zhang Y., Li L., Huang Y., Chen J.,
RA Jiang P., Fang X., Wu C., Chen Z.;
RT "Structure and regulation of human epithelial cell transforming 2
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:1027-1035(2020).
RN [56]
RP INVOLVEMENT IN EDFAOB, VARIANTS EDFAOB LYS-47 AND SER-71, CHARACTERIZATION
RP OF VARIANTS EDFAOB LYS-47 AND SER-71, FUNCTION, AND MUTAGENESIS OF GLY-14
RP AND THR-19.
RX PubMed=31570889; DOI=10.1038/s41588-019-0498-4;
RA Vabres P., Sorlin A., Kholmanskikh S.S., Demeer B., St-Onge J.,
RA Duffourd Y., Kuentz P., Courcet J.B., Carmignac V., Garret P., Bessis D.,
RA Boute O., Bron A., Captier G., Carmi E., Devauchelle B., Genevieve D.,
RA Gondry-Jouet C., Guibaud L., Lafon A., Mathieu-Dramard M., Thevenon J.,
RA Dobyns W.B., Bernard G., Polubothu S., Faravelli F., Kinsler V.A.,
RA Thauvin C., Faivre L., Ross M.E., Riviere J.B.;
RT "Postzygotic inactivating mutations of RHOA cause a mosaic neuroectodermal
RT syndrome.";
RL Nat. Genet. 51:1438-1441(2019).
RN [57]
RP STEAROYLATION AT LYS-185; LYS-186 AND LYS-187 (MICROBIAL INFECTION), AND
RP MUTAGENESIS OF 185-LYS--LYS-187.
RX PubMed=30061757; DOI=10.1038/s41564-018-0215-6;
RA Liu W., Zhou Y., Peng T., Zhou P., Ding X., Li Z., Zhong H., Xu Y.,
RA Chen S., Hang H.C., Shao F.;
RT "Nepsilon-fatty acylation of multiple membrane-associated proteins by
RT Shigella IcsB effector to modulate host function.";
RL Nat. Microbiol. 3:996-1009(2018).
RN [58]
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 [59]
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 with
RT a GTP analogue.";
RL J. Biol. Chem. 273:9656-9666(1998).
RN [60]
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., Hakoshima T.;
RT "Biochemical and crystallographic characterization of a Rho effector domain
RT of the protein serine/threonine kinase N in a complex with RhoA.";
RL J. Struct. Biol. 126:166-170(1999).
RN [61]
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., Hakoshima T.;
RT "An open conformation of switch I revealed by the crystal structure of a
RT Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP
RT exchange mechanism.";
RL J. Biol. Chem. 275:18311-18317(2000).
RN [62]
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., Smerdon S.J.,
RA 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 [63]
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 [64]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF MUTANT LEU-63 IN COMPLEX WITH A
RP 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).
RN [65] {ECO:0007744|PDB:5ZHX}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH RAP1GDS1 ISOFORM 2,
RP AND INTERACTION WITH RAP1GDS1.
RX PubMed=30190425; DOI=10.1073/pnas.1804740115;
RA Shimizu H., Toma-Fukai S., Kontani K., Katada T., Shimizu T.;
RT "GEF mechanism revealed by the structure of SmgGDS-558 and farnesylated
RT RhoA complex and its implication for a chaperone mechanism.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:9563-9568(2018).
