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 27-MAR-2024, entry version 214. 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 FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-135, AND UBIQUITINATION RP AT LYS-135. RX PubMed=23871831; DOI=10.1016/j.bbamcr.2013.07.005; RA Wei J., Mialki R.K., Dong S., Khoo A., Mallampalli R.K., Zhao Y., Zhao J.; RT "A new mechanism of RhoA ubiquitination and degradation: roles of RT SCF(FBXL19) E3 ligase and Erk2."; RL Biochim. Biophys. Acta 1833:2757-2764(2013). RN [51] 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 [52] 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 [53] 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 [54] 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 [55] 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 [56] 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 [57] 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 [58] 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 [59] 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 [60] 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 [61] 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 [62] 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 [63] 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 [64] 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 [65] 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 [66] {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 (PubMed:23871831). Regulates a signal CC transduction pathway linking plasma membrane receptors to the assembly CC of focal adhesions and actin stress fibers (PubMed:8910519, CC PubMed:9121475, PubMed:31570889). Involved in a microtubule-dependent CC signal that is required for the myosin contractile ring formation CC during cell cycle cytokinesis (PubMed:16236794, PubMed:12900402). Plays CC an essential role in cleavage furrow formation. Required for the apical CC junction 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:23871831, CC ECO:0000269|PubMed:23940119, ECO:0000269|PubMed:31570889, CC ECO:0000269|PubMed:31888991, ECO:0000269|PubMed:8910519, CC ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9635436}. CC -!- FUNCTION: (Microbial infection) Serves as a target for the yopT CC cysteine peptidase from Yersinia pestis, vector of the plague. CC {ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12538863}. CC -!- 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=11; IntAct=EBI-446668, EBI-311099; CC P61586; Q9NZN5: ARHGEF12; NbExp=3; IntAct=EBI-446668, EBI-821440; CC P61586; Q8IW93: ARHGEF19; NbExp=2; IntAct=EBI-446668, EBI-7799822; CC P61586; Q92974: ARHGEF2; NbExp=4; IntAct=EBI-446668, EBI-302405; CC P61586; Q12774: ARHGEF5; NbExp=2; IntAct=EBI-446668, EBI-602199; CC P61586; P46527: CDKN1B; NbExp=3; IntAct=EBI-446668, EBI-519280; CC P61586; Q9Y4D1: DAAM1; NbExp=8; 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=9; 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 Cytoplasm {ECO:0000269|PubMed:23871831}. Note=Localized to cell-cell CC contacts in calcium-treated keratinocytes (By similarity). Translocates CC to the equatorial region before furrow formation in a ECT2-dependent CC manner. Localizes to the equatorial cell cortex (at the site of the CC presumptive furrow) in early anaphase in an activated form and in a CC myosin- and actin-independent manner. {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 (PubMed:19782033). Ubiquitinated at Lys-135 in a FBXL19-mediated CC manner; leading to proteasomal degradation (PubMed:23871831). CC {ECO:0000269|PubMed:19782033, ECO:0000269|PubMed:23871831}. 