ID RAC1_HUMAN Reviewed; 192 AA.
AC P63000; O95501; P15154; Q3Y4D3; Q5JAA8; Q9BTB4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 05-FEB-2025, entry version 221.
DE RecName: Full=Ras-related C3 botulinum toxin substrate 1 {ECO:0000305};
DE EC=3.6.5.2 {ECO:0000269|PubMed:21565175};
DE AltName: Full=Cell migration-inducing gene 5 protein;
DE AltName: Full=Ras-like protein TC25;
DE AltName: Full=p21-Rac1;
DE Flags: Precursor;
GN Name=RAC1 {ECO:0000312|HGNC:HGNC:9801}; Synonyms=TC25; ORFNames=MIG5;
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] (ISOFORM A).
RX PubMed=2674130; DOI=10.1016/s0021-9258(19)84716-6;
RA Didsbury J., Weber R.F., Bokoch G.M., Evans T., Snyderman R.;
RT "Rac, a novel ras-related family of proteins that are botulinum toxin
RT substrates.";
RL J. Biol. Chem. 264:16378-16382(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=2108320; DOI=10.1128/mcb.10.4.1793-1798.1990;
RA Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.;
RT "Characterization of four novel ras-like genes expressed in a human
RT teratocarcinoma cell line.";
RL Mol. Cell. Biol. 10:1793-1798(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B).
RX PubMed=11062023; DOI=10.1006/bbrc.2000.3743;
RA Matos P., Skaug J., Marques B., Beck S., Verissimo F., Gespach C.,
RA Boavida M.G., Scherer S.W., Jordan P.;
RT "Small GTPase Rac1: structure, localization, and expression of the human
RT gene.";
RL Biochem. Biophys. Res. Commun. 277:741-751(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC TISSUE=Colon, and Skin;
RX PubMed=10597294; DOI=10.1038/sj.onc.1203233;
RA Jordan P., Brazao R., Boavida M.G., Gespach C., Chastre E.;
RT "Cloning of a novel human Rac1b splice variant with increased expression in
RT colorectal tumors.";
RL Oncogene 18:6835-6839(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RA Schnelzer A., Knaus U., Prechtel D., Dehne K., Harbeck N., Gerhard M.,
RA Schmitt M., Lengyel E.;
RT "Mutations and altered expression of Rac1 in human breast cancer
RT -- characterization of a new Rac1 isoform, Rac1ins.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RA Kim J.W.;
RT "Identification of a human migration-inducing gene.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT ILE-135.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Pancreas, and Skin;
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 [12]
RP SUBCELLULAR LOCATION, AND ISOPRENYLATION AT CYS-189.
RX PubMed=1903399; DOI=10.1016/s0021-9258(18)92889-9;
RA Kinsella B.T., Erdman R.A., Maltese W.A.;
RT "Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins
RT encoded by rac1, rac2, and ralA.";
RL J. Biol. Chem. 266:9786-9794(1991).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1643658; DOI=10.1016/0092-8674(92)90164-8;
RA Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., Hall A.;
RT "The small GTP-binding protein rac regulates growth factor-induced membrane
RT ruffling.";
RL Cell 70:401-410(1992).
RN [14]
RP GLYCOSYLATION AT THR-35 (MICROBIAL 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 [15]
RP GLYCOSYLATION AT THR-35 (MICROBIAL INFECTION).
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 [16]
RP INTERACTION WITH RALBP1.
RX PubMed=7673236; DOI=10.1074/jbc.270.38.22473;
RA Jullien-Flores V., Dorseuil O., Romero F., Letourneur F., Saragosti S.,
RA Berger R., Tavitian A., Gacon G., Camonis J.H.;
RT "Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac
RT GTPase-activating protein activity.";
RL J. Biol. Chem. 270:22473-22477(1995).
RN [17]
RP GLYCOSYLATION AT THR-35 (MICROBIAL INFECTION).
RX PubMed=8626575; DOI=10.1074/jbc.271.17.10149;
RA Just I., Selzer J., Hofmann F., Green G.A., Aktories K.;
RT "Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed
RT glucosylation.";
RL J. Biol. Chem. 271:10149-10153(1996).
RN [18]
RP GLYCOSYLATION AT THR-35 (MICROBIAL INFECTION).
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 [19]
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 [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 DOCK2.
RX PubMed=10559471; DOI=10.1016/s0167-4889(99)00133-0;
RA Nishihara H., Kobayashi S., Hashimoto Y., Ohba F., Mochizuki N., Kurata T.,
RA Nagashima K., Matsuda M.;
RT "Non-adherent cell-specific expression of DOCK2, a member of the human CDM-
RT family proteins.";
RL Biochim. Biophys. Acta 1452:179-187(1999).
RN [22]
RP INTERACTION WITH PARD6A, AND MUTAGENESIS OF GLN-61.
RX PubMed=10954424; DOI=10.1242/jcs.113.18.3267;
RA Johansson A.-S., Driessens M., Aspenstroem P.;
RT "The mammalian homologue of the Caenorhabditis elegans polarity protein
RT PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1.";
RL J. Cell Sci. 113:3267-3275(2000).
RN [23]
RP INTERACTION WITH BAIAP2.
RX PubMed=11130076; DOI=10.1038/35047107;
RA Miki H., Yamaguchi H., Suetsugu S., Takenawa T.;
RT "IRSp53 is an essential intermediate between Rac and WAVE in the regulation
RT of membrane ruffling.";
RL Nature 408:732-735(2000).
RN [24]
RP INTERACTION WITH PLXNB1.
RX PubMed=11035813; DOI=10.1073/pnas.220421797;
RA Vikis H.G., Li W., He Z., Guan K.-L.;
RT "The semaphorin receptor plexin-B1 specifically interacts with active Rac
RT in a ligand-dependent manner.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12457-12462(2000).
RN [25]
RP PHOSPHORYLATION AT SER-71, AND MUTAGENESIS OF SER-71.
RX PubMed=10617634; DOI=10.1074/jbc.275.1.423;
RA Kwon T., Kwon D.Y., Chun J., Kim J.H., Kang S.S.;
RT "Akt protein kinase inhibits Rac1-GTP binding through phosphorylation at
RT serine 71 of Rac1.";
RL J. Biol. Chem. 275:423-428(2000).