CC -!- FUNCTION: Small GTPase which cycles between an active GTP-bound and an
CC inactive GDP-bound state. Mainly associated with cytoskeleton
CC organization, in active state binds to a variety of effector proteins
CC to regulate cellular responses such as cytoskeletal dynamics, cell
CC migration and cell cycle. Regulates a signal transduction pathway
CC linking plasma membrane receptors to the assembly of focal adhesions
CC and actin stress fibers (PubMed:8910519, PubMed:9121475,
CC PubMed:31570889). Involved in a microtubule-dependent signal that is
CC required for the myosin contractile ring formation during cell cycle
CC cytokinesis (PubMed:16236794, PubMed:12900402). Plays an essential role
CC in cleavage furrow formation. Required for the apical junction
CC formation of keratinocyte cell-cell adhesion (PubMed:20974804,
CC PubMed:23940119). Essential for the SPATA13-mediated regulation of cell
CC migration and adhesion assembly and disassembly (PubMed:19934221). The
CC MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-
CC dependent stabilization of microtubules at the cell cortex. It controls
CC the localization of APC and CLASP2 to the cell membrane, via the
CC regulation of GSK3B activity. In turn, membrane-bound APC allows the
CC localization of the MACF1 to the cell membrane, which is required for
CC microtubule capture and stabilization (PubMed:20937854). Regulates
CC KCNA2 potassium channel activity by reducing its location at the cell
CC surface in response to CHRM1 activation; promotes KCNA2 endocytosis
CC (PubMed:9635436, PubMed:19403695). Acts as an allosteric activator of
CC guanine nucleotide exchange factor ECT2 by binding in its activated
CC GTP-bound form to the PH domain of ECT2 which stimulates the release of
CC PH inhibition and promotes the binding of substrate RHOA to the ECT2
CC catalytic center (PubMed:31888991). May be an activator of PLCE1
CC (PubMed:16103226). In neurons, involved in the inhibition of the
CC initial spine growth. Upon activation by CaMKII, modulates dendritic
CC spine structural plasticity by relaying CaMKII transient activation to
CC synapse-specific, long-term signaling (By similarity). Acts as a
CC regulator of platelet alpha-granule release during activation and
CC aggregation of platelets (By similarity).
CC {ECO:0000250|UniProtKB:P61589, ECO:0000250|UniProtKB:Q9QUI0,
CC ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:16103226,
CC ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:19403695,
CC ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20937854,
CC ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:23940119,
CC ECO:0000269|PubMed:31570889, ECO:0000269|PubMed:31888991,
CC ECO:0000269|PubMed:8910519, ECO:0000269|PubMed:9121475,
CC 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 -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:21565175, ECO:0000269|PubMed:23940119};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:21565175, ECO:0000305|PubMed:23940119};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12777804};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. Activated by GEFs such as ARHGEF2, ARHGEF3,
CC ARHGEF28 and BCR (PubMed:23940119, PubMed:12221096). Inhibited by GAPs
CC such as ARHGAP30 (PubMed:21565175). Inhibited by GDP dissociation
CC inhibitors such as ARHGDIA (PubMed:20400958).
CC {ECO:0000269|PubMed:12221096, ECO:0000269|PubMed:20400958,
CC ECO:0000269|PubMed:21565175, ECO:0000269|PubMed:23940119}.
CC -!- SUBUNIT: Interacts with ARHGEF28 (By similarity). Interacts (via GTP-
CC bound form) with RIPOR1 (via N-terminus); this interaction links RHOA
CC to STK24 and STK26 kinases (PubMed:27807006). Interacts with RIPOR2
CC (via active GTP- or inactive GDP-bound forms) isoform 1 and isoform 2;
CC these interactions are direct, block the loading of GTP to RHOA and
CC decrease upon chemokine CCL19 stimulation in primary T lymphocytes
CC (PubMed:25588844). Binds PRKCL1, ROCK1 and ROCK2 (PubMed:10388627,
CC PubMed:8617235, PubMed:8641286). Interacts with ARHGEF2, ARHGEF3, NET1
CC and RTKN (PubMed:10940294, PubMed:12221096, PubMed:9857026). Interacts
CC with PLCE1 and AKAP13 (PubMed:11696353, PubMed:12900402). Interacts
CC with DIAPH1 (PubMed:23325789). Interacts (in the constitutively
CC activated, GTP-bound form) with DGKQ (PubMed:10066731). Interacts with
CC RACK1; enhances RHOA activation (PubMed:20499158). Interacts with PKP4;
CC the interaction is detected at the midbody (PubMed:17115030). Interacts
CC (GTP-bound form preferentially) with PKN2; the interaction stimulates
CC autophosphorylation and phosphorylation of PKN2 (PubMed:20974804,
CC PubMed:9121475). Interacts with ARHGDIA; this interaction inactivates
CC and stabilizes RHOA (PubMed:20400958). Interacts with ARHGDIB.