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="https://atlasgeneticsoncology.org/gene/42107/RHOA"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7G80; X-ray; 1.67 A; A=1-184. DR PDB; 7G81; X-ray; 1.51 A; A=1-184. DR PDB; 7G82; X-ray; 1.41 A; A=1-184. DR PDB; 7G83; X-ray; 1.31 A; A=1-184. DR PDB; 7G84; X-ray; 1.81 A; A=1-184. DR PDB; 7G85; X-ray; 1.74 A; A=1-184. DR PDB; 7G86; X-ray; 1.70 A; A=1-184. DR PDB; 7G87; X-ray; 2.05 A; A=1-184. DR PDB; 7G88; X-ray; 1.87 A; A=1-184. DR PDB; 7G89; X-ray; 1.90 A; A=1-184. DR PDB; 7G8A; X-ray; 1.50 A; A=1-184. DR PDB; 7G8B; X-ray; 1.42 A; A=1-184. DR PDB; 7G8C; X-ray; 2.18 A; A=1-184. DR PDB; 7G8D; X-ray; 1.94 A; A=1-184. DR PDB; 7G8E; X-ray; 1.79 A; A=1-184. DR PDB; 7G8F; X-ray; 1.42 A; A=1-184. DR PDB; 7G8G; X-ray; 1.92 A; A=1-184. DR PDB; 7G8H; X-ray; 1.67 A; A=1-184. DR PDB; 7G8I; X-ray; 2.47 A; A=1-184. DR PDB; 7G8J; X-ray; 1.99 A; A=1-184. DR PDB; 7G8K; X-ray; 1.49 A; A=1-184. DR PDB; 7G8L; X-ray; 1.60 A; A=1-184. DR PDB; 7G8M; X-ray; 2.03 A; A=1-184. DR PDB; 7G8N; X-ray; 2.32 A; A=1-184. DR PDB; 7G8O; X-ray; 1.58 A; A=1-184. DR PDB; 7G8P; X-ray; 2.21 A; A=1-184. DR PDB; 7G8Q; X-ray; 1.56 A; A=1-184. DR PDB; 7G8R; X-ray; 1.44 A; A=1-184. DR PDB; 7G8S; X-ray; 1.60 A; A=1-184. DR PDB; 7G8T; X-ray; 1.39 A; A=1-184. DR PDB; 7G8U; X-ray; 2.44 A; A=1-184. DR PDB; 7G8V; X-ray; 1.45 A; A=1-184. DR PDB; 7G8W; X-ray; 1.94 A; A=1-184. DR PDB; 7G8X; X-ray; 1.71 A; A=1-184. DR PDB; 7G8Y; X-ray; 1.75 A; A=1-184. DR PDB; 7G8Z; X-ray; 1.51 A; A=1-184. DR PDB; 7G90; X-ray; 1.91 A; A=1-184. DR PDB; 7G91; X-ray; 2.29 A; A=1-184. DR PDB; 7G92; X-ray; 1.87 A; A=1-184. DR PDB; 7G93; X-ray; 1.69 A; A=1-184. DR PDB; 7G94; X-ray; 1.47 A; A=1-184. DR PDB; 7G95; X-ray; 1.55 A; A=1-184. DR PDB; 7G96; X-ray; 2.30 A; A=1-184. DR PDB; 7G97; X-ray; 2.30 A; A=1-184. DR PDB; 7G98; X-ray; 2.88 A; A=1-184. DR PDB; 7G99; X-ray; 1.78 A; A=1-184. DR PDB; 7G9A; X-ray; 2.58 A; A=1-184. DR PDB; 7G9B; X-ray; 2.55 A; A=1-184. DR PDB; 7G9C; X-ray; 2.69 A; A=1-184. DR PDB; 7G9D; X-ray; 2.66 A; A=1-184. DR PDB; 7G9E; X-ray; 2.15 A; A=1-184. DR PDB; 7G9F; X-ray; 1.94 A; A=1-184. DR PDB; 7G9G; X-ray; 2.08 A; A=1-184. DR PDB; 7G9H; X-ray; 2.75 A; A=1-184. DR PDB; 7G9I; X-ray; 2.20 A; A=1-184. DR PDB; 7G9J; X-ray; 1.97 A; A=1-184. DR PDB; 7QSC; X-ray; 1.91 A; B/D=2-193. DR PDB; 7QTM; X-ray; 2.25 A; B/I=2-193. DR PDB; 7WZA; X-ray; 1.50 A; A=1-181. DR PDB; 7WZC; X-ray; 1.80 A; A=1-181. DR PDB; 8BNT; X-ray; 1.40 A; A=1-184. DR PDB; 8FC7; EM; 3.30 A; E/F/G/H=1-193. DR PDB; 8FC9; EM; 3.75 A; E/F/G/H=1-193. DR PDB; 8FCB; EM; 3.52 A; E/F/G/H=1-193. DR PDB; 8T1C; EM; 3.49 A; E=1-193. 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 PDBsum; 7G80; -. DR PDBsum; 7G81; -. DR PDBsum; 7G82; -. DR PDBsum; 7G83; -. DR PDBsum; 7G84; -. DR PDBsum; 7G85; -. DR PDBsum; 7G86; -. DR PDBsum; 7G87; -. DR PDBsum; 7G88; -. DR PDBsum; 7G89; -. DR PDBsum; 7G8A; -. DR PDBsum; 7G8B; -. DR PDBsum; 7G8C; -. DR PDBsum; 7G8D; -. DR PDBsum; 7G8E; -. DR PDBsum; 7G8F; -. DR PDBsum; 7G8G; -. DR PDBsum; 7G8H; -. DR PDBsum; 7G8I; -. DR PDBsum; 7G8J; -. DR PDBsum; 7G8K; -. DR PDBsum; 7G8L; -. DR PDBsum; 7G8M; -. DR PDBsum; 7G8N; -. DR PDBsum; 7G8O; -. DR PDBsum; 7G8P; -. DR PDBsum; 7G8Q; -. DR PDBsum; 7G8R; -. DR PDBsum; 7G8S; -. DR PDBsum; 7G8T; -. DR PDBsum; 7G8U; -. DR PDBsum; 7G8V; -. DR PDBsum; 7G8W; -. DR PDBsum; 7G8X; -. DR PDBsum; 7G8Y; -. DR PDBsum; 7G8Z; -. DR PDBsum; 7G90; -. DR PDBsum; 7G91; -. DR PDBsum; 7G92; -. DR PDBsum; 7G93; -. DR PDBsum; 7G94; -. DR PDBsum; 7G95; -. DR PDBsum; 7G96; -. DR PDBsum; 7G97; -. DR PDBsum; 7G98; -. DR PDBsum; 7G99; -. DR PDBsum; 7G9A; -. DR PDBsum; 7G9B; -. DR PDBsum; 7G9C; -. DR PDBsum; 7G9D; -. DR PDBsum; 7G9E; -. DR PDBsum; 7G9F; -. DR PDBsum; 7G9G; -. DR PDBsum; 7G9H; -. DR PDBsum; 7G9I; -. DR PDBsum; 7G9J; -. DR PDBsum; 7QSC; -. DR PDBsum; 7QTM; -. DR PDBsum; 7WZA; -. DR PDBsum; 7WZC; -. DR PDBsum; 8BNT; -. DR PDBsum; 8FC7; -. DR PDBsum; 8FC9; -. DR PDBsum; 8FCB; -. DR PDBsum; 8T1C; -. DR AlphaFoldDB; P61586; -. DR BMRB; P61586; -. DR EMDB; EMD-28975; -. DR EMDB; EMD-28977; -. DR EMDB; EMD-40959; -. DR SMR; P61586; -. DR BioGRID; 106880; 1246. DR CORUM; P61586; -. DR DIP; DIP-29642N; -. DR IntAct; P61586; 201. DR MINT; P61586; -. DR STRING; 9606.ENSP00000400175; -. DR BindingDB; P61586; -. DR ChEMBL; CHEMBL6052; -. DR DrugBank; DB04315; Guanosine-5'-Diphosphate. DR GlyCosmos; P61586; 2 sites, No reported glycans. DR GlyGen; P61586; 2 sites, 1 O-linked glycan (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; 9606-ENSP00000400175; -. DR PeptideAtlas; P61586; -. DR ProteomicsDB; 57321; -. DR Pumba; P61586; -. DR TopDownProteomics; P61586; -. DR Antibodypedia; 30508; 839 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 AGR; HGNC:667; -. 