RN [26]
RP INTERACTION WITH PARD6A; PARD6B AND PARD6G; PRKCI AND PRKCZ, AND
RP MUTAGENESIS OF GLY-12 AND THR-17.
RX PubMed=11260256; DOI=10.1046/j.1365-2443.2001.00404.x;
RA Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.;
RT "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6
RT as an adaptor that links the small GTPases Rac and Cdc42 to atypical
RT protein kinase C.";
RL Genes Cells 6:107-119(2001).
RN [27]
RP ACTIVATION BY PREX1.
RX PubMed=11955434; DOI=10.1016/s0092-8674(02)00663-3;
RA Welch H.C.E., Coadwell W.J., Ellson C.D., Ferguson G.J., Andrews S.R.,
RA Erdjument-Bromage H., Tempst P., Hawkins P.T., Stephens L.R.;
RT "P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide
RT exchange factor for Rac.";
RL Cell 108:809-821(2002).
RN [28]
RP INTERACTION WITH ITGB1BP1.
RX PubMed=11807099; DOI=10.1083/jcb.200108030;
RA Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L.,
RA Eva A., Tarone G.;
RT "The integrin cytoplasmic domain-associated protein ICAP-1 binds and
RT regulates Rho family GTPases during cell spreading.";
RL J. Cell Biol. 156:377-387(2002).
RN [29]
RP SUBUNIT OF A COMPLEX CONTAINING ELMO1 AND DOCK1.
RX PubMed=12134158; DOI=10.1038/ncb824;
RA Brugnera E., Haney L., Grimsley C., Lu M., Walk S.F.,
RA Tosello-Trampont A.-C., Macara I.G., Madhani H., Fink G.R.,
RA Ravichandran K.S.;
RT "Unconventional Rac-GEF activity is mediated through the Dock180-ELMO
RT complex.";
RL Nat. Cell Biol. 4:574-582(2002).
RN [30]
RP INTERACTION WITH RAP1GDS1, SUBCELLULAR LOCATION, AND POLYBASIC REGION.
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 [31]
RP INTERACTION WITH NOXA1.
RX PubMed=12716910; DOI=10.1074/jbc.m212856200;
RA Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H.,
RA Sumimoto H.;
RT "Novel human homologues of p47phox and p67phox participate in activation of
RT superoxide-producing NADPH oxidases.";
RL J. Biol. Chem. 278:25234-25246(2003).
RN [32]
RP FUNCTION.
RX PubMed=12695502; DOI=10.1083/jcb.200211002;
RA Zhang H., Webb D.J., Asmussen H., Horwitz A.F.;
RT "Synapse formation is regulated by the signaling adaptor GIT1.";
RL J. Cell Biol. 161:131-142(2003).
RN [33]
RP INTERACTION WITH USP6.
RX PubMed=12612085; DOI=10.1128/mcb.23.6.2151-2161.2003;
RA Masuda-Robens J.M., Kutney S.N., Qi H., Chou M.M.;
RT "The TRE17 oncogene encodes a component of a novel effector pathway for Rho
RT GTPases Cdc42 and Rac1 and stimulates actin remodeling.";
RL Mol. Cell. Biol. 23:2151-2161(2003).
RN [34]
RP RETRACTED PAPER.
RX PubMed=15169762; DOI=10.1074/jbc.m401878200;
RA Li W., Guan K.L.;
RT "The Down syndrome cell adhesion molecule (DSCAM) interacts with and
RT activates Pak.";
RL J. Biol. Chem. 279:32824-32831(2004).
RN [35]
RP RETRACTION NOTICE OF PUBMED:15169762.
RX PubMed=26048998; DOI=10.1074/jbc.a115.401878;
RA Li W., Guan K.L.;
RT "The Down syndrome cell adhesion molecule (DSCAM) interacts with and
RT activates Pak.";
RL J. Biol. Chem. 290:14797-14797(2015).
RN [36]
RP INTERACTION WITH S100A8 AND CALPROTECTIN.
RX PubMed=15642721; DOI=10.1096/fj.04-2377fje;
RA Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C., Doussiere J.;
RT "The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase
RT activation by interaction with p67phox and Rac-2.";
RL FASEB J. 19:467-469(2005).
RN [37]
RP INTERACTION WITH DOCK4.
RX PubMed=16464467; DOI=10.1016/j.jmb.2006.01.017;
RA Yan D., Li F., Hall M.L., Sage C., Hu W.H., Giallourakis C., Upadhyay G.,
RA Ouyang X.M., Du L.L., Bethea J.R., Chen Z.Y., Yajnik V., Liu X.Z.;
RT "An isoform of GTPase regulator DOCK4 localizes to the stereocilia in the
RT inner ear and binds to harmonin (USH1C).";
RL J. Mol. Biol. 357:755-764(2006).
RN [38]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [39]
RP INTERACTION WITH DOCK7.
RX PubMed=16982419; DOI=10.1016/j.neuron.2006.07.020;
RA Watabe-Uchida M., John K.A., Janas J.A., Newey S.E., Van Aelst L.;
RT "The Rac activator DOCK7 regulates neuronal polarity through local
RT phosphorylation of stathmin/Op18.";
RL Neuron 51:727-739(2006).
RN [40]
RP INTERACTION WITH DEF6, AND DOMAIN.
RX PubMed=17121847; DOI=10.1074/jbc.m605153200;
RA Oka T., Ihara S., Fukui Y.;
RT "Cooperation of DEF6 with activated Rac in regulating cell morphology.";
RL J. Biol. Chem. 282:2011-2018(2007).
RN [41]
RP INTERACTION WITH BAIAP2L1.
RX PubMed=17430976; DOI=10.1242/jcs.001776;
RA Millard T.H., Dawson J., Machesky L.M.;
RT "Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with
RT distinct filament bundling properties.";
RL J. Cell Sci. 120:1663-1672(2007).
RN [42]
RP INTERACTION WITH SPATA13.
RX PubMed=17145773; DOI=10.1128/mcb.01608-06;
RA Hamann M.J., Lubking C.M., Luchini D.N., Billadeau D.D.;
RT "Asef2 functions as a Cdc42 exchange factor and is stimulated by the
RT release of an autoinhibitory module from a concealed C-terminal activation
RT element.";
RL Mol. Cell. Biol. 27:1380-1393(2007).
RN [43]
RP INTERACTION WITH RAPH1, AND MUTAGENESIS OF GLN-61.