CC Interacts (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal
CC domain) (PubMed:9635436). Interacts (GTP-bound form) with ECT2; the
CC interaction results in allosteric activation of ECT2 (PubMed:31888991).
CC Interacts with RAP1GDS1; the interaction is direct and in a 1:1
CC stoichiometry (PubMed:28630045, PubMed:30190425, PubMed:20709748,
CC PubMed:12551911). {ECO:0000250|UniProtKB:Q9QUI0,
CC ECO:0000269|PubMed:10066731, ECO:0000269|PubMed:10388627,
CC ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:11696353,
CC ECO:0000269|PubMed:12221096, ECO:0000269|PubMed:12551911,
CC ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:17115030,
CC ECO:0000269|PubMed:20400958, ECO:0000269|PubMed:20499158,
CC ECO:0000269|PubMed:20709748, ECO:0000269|PubMed:20974804,
CC ECO:0000269|PubMed:25588844, ECO:0000269|PubMed:27807006,
CC ECO:0000269|PubMed:28630045, ECO:0000269|PubMed:30190425,
CC ECO:0000269|PubMed:31888991, 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 yopT from Yersinia
CC pestis. {ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12538863}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human respiratory
CC syncytial virus (HRSV) protein F; this interaction facilitates virus-
CC induced syncytium formation. {ECO:0000269|PubMed:10438814}.
CC -!- INTERACTION:
CC P61586; Q15109: AGER; NbExp=2; IntAct=EBI-446668, EBI-1646426;
CC P61586; Q7Z6G8-3: ANKS1B; NbExp=3; IntAct=EBI-446668, EBI-17714371;
CC P61586; P05067: APP; NbExp=3; IntAct=EBI-446668, EBI-77613;
CC P61586; Q07960: ARHGAP1; NbExp=3; IntAct=EBI-446668, EBI-602762;
CC P61586; P52565: ARHGDIA; NbExp=5; IntAct=EBI-446668, EBI-712693;
CC P61586; O15085: ARHGEF11; NbExp=9; IntAct=EBI-446668, EBI-311099;
CC P61586; Q9NZN5: ARHGEF12; NbExp=2; IntAct=EBI-446668, EBI-821440;
CC P61586; Q8IW93: ARHGEF19; NbExp=2; IntAct=EBI-446668, EBI-7799822;
CC P61586; Q92974: ARHGEF2; NbExp=3; IntAct=EBI-446668, EBI-302405;
CC P61586; P46527: CDKN1B; NbExp=3; IntAct=EBI-446668, EBI-519280;
CC P61586; Q9Y4D1: DAAM1; NbExp=5; IntAct=EBI-446668, EBI-2817289;
CC P61586; O60610: DIAPH1; NbExp=3; IntAct=EBI-446668, EBI-3959709;
CC P61586; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-446668, EBI-747204;
CC P61586; P19338: NCL; NbExp=3; IntAct=EBI-446668, EBI-346967;
CC P61586; Q9Y4F9: RIPOR2; NbExp=4; IntAct=EBI-446668, EBI-2798942;
CC P61586; Q9Y4F9-2: RIPOR2; NbExp=3; IntAct=EBI-446668, EBI-14509742;
CC P61586; Q96MK2: RIPOR3; NbExp=3; IntAct=EBI-446668, EBI-12010512;
CC P61586; Q13464: ROCK1; NbExp=4; IntAct=EBI-446668, EBI-876651;
CC P61586; Q9BST9: RTKN; NbExp=6; IntAct=EBI-446668, EBI-446694;
CC P61586; Q15796: SMAD2; NbExp=2; IntAct=EBI-446668, EBI-1040141;
CC P61586; Q9HCE7-2: SMURF1; NbExp=2; IntAct=EBI-446668, EBI-9845742;
CC P61586; Q15654: TRIP6; NbExp=3; IntAct=EBI-446668, EBI-742327;
CC P61586; O08808: Diaph1; Xeno; NbExp=3; IntAct=EBI-446668, EBI-1026445;
CC P61586; Q6PDM6: Mcf2l; Xeno; NbExp=3; IntAct=EBI-446668, EBI-602149;
CC P61586; Q9Z0S9: Rabac1; Xeno; NbExp=2; IntAct=EBI-446668, EBI-476965;
CC P61586; Q8C6B2: Rtkn; Xeno; NbExp=4; IntAct=EBI-446668, EBI-1162441;
CC P61586; A0A0F6B1Q8: sseJ; Xeno; NbExp=10; IntAct=EBI-446668, EBI-10760263;
CC P61586; Q9FD10: sseJ; Xeno; NbExp=3; IntAct=EBI-446668, EBI-10690199;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side.