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; EDIKIHL; -. DR OrthoDB; 20499at2759; -. 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; 284 hits in 1194 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 214 other cell types or tissues. DR ExpressionAtlas; P61586; baseline and differential. DR GO; GO:0043296; C:apical junction complex; IDA:UniProtKB. 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:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0043197; C:dendritic spine; IDA:SynGO. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005768; C:endosome; IMP:AgBase. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO: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: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:0019901; F:protein kinase binding; IBA:GO_Central. DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB. 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:0003189; P:aortic valve formation; IGI:BHF-UCL. 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:0061430; P:bone trabecula morphogenesis; ISS:BHF-UCL. DR GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB. DR GO; GO:0016477; P:cell migration; IDA:UniProtKB. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. 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: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:0021861; P:forebrain radial glial cell differentiation; 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: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: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:0001764; P:neuron migration; 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:0046638; P:positive regulation of alpha-beta T cell differentiation; IEA:Ensembl. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:ARUK-UCL. DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP: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:0045666; P:positive regulation of neuron differentiation; IMP:MGI. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; NAS:UniProtKB. 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: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:0030334; P:regulation of cell migration; IMP:UniProtKB. 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; IDA:SynGO. DR GO; GO:0099159; P:regulation of modification of postsynaptic structure; IDA:SynGO. DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl. DR GO; GO:0010975; P:regulation of neuron projection development; 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:0007266; P:Rho protein signal transduction; IDA:UniProtKB. DR GO; GO:0035385; P:Roundabout signaling pathway; IDA:UniProtKB. DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:BHF-UCL. 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:0021762; P:substantia nigra development; HEP:UniProtKB. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB. 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 CDD; cd01870; RhoA_like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1. DR PANTHER; PTHR24072:SF153; TRANSFORMING PROTEIN RHOA; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51420; RHO; 1. DR Genevisible; P61586; HS. 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; Isopeptide bond; Lipoprotein; Magnesium; KW Membrane; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; KW Prenylation; 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 CROSSLNK 135 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:23871831" 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 135 FT /note="K->R: Reduced FBXL19-mediated ubiquitination and FT subsequent degradation." FT /evidence="ECO:0000269|PubMed:23871831" 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:8BNT" 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 //