RX PubMed=18499456; DOI=10.1016/j.cub.2008.04.050;
RA Quinn C.C., Pfeil D.S., Wadsworth W.G.;
RT "CED-10/Rac1 mediates axon guidance by regulating the asymmetric
RT distribution of MIG-10/lamellipodin.";
RL Curr. Biol. 18:808-813(2008).
RN [44]
RP UBIQUITINATION AT LYS-147.
RX PubMed=18093184; DOI=10.1111/j.1742-4658.2007.06209.x;
RA Visvikis O., Lores P., Boyer L., Chardin P., Lemichez E., Gacon G.;
RT "Activated Rac1, but not the tumorigenic variant Rac1b, is ubiquitinated on
RT Lys 147 through a JNK-regulated process.";
RL FEBS J. 275:386-396(2008).
RN [45]
RP FUNCTION, AND MUTAGENESIS OF GLY-12 AND THR-17.
RX PubMed=19029984; DOI=10.1038/nm.1879;
RA Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H.,
RA Miyoshi J., Takai Y., Fujita T.;
RT "Modification of mineralocorticoid receptor function by Rac1 GTPase:
RT implication in proteinuric kidney disease.";
RL Nat. Med. 14:1370-1376(2008).
RN [46]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 (ISOFORM B), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [47]
RP GLYCOSYLATION AT THR-35 (MICROBIAL INFECTION).
RX PubMed=19744486; DOI=10.1016/j.febslet.2009.09.006;
RA Huelsenbeck S.C., Klose I., Reichenbach M., Huelsenbeck J., Genth H.;
RT "Distinct kinetics of (H/K/N)Ras glucosylation and Rac1 glucosylation
RT catalysed by Clostridium sordellii lethal toxin.";
RL FEBS Lett. 583:3133-3139(2009).
RN [48]
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 [49]
RP INTERACTION WITH MTSS2.
RX PubMed=20875796; DOI=10.1016/j.bbrc.2010.09.087;
RA Zheng D., Niu S., Yu D., Zhan X.H., Zeng X., Cui B., Chen Y., Yoon J.,
RA Martin S.S., Lu X., Zhan X.;
RT "Abba promotes PDGF-mediated membrane ruffling through activation of the
RT small GTPase Rac1.";
RL Biochem. Biophys. Res. Commun. 401:527-532(2010).
RN [50]
RP INTERACTION WITH UNKL.
RX PubMed=20148946; DOI=10.1111/j.1742-4658.2010.07575.x;
RA Lores P., Visvikis O., Luna R., Lemichez E., Gacon G.;
RT "The SWI/SNF protein BAF60b is ubiquitinated through a signalling process
RT involving Rac GTPase and the RING finger protein Unkempt.";
RL FEBS J. 277:1453-1464(2010).
RN [51]
RP FUNCTION, AND INTERACTION WITH ITGB4.
RX PubMed=19403692; DOI=10.1091/mbc.e09-01-0051;
RA Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.;
RT "BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated
RT modulation of Rac1 and cofilin activities.";
RL Mol. Biol. Cell 20:2954-2962(2009).
RN [52]
RP AMPYLATION AT TYR-32 (MICROBIAL INFECTION), IDENTIFICATION BY MASS
RP SPECTROMETRY, AND MUTAGENESIS OF TYR-32.
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 [53]
RP AMPYLATION AT THR-35 (MICROBIAL INFECTION), IDENTIFICATION BY MASS
RP SPECTROMETRY, AND MUTAGENESIS OF THR-35.
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 [54]
RP INTERACTION WITH TBC1D2.
RX PubMed=20116244; DOI=10.1016/j.cub.2009.12.053;
RA Frasa M.A., Maximiano F.C., Smolarczyk K., Francis R.E., Betson M.E.,
RA Lozano E., Goldenring J., Seabra M.C., Rak A., Ahmadian M.R., Braga V.M.;
RT "Armus is a Rac1 effector that inactivates Rab7 and regulates E-cadherin
RT degradation.";
RL Curr. Biol. 20:198-208(2010).
RN [55]
RP INTERACTION WITH PAK2; SH3RF1 AND SH3RF3.
RX PubMed=20696164; DOI=10.1016/j.febslet.2010.07.060;
RA Kaerkkaeinen S., van der Linden M., Renkema G.H.;
RT "POSH2 is a RING finger E3 ligase with Rac1 binding activity through a
RT partial CRIB domain.";
RL FEBS Lett. 584:3867-3872(2010).
RN [56]
RP FUNCTION.
RX PubMed=20696765; DOI=10.1074/jbc.m110.120451;
RA Li X., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through
RT RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
RL J. Biol. Chem. 285:32436-32445(2010).
RN [57]
RP FUNCTION, INTERACTION WITH PPP5C, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-17; GLY-30; THR-35 AND GLN-61.
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 [58]
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 [59]
RP INTERACTION WITH ARHGEF16.
RX PubMed=20679435; DOI=10.1083/jcb.201005141;
RA Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S.,
RA Negishi M., Katoh H.;
RT "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent
RT mechanism.";
RL J. Cell Biol. 190:461-477(2010).
RN [60]
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 [61]
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 [62]
RP UBIQUITINATION.
RX PubMed=22036506; DOI=10.1016/j.devcel.2011.08.015;
RA Torrino S., Visvikis O., Doye A., Boyer L., Stefani C., Munro P.,
RA Bertoglio J., Gacon G., Mettouchi A., Lemichez E.;
RT "The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation of active
RT Rac1.";
RL Dev. Cell 21:959-965(2011).
RN [63]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PACSIN2.
RX PubMed=21693584; DOI=10.1242/jcs.080630;
RA de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C., Hensbergen P.J.,
RA Deelder A.M., Plomann M., Hordijk P.L.;
RT "The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell
RT spreading and migration.";
RL J. Cell Sci. 124:2375-2388(2011).
RN [64]
RP 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 [65]
RP FUNCTION, AND INTERACTION WITH DSG3.
RX PubMed=22796473; DOI=10.1016/j.yexcr.2012.07.002;
RA Tsang S.M., Brown L., Gadmor H., Gammon L., Fortune F., Wheeler A., Wan H.;
RT "Desmoglein 3 acting as an upstream regulator of Rho GTPases, Rac-1/Cdc42
RT in the regulation of actin organisation and dynamics.";
RL Exp. Cell Res. 318:2269-2283(2012).