CC Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:9635436}. Midbody. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q9QUI0}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9QUI0}. Nucleus {ECO:0000269|PubMed:12551911}.
CC Note=Localized to cell-cell contacts in calcium-treated keratinocytes
CC (By similarity). Translocates to the equatorial region before furrow
CC formation in a ECT2-dependent manner. Localizes to the equatorial cell
CC cortex (at the site of the presumptive furrow) in early anaphase in an
CC activated form and in a myosin- and actin-independent manner.
CC {ECO:0000250|UniProtKB:Q9QUI0}.
CC -!- DOMAIN: (Microbial infection) The basic-rich region is essential for
CC yopT recognition and cleavage. {ECO:0000269|PubMed:12062101,
CC ECO:0000269|PubMed:12538863}.
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 is
CC infected by some Yersinia pathogens. This removes the lipid attachment,
CC and leads to its displacement from plasma membrane and to subsequent
CC cytoskeleton cleavage. {ECO:0000269|PubMed:12062101,
CC ECO:0000269|PubMed:12538863}.
CC -!- PTM: (Microbial infection) AMPylation at Tyr-34 and Thr-37 are mediated
CC by bacterial enzymes in case of infection by H.somnus and
CC V.parahaemolyticus, respectively. AMPylation occurs in the effector
CC region and leads to inactivation of the GTPase activity by preventing
CC the interaction with downstream effectors, thereby inhibiting actin
CC assembly in infected cells. It is unclear whether some human enzyme
CC mediates AMPylation; FICD has such ability in vitro but additional
CC experiments remain to be done to confirm results in vivo.
CC {ECO:0000269|PubMed:19039103, 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 inhibits
CC downstream signaling by an impaired interaction with diverse regulator
CC and effector proteins of Rho and leads to actin disassembly.
CC {ECO:0000269|PubMed:24141704}.
CC -!- PTM: (Microbial infection) Glucosylated at Thr-37 by C.difficile toxins
CC TcdA and TcdB in the colonic epithelium (PubMed:7777059,
CC PubMed:7775453, PubMed:24905543). Monoglucosylation completely prevents
CC the recognition of the downstream effector, blocking the GTPases in
CC their inactive form, leading to actin cytoskeleton disruption and cell
CC death, resulting in the loss of colonic epithelial barrier function
CC (PubMed:7777059, PubMed:7775453). {ECO:0000269|PubMed:24905543,
CC ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059}.
CC -!- PTM: (Microbial infection) Glycosylated (O-GlcNAcylated) at Thr-37 by
CC C.novyi toxin TcdA (PubMed:8810274). O-GlcNAcylation completely
CC prevents the recognition of the downstream effector, blocking the
CC GTPases in their inactive form, leading to actin cytoskeleton
CC disruption (PubMed:8810274). {ECO:0000269|PubMed:8810274}.
CC -!- PTM: (Microbial infection) Stearoylated By S.flexneri N-epsilon-fatty
CC acyltransferase IcsB, thereby disrupting the host actin cytoskeleton.
CC {ECO:0000269|PubMed:30061757}.
CC -!- PTM: Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling
CC (PubMed:11162591). Phosphorylation by SLK at Ser-188 in response to
CC AGTR2 activation (By similarity). {ECO:0000250|UniProtKB:P61589,
CC ECO:0000269|PubMed:11162591}.
CC -!- PTM: Ubiquitinated by the BCR(KCTD13) and BCR(TNFAIP1) E3 ubiquitin
CC ligase complexes, leading to its degradation by the proteasome, thereby
CC regulating the actin cytoskeleton and synaptic transmission in neurons.
CC {ECO:0000269|PubMed:19782033}.
CC -!- PTM: Serotonylation of Gln-63 by TGM2 during activation and aggregation
CC of platelets leads to constitutive activation of GTPase activity.
CC {ECO:0000250|UniProtKB:Q9QUI0}.
CC -!- DISEASE: Ectodermal dysplasia with facial dysmorphism and acral,
CC ocular, and brain anomalies (EDFAOB) [MIM:618727]: A neuroectodermal
CC syndrome characterized by linear hypopigmentation, alopecia, apparently
CC asymptomatic leukoencephalopathy, and facial, ocular, dental and acral
CC anomalies. Patients show no intellectual or neurologic impairment.
CC {ECO:0000269|PubMed:31570889}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RHOAID42107ch3p21.html";
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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 PDB; 6KX2; X-ray; 1.45 A; A=1-181.
DR PDB; 6KX3; X-ray; 1.98 A; A=1-181.
DR PDB; 6R3V; X-ray; 1.75 A; B=1-193.
DR PDB; 6V6M; X-ray; 1.39 A; A=1-181.
DR PDB; 6V6U; X-ray; 1.16 A; A=1-181.
DR PDB; 6V6V; X-ray; 1.40 A; A=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 PDBsum; 6KX2; -.
DR PDBsum; 6KX3; -.
DR PDBsum; 6R3V; -.
DR PDBsum; 6V6M; -.
DR PDBsum; 6V6U; -.
DR PDBsum; 6V6V; -.
DR AlphaFoldDB; P61586; -.
DR BMRB; P61586; -.
DR SMR; P61586; -.
DR BioGRID; 106880; 1225.
DR CORUM; P61586; -.
DR DIP; DIP-29642N; -.
DR IntAct; P61586; 176.
DR MINT; P61586; -.
DR STRING; 9606.ENSP00000400175; -.
DR BindingDB; P61586; -.
DR ChEMBL; CHEMBL6052; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR GlyGen; P61586; 1 site.
DR iPTMnet; P61586; -.
DR MetOSite; P61586; -.
DR PhosphoSitePlus; P61586; -.
DR SwissPalm; P61586; -.
DR BioMuta; RHOA; -.
DR DMDM; 47606458; -.
DR EPD; P61586; -.
DR jPOST; P61586; -.
DR MassIVE; P61586; -.
DR MaxQB; P61586; -.
DR PaxDb; P61586; -.
DR PeptideAtlas; P61586; -.
DR PRIDE; P61586; -.
DR ProteomicsDB; 57321; -.
DR TopDownProteomics; P61586; -.
DR Antibodypedia; 30508; 712 antibodies from 39 providers.
DR DNASU; 387; -.
DR Ensembl; ENST00000418115.6; ENSP00000400175.1; ENSG00000067560.14.
DR Ensembl; ENST00000445425.6; ENSP00000408402.3; ENSG00000067560.14.
DR Ensembl; ENST00000678200.1; ENSP00000504180.1; ENSG00000067560.14.
DR Ensembl; ENST00000679208.1; ENSP00000503282.1; ENSG00000067560.14.
DR GeneID; 387; -.
DR KEGG; hsa:387; -.
DR MANE-Select; ENST00000418115.6; ENSP00000400175.1; NM_001664.4; NP_001655.1.
DR UCSC; uc003cwu.4; human.
DR CTD; 387; -.
DR DisGeNET; 387; -.
DR GeneCards; RHOA; -.
DR HGNC; HGNC:667; RHOA.
DR HPA; ENSG00000067560; Low tissue specificity.
DR MalaCards; RHOA; -.
DR MIM; 165390; gene.
DR MIM; 618727; phenotype.