RN [66]
RP FUNCTION, INTERACTION WITH CD151 AND INTEGRIN BETA1/ITGB1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22843693; DOI=10.1074/jbc.m111.314443;
RA Hong I.K., Jeoung D.I., Ha K.S., Kim Y.M., Lee H.;
RT "Tetraspanin CD151 stimulates adhesion-dependent activation of Ras, Rac,
RT and Cdc42 by facilitating molecular association between beta1 integrins and
RT small GTPases.";
RL J. Biol. Chem. 287:32027-32039(2012).
RN [67]
RP INTERACTION WITH FARP1.
RX PubMed=23209303; DOI=10.1083/jcb.201205041;
RA Cheadle L., Biederer T.;
RT "The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal
RT dynamics and transsynaptic organization.";
RL J. Cell Biol. 199:985-1001(2012).
RN [68]
RP FUNCTION, MUTAGENESIS OF SER-71 AND LYS-166, AND UBIQUITINATION AT LYS-166.
RX PubMed=23512198; DOI=10.1096/fj.12-223099;
RA Zhao J., Mialki R.K., Wei J., Coon T.A., Zou C., Chen B.B.,
RA Mallampalli R.K., Zhao Y.;
RT "SCF E3 ligase F-box protein complex SCF(FBXL19) regulates cell migration
RT by mediating Rac1 ubiquitination and degradation.";
RL FASEB J. 27:2611-2619(2013).
RN [69]
RP INTERACTION WITH ARHGDIA.
RX PubMed=23434736; DOI=10.1136/jmedgenet-2012-101442;
RA Gupta I.R., Baldwin C., Auguste D., Ha K.C., El Andalousi J.,
RA Fahiminiya S., Bitzan M., Bernard C., Akbari M.R., Narod S.A.,
RA Rosenblatt D.S., Majewski J., Takano T.;
RT "ARHGDIA: a novel gene implicated in nephrotic syndrome.";
RL J. Med. Genet. 50:330-338(2013).
RN [70]
RP FUNCTION.
RX PubMed=23633677; DOI=10.1126/scisignal.2003627;
RA Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B.,
RA Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A., Bonecchi R.,
RA Locati M.;
RT "Beta-arrestin-dependent activation of the cofilin pathway is required for
RT the scavenging activity of the atypical chemokine receptor D6.";
RL Sci. Signal. 6:RA30-RA30(2013).
RN [71]
RP GLYCOSYLATION AT TYR-32 (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 [72]
RP INTERACTION WITH FARP2.
RX PubMed=23375260; DOI=10.1016/j.str.2013.01.001;
RA He X., Kuo Y.C., Rosche T.J., Zhang X.;
RT "Structural basis for autoinhibition of the guanine nucleotide exchange
RT factor FARP2.";
RL Structure 21:355-364(2013).
RN [73]
RP GLYCOSYLATION AT THR-35 (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 [74]
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 [75]
RP FUNCTION, INVOLVEMENT IN MRD48, VARIANTS MRD48 TYR-18; SER-39; LEU-51;
RP MET-51; ASP-64; LEU-73 AND TYR-157, AND CHARACTERIZATION OF VARIANTS MRD48
RP TYR-18; SER-39; MET-51; ASP-64; LEU-73 AND TYR-157.
RX PubMed=28886345; DOI=10.1016/j.ajhg.2017.08.007;
RG Deciphering Developmental Disorders Study;
RA Reijnders M.R.F., Ansor N.M., Kousi M., Yue W.W., Tan P.L., Clarkson K.,
RA Clayton-Smith J., Corning K., Jones J.R., Lam W.W.K., Mancini G.M.S.,
RA Marcelis C., Mohammed S., Pfundt R., Roifman M., Cohn R., Chitayat D.,
RA Millard T.H., Katsanis N., Brunner H.G., Banka S.;
RT "RAC1 Missense Mutations in Developmental Disorders with Diverse
RT Phenotypes.";
RL Am. J. Hum. Genet. 101:466-477(2017).
RN [76]
RP PALMITOYLATION AT LYS-183 AND LYS-184 (MICROBIAL INFECTION), SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLY-12; 183-LYS--LYS-188; LYS-183; LYS-184;
RP 185-ARG--ARG-187; LYS-186 AND LYS-188.
RX PubMed=29074776; DOI=10.1126/science.aam8659;
RA Zhou Y., Huang C., Yin L., Wan M., Wang X., Li L., Liu Y., Wang Z., Fu P.,
RA Zhang N., Chen S., Liu X., Shao F., Zhu Y.;
RT "Nepsilon-fatty acylation of Rho GTPases by a MARTX toxin effector.";
RL Science 358:528-531(2017).
RN [77]
RP INTERACTION WITH CYRIB, AND MUTAGENESIS OF GLY-12; THR-17 AND GLN-61.
RX PubMed=30250061; DOI=10.1038/s41556-018-0198-9;
RA Fort L., Batista J.M., Thomason P.A., Spence H.J., Whitelaw J.A.,
RA Tweedy L., Greaves J., Martin K.J., Anderson K.I., Brown P., Lilla S.,
RA Neilson M.P., Tafelmeyer P., Zanivan S., Ismail S., Bryant D.M.,
RA Tomkinson N.C.O., Chamberlain L.H., Mastick G.S., Insall R.H.,
RA Machesky L.M.;
RT "Fam49/CYRI interacts with Rac1 and locally suppresses protrusions.";
RL Nat. Cell Biol. 20:1159-1171(2018).
RN [78]
RP INTERACTION WITH CYRIB.
RX PubMed=31285585; DOI=10.1038/s41564-019-0484-8;
RA Yuki K.E., Marei H., Fiskin E., Eva M.M., Gopal A.A.,
RA Schwartzentruber J.A., Majewski J., Cellier M., Mandl J.N., Vidal S.M.,
RA Malo D., Dikic I.;
RT "CYRI/FAM49B negatively regulates RAC1-driven cytoskeletal remodelling and
RT protects against bacterial infection.";
RL Nat. Microbiol. 4:1516-1531(2019).
RN [79]
RP INTERACTION WITH GARRE1, AND MUTAGENESIS OF GLY-12.