DR neXtProt; NX_P61586; -.
DR OpenTargets; ENSG00000067560; -.
DR Orphanet; 589608; Linear hypopigmentation and craniofacial asymmetry with acral, ocular and brain anomalies.
DR PharmGKB; PA134865095; -.
DR VEuPathDB; HostDB:ENSG00000067560; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00950000182945; -.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; P61586; -.
DR OMA; RWIPEIK; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; P61586; -.
DR TreeFam; TF300837; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P61586; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
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-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR SABIO-RK; P61586; -.
DR SignaLink; P61586; -.
DR SIGNOR; P61586; -.
DR BioGRID-ORCS; 387; 266 hits in 1099 CRISPR screens.
DR ChiTaRS; RHOA; human.
DR EvolutionaryTrace; P61586; -.
DR GeneWiki; RHOA; -.
DR GenomeRNAi; 387; -.
DR Pharos; P61586; Tbio.
DR PRO; PR:P61586; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P61586; protein.
DR Bgee; ENSG00000067560; Expressed in monocyte and 212 other tissues.
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:0030054; C:cell junction; TAS:Reactome.
DR GO; GO:0071944; C:cell periphery; IMP:UniProtKB.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0003925; F:G protein activity; IEA:UniProtKB-EC.
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: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:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP: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:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0021861; P:forebrain radial glial cell differentiation; IEA:Ensembl.
DR GO; GO:0046039; P:GTP metabolic process; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; 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:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0050919; P:negative chemotaxis; IMP:UniProtKB.
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:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; 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:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0043931; P:ossification involved in bone maturation; ISS:BHF-UCL.
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: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 associated smooth muscle contraction; IEA:Ensembl.
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: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; IMP: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: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:0009410; P:response to xenobiotic 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:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0061383; P:trabecula morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00274; -.
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 PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cell cycle; Cell division; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Disease variant; Ectodermal dysplasia; Glycoprotein; GTP-binding;
KW Host-virus interaction; Hydrolase; Lipoprotein; Magnesium; Membrane;
KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; Prenylation;
KW Proto-oncogene; Reference proteome; Ubl conjugation.
FT CHAIN 1..190
FT /note="Transforming protein RhoA"
FT /id="PRO_0000030411"
FT PROPEP 191..193
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT /id="PRO_0000030412"
FT REGION 61..78
FT /note="Switch II region; involved in RAP1GDS1 isoform 2
FT binding"
FT /evidence="ECO:0000269|PubMed:30190425,
FT ECO:0007744|PDB:5ZHX"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:10748207,
FT ECO:0000269|PubMed:12777804"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:10748207,
FT ECO:0000269|PubMed:12777804"
FT BINDING 160..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT SITE 189..190
FT /note="(Microbial infection) Cleavage; by yopT"
FT /evidence="ECO:0000269|PubMed:12062101,
FT ECO:0000269|PubMed:12538863"
FT MOD_RES 34
FT /note="(Microbial infection) O-AMP-tyrosine; by Haemophilus
FT IbpA; alternate"
FT /evidence="ECO:0000269|PubMed:19362538"
FT MOD_RES 37
FT /note="(Microbial infection) O-AMP-threonine; by Vibrio
FT VopS"
FT /evidence="ECO:0000269|PubMed:19039103"
FT MOD_RES 41
FT /note="(Microbial infection) ADP-ribosylasparagine; by
FT botulinum toxin"
FT /evidence="ECO:0000305|PubMed:1328215"
FT MOD_RES 63
FT /note="5-glutamyl serotonin"
FT /evidence="ECO:0000250|UniProtKB:Q9QUI0"
FT MOD_RES 188
FT /note="Phosphoserine; by PKG/PRKG1"
FT /evidence="ECO:0000269|PubMed:11162591"
FT MOD_RES 190
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT LIPID 185
FT /note="(Microbial infection) N6-stearoyl lysine"
FT /evidence="ECO:0000269|PubMed:30061757"
FT LIPID 186
FT /note="(Microbial infection) N6-stearoyl lysine"
FT /evidence="ECO:0000269|PubMed:30061757"
FT LIPID 187
FT /note="(Microbial infection) N6-stearoyl lysine"
FT /evidence="ECO:0000269|PubMed:30061757"
FT LIPID 190
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT CARBOHYD 34
FT /note="(Microbial infection) O-linked (GlcNAc) tyrosine; by
FT Photorhabdus PAU_02230; alternate"
FT /evidence="ECO:0000269|PubMed:24141704"
FT CARBOHYD 37
FT /note="(Microbial infection) O-alpha-linked (GlcNAc)
FT threonine; by C.novyi toxin TcdA; alternate"
FT /evidence="ECO:0000269|PubMed:8810274"
FT CARBOHYD 37
FT /note="(Microbial infection) O-linked (Glc) threonine; by
FT C.difficile toxins TcdA and TcdB; alternate"
FT /evidence="ECO:0000269|PubMed:24905543,
FT ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059"
FT VARIANT 47
FT /note="E -> K (in EDFAOB; somatic mosaic variant; decreased
FT Rho protein signal transduction; decreased substrate
FT adhesion-dependent cell spreading; decreased number of
FT stress fibers assembly; decreased cytoplasmic microtubule
FT organization)"
FT /evidence="ECO:0000269|PubMed:31570889"
FT /id="VAR_083545"
FT VARIANT 71
FT /note="P -> S (in EDFAOB; somatic mosaic variant; decreased
FT Rho protein signal transduction; decreased substrate
FT adhesion-dependent cell spreading; decreased stress fibers
FT assembly; decreased cytoplasmic microtubule organization)"
FT /evidence="ECO:0000269|PubMed:31570889"
FT /id="VAR_083546"
FT MUTAGEN 14
FT /note="G->V: Increased Rho protein signal transduction.
FT Constitutively active."
FT /evidence="ECO:0000269|PubMed:19948726,
FT ECO:0000269|PubMed:31570889"
FT MUTAGEN 19
FT /note="T->N: Decreased Rho protein signal transduction.
FT Decreased substrate adhesion-dependent cell spreading.
FT Decreased stress fibers assembly. Decreased cytoplasmic
FT microtubule organization."
FT /evidence="ECO:0000269|PubMed:31570889"
FT MUTAGEN 34
FT /note="Y->A: Abolishes interaction with DGKQ."
FT /evidence="ECO:0000269|PubMed:10066731,
FT ECO:0000269|PubMed:19362538"
FT MUTAGEN 34
FT /note="Y->F: Abolishes AMPylation by Haemophilus IbpA."
FT /evidence="ECO:0000269|PubMed:10066731,
FT ECO:0000269|PubMed:19362538"
FT MUTAGEN 37
FT /note="T->A: Abolished monoglucosylation by C.difficile
FT toxin TcdA. Abolished O-GlcNAcylation by C.novyi toxin
FT TcdA."
FT /evidence="ECO:0000269|PubMed:7775453,
FT ECO:0000269|PubMed:8810274"
FT MUTAGEN 63
FT /note="Q->L: Causes constitutive activation."
FT MUTAGEN 185..187
FT /note="KKK->RRR: In 3KR mutant; abolished stearoylation in
FT response to S.flexneri infection."
FT /evidence="ECO:0000269|PubMed:30061757"
FT MUTAGEN 193
FT /note="L->M: Converts geranyl-geranylation to
FT farnesylation; does not prevent the cleavage by yopT."
FT /evidence="ECO:0000269|PubMed:12538863"
FT CONFLICT 23
FT /note="I -> T (in Ref. 5; BAD96276)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:6V6U"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:4XH9"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:6V6U"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6V6U"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:6V6U"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:6V6U"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6V6U"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:6V6U"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6V6U"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:6V6U"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:6V6U"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5FR2"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6V6U"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:6V6U"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:6V6U"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6V6U"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:6V6U"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:6V6U"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6V6U"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:6V6U"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:5ZHX"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5ZHX"
FT STRAND 190..193
FT /evidence="ECO:0007829|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