RX PubMed=31871319; DOI=10.1038/s41556-019-0438-7;
RA Bagci H., Sriskandarajah N., Robert A., Boulais J., Elkholi I.E., Tran V.,
RA Lin Z.Y., Thibault M.P., Dube N., Faubert D., Hipfner D.R., Gingras A.C.,
RA Cote J.F.;
RT "Mapping the proximity interaction network of the Rho-family GTPases
RT reveals signalling pathways and regulatory mechanisms.";
RL Nat. Cell Biol. 22:120-134(2020).
RN [80]
RP INTERACTION WITH TNFAIP8L2.
RX PubMed=32460619; DOI=10.1080/15548627.2020.1761748;
RA Li W., Li Y., Guan Y., Du Y., Zhao M., Chen X., Zhu F., Guo C., Jia Y.,
RA Li Y., Wang X., Wang X., Shi Y., Wang Q., Li Y., Zhang L.;
RT "TNFAIP8L2/TIPE2 impairs autolysosome reformation via modulating the RAC1-
RT MTORC1 axis.";
RL Autophagy 17:1410-1425(2021).
RN [81]
RP INTERACTION WITH ARHGAP36.
RX PubMed=35986704; DOI=10.1111/bjd.21842;
RA Liu Y., Banka S., Huang Y., Hardman-Smart J., Pye D., Torrelo A.,
RA Beaman G.M., Kazanietz M.G., Baker M.J., Ferrazzano C., Shi C., Orozco G.,
RA Eyre S., van Geel M., Bygum A., Fischer J., Miedzybrodzka Z., Abuzahra F.,
RA Ruebben A., Cuvertino S., Ellingford J.M., Smith M.J., Evans D.G.,
RA Weppner-Parren L.J.M.T., van Steensel M.A.M., Chaudhary I.H., Mangham D.C.,
RA Lear J.T., Paus R., Frank J., Newman W.G., Zhang X.;
RT "Germline intergenic duplications at Xq26.1 underlie Bazex-Dupre-Christol
RT basal cell carcinoma susceptibility syndrome.";
RL Br. J. Dermatol. 187:948-961(2022).
RN [82]
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 1-184 IN COMPLEX WITH GTP ANALOG.
RX PubMed=9033596; DOI=10.1038/nsb0297-147;
RA Hirshberg M., Stockley R.W., Dodson G., Webb M.R.;
RT "The crystal structure of human rac1, a member of the rho-family complexed
RT with a GTP analogue.";
RL Nat. Struct. Biol. 4:147-152(1997).
RN [83]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT LEU-61 IN COMPLEX WITH GTP
RP AND NCF2.
RX PubMed=11090627; DOI=10.1016/s1097-2765(05)00091-2;
RA Lapouge K., Smith S.J., Walker P.A., Gamblin S.J., Smerdon S.J.,
RA Rittinger K.;
RT "Structure of the TPR domain of p67phox in complex with Rac.GTP.";
RL Mol. Cell 6:899-907(2000).
RN [84]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-177 IN COMPLEX WITH TIAM1.
RX PubMed=11130063; DOI=10.1038/35047014;
RA Worthylake D.K., Rossman K.L., Sondek J.;
RT "Crystal structure of Rac1 in complex with the guanine nucleotide exchange
RT region of Tiam1.";
RL Nature 408:682-688(2000).
RN [85]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-184 IN COMPLEX WITH SALMONELLA
RP SPTP.
RX PubMed=11163217; DOI=10.1016/s1097-2765(00)00141-6;
RA Stebbins C.E., Galan J.E.;
RT "Modulation of host signaling by a bacterial mimic: structure of the
RT Salmonella effector SptP bound to Rac1.";
RL Mol. Cell 6:1449-1460(2000).
RN [86]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-176 IN COMPLEX WITH GTP ANALOG
RP AND P.AERUGINOSA EXOS.
RX PubMed=11135665; DOI=10.1038/83007;
RA Wuertele M., Wolf E., Pederson K.J., Buchwald G., Ahmadian M.R.,
RA Barbieri J.T., Wittinghofer A.;
RT "How the Pseudomonas aeruginosa ExoS toxin downregulates Rac.";
RL Nat. Struct. Biol. 8:23-26(2001).
RN [87]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ARHGDIA.
RX PubMed=11513578; DOI=10.1021/bi010288k;
RA Grizot S., Faure J., Fieschi F., Vignais P.V., Dagher M.-C.,
RA Pebay-Peyroula E.;
RT "Crystal structure of the Rac1-RhoGDI complex involved in NADPH oxidase
RT activation.";
RL Biochemistry 40:10007-10013(2001).
RN [88]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND
RP ARFIP2.
RX PubMed=11346801; DOI=10.1038/35075620;
RA Tarricone C., Xiao B., Justin N., Walker P.A., Rittinger K., Gamblin S.J.,
RA Smerdon S.J.;
RT "The structural basis of Arfaptin-mediated cross-talk between Rac and Arf
RT signalling pathways.";
RL Nature 411:215-219(2001).
RN [89]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF ISOFORM B, AND FUNCTION (ISOFORM
RP B).
RX PubMed=14625275; DOI=10.1074/jbc.m310281200;
RA Fiegen D., Haeusler L.C., Blumenstein L., Herbrand U., Dvorsky R.,
RA Vetter I.R., Ahmadian M.R.;
RT "Alternative splicing of Rac1 generates Rac1b, a self-activating GTPase.";
RL J. Biol. Chem. 279:4743-4749(2004).
RN [90]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-184 IN COMPLEX WITH
RP Y.PSEUDOTUBERCULOSIS YPKA.
RX PubMed=16959567; DOI=10.1016/j.cell.2006.06.056;
RA Prehna G., Ivanov M.I., Bliska J.B., Stebbins C.E.;
RT "Yersinia virulence depends on mimicry of host Rho-family nucleotide
RT dissociation inhibitors.";
RL Cell 126:869-880(2006).
RN [91]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-177 IN COMPLEX WITH GTP ANALOG
RP AND PLCB2, AND MUTAGENESIS OF PHE-37; TRP-56; LEU-67 AND LEU-70.
RX PubMed=17115053; DOI=10.1038/nsmb1175;
RA Jezyk M.R., Snyder J.T., Gershberg S., Worthylake D.K., Harden T.K.,
RA Sondek J.;
RT "Crystal structure of Rac1 bound to its effector phospholipase C-beta2.";
RL Nat. Struct. Mol. Biol. 13:1135-1140(2006).
RN [92]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-177 IN COMPLEX WITH DOCK2.
RX PubMed=21613211; DOI=10.1074/jbc.m111.236455;
RA Kulkarni K., Yang J., Zhang Z., Barford D.;
RT "Multiple factors confer specific Cdc42 and Rac protein activation by
RT dedicator of cytokinesis (DOCK) nucleotide exchange factors.";
RL J. Biol. Chem. 286:25341-25351(2011).
RN [93] {ECO:0007744|PDB:8Q0N}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH HACE1 AND
RP GTP, UBIQUITINATION AT LYS-147, AND MUTAGENESIS OF GLN-61.
RX PubMed=38332367; DOI=10.1038/s41594-023-01203-4;
RA During J., Wolter M., Toplak J.J., Torres C., Dybkov O., Fokkens T.J.,
RA Bohnsack K.E., Urlaub H., Steinchen W., Dienemann C., Lorenz S.;
RT "Structural mechanisms of autoinhibition and substrate recognition by the
RT ubiquitin ligase HACE1.";
RL Nat. Struct. Mol. Biol. 31:364-377(2024).
RN [94] {ECO:0007744|PDB:8WEJ}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.79 ANGSTROMS) OF 1-192 IN COMPLEX WITH
RP CYBA; CYBB; NFC1; NFC2 AND GTP, SUBUNIT, FUNCTION, AND IDENTIFICATION OF
RP THE NADPH OXIDASE COMPLEX.
RX PubMed=38355798; DOI=10.1038/s41586-024-07056-1;
RA Liu X., Shi Y., Liu R., Song K., Chen L.;
RT "Structure of human phagocyte NADPH oxidase in the activated state.";
RL Nature 627:189-195(2024).
CC -!- FUNCTION: Plasma membrane-associated small GTPase which cycles between
CC active GTP-bound and inactive GDP-bound states. In its active state,
CC binds to a variety of effector proteins to regulate cellular responses
CC such as secretory processes, phagocytosis of apoptotic cells,
CC epithelial cell polarization, neurons adhesion, migration and
CC differentiation, and growth-factor induced formation of membrane
CC ruffles (PubMed:1643658, PubMed:22843693, PubMed:23512198,
CC PubMed:28886345). Rac1 p21/rho GDI heterodimer is the active component
CC of the cytosolic factor sigma 1, which is involved in stimulation of
CC the NADPH oxidase activity in macrophages. Essential for the SPATA13-
CC mediated regulation of cell migration and adhesion assembly and
CC disassembly. Stimulates PKN2 kinase activity (PubMed:9121475). In
CC concert with RAB7A, plays a role in regulating the formation of RBs
CC (ruffled borders) in osteoclasts (PubMed:1643658). In podocytes,
CC promotes nuclear shuttling of NR3C2; this modulation is required for a
CC proper kidney functioning. Required for atypical chemokine receptor
CC ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1)
CC and for up-regulation of ACKR2 from endosomal compartment to cell
CC membrane, increasing its efficiency in chemokine uptake and
CC degradation. In neurons, is involved in dendritic spine formation and
CC synaptic plasticity (By similarity). In hippocampal neurons, involved
CC in spine morphogenesis and synapse formation, through local activation
CC at synapses by guanine nucleotide exchange factors (GEFs), such as
CC ARHGEF6/ARHGEF7/PIX (PubMed:12695502). In synapses, seems to mediate
CC the regulation of F-actin cluster formation performed by SHANK3. In
CC neurons, plays a crucial role in regulating GABA(A) receptor synaptic
CC stability and hence GABAergic inhibitory synaptic transmission through
CC its role in PAK1 activation and eventually F-actin stabilization (By
CC similarity). Required for DSG3 translocation to cell-cell junctions,
CC DSG3-mediated organization of cortical F-actin bundles and anchoring of
CC actin at cell junctions; via interaction with DSG3 (PubMed:22796473).
CC Subunit of the phagocyte NADPH oxidase complex that mediates the
CC transfer of electrons from cytosolic NADPH to O2 to produce the
CC superoxide anion (O2(-)) (PubMed:38355798).
CC {ECO:0000250|UniProtKB:P63001, ECO:0000250|UniProtKB:Q6RUV5,
CC ECO:0000269|PubMed:12695502, ECO:0000269|PubMed:1643658,
CC ECO:0000269|PubMed:22796473, ECO:0000269|PubMed:22843693,
CC ECO:0000269|PubMed:23512198, ECO:0000269|PubMed:28886345,
CC ECO:0000269|PubMed:38355798, ECO:0000269|PubMed:9121475}.
CC -!- FUNCTION: [Isoform B]: Isoform B has an accelerated GEF-independent
CC GDP/GTP exchange and an impaired GTP hydrolysis, which is restored
CC partially by GTPase-activating proteins (PubMed:14625275). It is able
CC to bind to the GTPase-binding domain of PAK but not full-length PAK in
CC a GTP-dependent manner, suggesting that the insertion does not
CC completely abolish effector interaction (PubMed:14625275).
CC {ECO:0000269|PubMed:14625275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + phosphate + H(+); 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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:21565175};
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. GTP hydrolysis is stimulated by ARHGAP30.
CC {ECO:0000269|PubMed:21565175}.
CC -!- SUBUNIT: Interacts with NISCH. Interacts with PIP5K1A. Interacts with
CC the GTP-bound form of RAB7A. Interacts with SRGAP2. Interacts with
CC CYFIP1/SRA-1. Interacts with PLXNB3. Interacts with ARHGDIA; the
CC interaction is induced by SEMA5A, mediated through PLXNB3 and
CC inactivates and stabilizes RAC1. Interacts (GTP-bound form
CC preferentially) with PKN2 (via the REM repeats); the interaction
CC stimulates autophosphorylation and phosphorylation of PKN2. Interacts
CC with the GEF proteins PREX1, RASGRF2, FARP1, FARP2, DOCK1, DOCK2 and
CC DOCK7, which promote the exchange between GDP and GTP, and therefore
CC activate it. Interacts with PARD6A, PARD6B and PARD6G in a GTP-
CC dependent manner. Part of a quaternary complex containing PARD3, some
CC PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein
CC (PRKCI or PRKCZ), which plays a central role in epithelial cell
CC polarization. Found in a trimeric complex composed of DOCK1 and ELMO1,
CC which plays a central role in phagocytosis of apoptotic cells.
CC Interacts with RALBP1 via its effector domain. Interacts with PLXNB1.
CC Part of a complex with MAP2K3, MAP3K3, CCM2 and DEF6. Interacts with
CC BAIAP2, BAIAP2L1 and DEF6. Interacts with Y.pseudotuberculosis YPKA and
CC PLCB2. Interacts with NOXA1. Interacts with ARHGEF2. Interacts with
CC TBC1D2. Interacts with UNKL. Interacts with USP6. Interacts with
CC SPATA13. Interacts with ARHGEF16; mediates activation of RAC1 by EPHA2.
CC Interacts with ITGB4. Interacts with S100A8 and calprotectin
CC (S100A8/9). Interacts with PACSIN2. Interacts with ITGB1BP1. Interacts
CC (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase
CC activity and translocates PPP5C to the cell membrane. Interacts with
CC RAPH1 (via Ras associating and PH domains) (PubMed:18499456). Interacts
CC with MTSS2 (via IMD domain); this interaction may be important to
CC potentiate PDGF-induced RAC1 activation (PubMed:20875796). Interacts
CC with PAK2 (PubMed:20696164). Interacts (GTP-bound form) with SH3RF1 and
CC SH3RF3 (PubMed:20696164). Found in a complex with SH3RF1,
CC MAPK8IP1/JIP1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1. Interacts
CC (both active GTP- or inactive GDP-bound forms) with SH3RF2 (By
CC similarity). Interacts (GTP-bound form preferentially) with CYRIB
CC (PubMed:30250061, PubMed:31285585). Interacts with DOCK4 (via DOCKER
CC domain); functions as a guanine nucleotide exchange factor (GEF) for
CC RAC1 (PubMed:16464467). Interacts with GARRE1 (PubMed:31871319).
CC Interacts with RAP1GDS1 (PubMed:12551911, PubMed:20709748). Interacts
CC with TNFAIP8L2 (PubMed:32460619). May interact with ARHGAP36
CC (PubMed:35986704). Interacts with CD151 and integrin beta1/ITGB1
CC (PubMed:22843693). Interacts with DSG3; the interaction is required for
CC DSG3 translocation to cell-cell junctions, organization of cortical F-
CC actin bundles and actin anchoring at cell-cell junctions
CC (PubMed:22796473). Component of the phagocyte NADPH oxidase complex
CC composed of an obligatory core heterodimer formed by the membrane
CC proteins CYBA and CYBB and the cytosolic regulatory subunits NCF1/p47-
CC phox, NCF2/p67-phox, NCF4/p40-phox and the small GTPase RAC1 or RAC2
CC (PubMed:38355798). Interacts with NCF2 (PubMed:11090627).
CC {ECO:0000250|UniProtKB:P63001, ECO:0000250|UniProtKB:Q6RUV5,
CC ECO:0000269|PubMed:10559471, ECO:0000269|PubMed:10954424,
CC ECO:0000269|PubMed:11035813, ECO:0000269|PubMed:11090627,
CC ECO:0000269|PubMed:11130063, ECO:0000269|PubMed:11130076,
CC ECO:0000269|PubMed:11135665, ECO:0000269|PubMed:11163217,
CC ECO:0000269|PubMed:11260256, ECO:0000269|PubMed:11346801,
CC ECO:0000269|PubMed:11513578, ECO:0000269|PubMed:11807099,
CC ECO:0000269|PubMed:12134158, ECO:0000269|PubMed:12551911,
CC ECO:0000269|PubMed:12612085, ECO:0000269|PubMed:12716910,
CC ECO:0000269|PubMed:15642721, ECO:0000269|PubMed:16464467,
CC ECO:0000269|PubMed:16959567, ECO:0000269|PubMed:16982419,
CC ECO:0000269|PubMed:17115053, ECO:0000269|PubMed:17121847,
CC ECO:0000269|PubMed:17145773, ECO:0000269|PubMed:17430976,
CC ECO:0000269|PubMed:18499456, ECO:0000269|PubMed:19403692,
CC ECO:0000269|PubMed:19948726, ECO:0000269|PubMed:20116244,
CC ECO:0000269|PubMed:20148946, ECO:0000269|PubMed:20679435,
CC ECO:0000269|PubMed:20696164, ECO:0000269|PubMed:20709748,
CC ECO:0000269|PubMed:20875796, ECO:0000269|PubMed:20974804,
CC ECO:0000269|PubMed:21613211, ECO:0000269|PubMed:21693584,
CC ECO:0000269|PubMed:22796473, ECO:0000269|PubMed:22843693,
CC ECO:0000269|PubMed:23209303, ECO:0000269|PubMed:23375260,
CC ECO:0000269|PubMed:23434736, ECO:0000269|PubMed:30250061,
CC ECO:0000269|PubMed:31285585, ECO:0000269|PubMed:31871319,
CC ECO:0000269|PubMed:32460619, ECO:0000269|PubMed:35986704,
CC ECO:0000269|PubMed:38355798, ECO:0000269|PubMed:7673236,
CC ECO:0000269|PubMed:9033596, ECO:0000269|PubMed:9121475,
CC ECO:0000269|PubMed:9857026}.
CC -!- INTERACTION:
CC P63000; Q9NY61: AATF; NbExp=3; IntAct=EBI-413628, EBI-372428;
CC P63000; P05067: APP; NbExp=3; IntAct=EBI-413628, EBI-77613;
CC P63000; P53365: ARFIP2; NbExp=13; IntAct=EBI-413628, EBI-638194;
CC P63000; Q92619: ARHGAP45; NbExp=3; IntAct=EBI-413628, EBI-2825900;
CC P63000; P52565: ARHGDIA; NbExp=10; IntAct=EBI-413628, EBI-712693;
CC P63000; Q14155: ARHGEF7; NbExp=8; IntAct=EBI-413628, EBI-717515;
CC P63000; Q9UQB8: BAIAP2; NbExp=4; IntAct=EBI-413628, EBI-525456;
CC P63000; Q14457: BECN1; NbExp=3; IntAct=EBI-413628, EBI-949378;
CC P63000; Q13490: BIRC2; NbExp=2; IntAct=EBI-413628, EBI-514538;
CC P63000; Q03135: CAV1; NbExp=3; IntAct=EBI-413628, EBI-603614;
CC P63000; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-413628, EBI-396137;
CC P63000; P52757: CHN2; NbExp=4; IntAct=EBI-413628, EBI-714925;
CC P63000; Q14185: DOCK1; NbExp=10; IntAct=EBI-413628, EBI-446740;
CC P63000; Q92608: DOCK2; NbExp=3; IntAct=EBI-413628, EBI-448771;
CC P63000; O75369: FLNB; NbExp=2; IntAct=EBI-413628, EBI-352089;
CC P63000; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-413628, EBI-618189;
CC P63000; Q8IYU2: HACE1; NbExp=5; IntAct=EBI-413628, EBI-308277;
CC P63000; Q8WUI4-6: HDAC7; NbExp=4; IntAct=EBI-413628, EBI-12094670;
CC P63000; P46940: IQGAP1; NbExp=11; IntAct=EBI-413628, EBI-297509;
CC P63000; P05412: JUN; NbExp=5; IntAct=EBI-413628, EBI-852823;
CC P63000; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-413628, EBI-743960;
CC P63000; Q6A162: KRT40; NbExp=3; IntAct=EBI-413628, EBI-10171697;
CC P63000; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-413628, EBI-11985629;
CC P63000; Q5S007: LRRK2; NbExp=5; IntAct=EBI-413628, EBI-5323863;
CC P63000; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-413628, EBI-741037;
CC P63000; Q13387-4: MAPK8IP2; NbExp=3; IntAct=EBI-413628, EBI-12345753;
CC P63000; Q99750: MDFI; NbExp=3; IntAct=EBI-413628, EBI-724076;
CC P63000; P41227: NAA10; NbExp=3; IntAct=EBI-413628, EBI-747693;
CC P63000; Q01968: OCRL; NbExp=3; IntAct=EBI-413628, EBI-6148898;
CC P63000; Q13153: PAK1; NbExp=26; IntAct=EBI-413628, EBI-1307;
CC P63000; Q13177: PAK2; NbExp=5; IntAct=EBI-413628, EBI-1045887;
CC P63000; Q9NPB6: PARD6A; NbExp=2; IntAct=EBI-413628, EBI-81876;
CC P63000; Q9BYG5: PARD6B; NbExp=3; IntAct=EBI-413628, EBI-295391;
CC P63000; Q9BYG4: PARD6G; NbExp=2; IntAct=EBI-413628, EBI-295417;
CC P63000; Q9UHV9: PFDN2; NbExp=3; IntAct=EBI-413628, EBI-359873;
CC P63000; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-413628, EBI-9090282;
CC P63000; P19174: PLCG1; NbExp=7; IntAct=EBI-413628, EBI-79387;
CC P63000; P00491: PNP; NbExp=3; IntAct=EBI-413628, EBI-712238;
CC P63000; P41743: PRKCI; NbExp=3; IntAct=EBI-413628, EBI-286199;
CC P63000; P52306: RAP1GDS1; NbExp=4; IntAct=EBI-413628, EBI-746389;
CC P63000; Q92963: RIT1; NbExp=5; IntAct=EBI-413628, EBI-365845;
CC P63000; P04271: S100B; NbExp=3; IntAct=EBI-413628, EBI-458391;
CC P63000; Q01105: SET; NbExp=8; IntAct=EBI-413628, EBI-1053182;
CC P63000; Q7Z6J0: SH3RF1; NbExp=2; IntAct=EBI-413628, EBI-311339;
CC P63000; Q8TEJ3: SH3RF3; NbExp=6; IntAct=EBI-413628, EBI-7975674;
CC P63000; P43405-2: SYK; NbExp=3; IntAct=EBI-413628, EBI-25892332;
CC P63000; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-413628, EBI-17438286;
CC P63000; Q6P589: TNFAIP8L2; NbExp=2; IntAct=EBI-413628, EBI-9073209;
CC P63000; O60784-2: TOM1; NbExp=3; IntAct=EBI-413628, EBI-12117154;
CC P63000; Q9H9P5: UNKL; NbExp=2; IntAct=EBI-413628, EBI-7797561;
CC P63000; Q9Y6N9: USH1C; NbExp=3; IntAct=EBI-413628, EBI-954308;
CC P63000; Q9BVJ6: UTP14A; NbExp=3; IntAct=EBI-413628, EBI-473284;
CC P63000; P15498: VAV1; NbExp=2; IntAct=EBI-413628, EBI-625518;
CC P63000; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-413628, EBI-11141397;
CC P63000; P98170: XIAP; NbExp=3; IntAct=EBI-413628, EBI-517127;
CC P63000; Q98PK8: smc; Xeno; NbExp=5; IntAct=EBI-413628, EBI-12740386;
CC P63000-1; Q13153: PAK1; NbExp=3; IntAct=EBI-7212896, EBI-1307;
CC P63000-1; Q8TCU6: PREX1; NbExp=2; IntAct=EBI-7212896, EBI-1046542;
CC P63000-1; Q6P589: TNFAIP8L2; NbExp=6; IntAct=EBI-7212896, EBI-9073209;
CC P63000-1; O75962-4: TRIO; NbExp=2; IntAct=EBI-7212896, EBI-15915736;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1643658,
CC ECO:0000269|PubMed:22843693, ECO:0000269|PubMed:29074776}; Lipid-anchor
CC {ECO:0000269|PubMed:1903399}; Cytoplasmic side
CC {ECO:0000269|PubMed:1643658, ECO:0000269|PubMed:19948726}. Melanosome
CC {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:19948726,
CC ECO:0000269|PubMed:21693584}. Cytoplasm {ECO:0000269|PubMed:19948726,
CC ECO:0000269|PubMed:29074776}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P63001}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P63001}. Synapse {ECO:0000250|UniProtKB:Q6RUV5}.
CC Nucleus {ECO:0000269|PubMed:12551911}. Note=Inner surface of plasma
CC membrane possibly with attachment requiring prenylation of the C-
CC terminal cysteine (PubMed:1903399). Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV (PubMed:17081065). Found
CC in the ruffled border (a late endosomal-like compartment in the plasma
CC membrane) of bone-resorbing osteoclasts. Localizes to the lamellipodium
CC in a SH3RF1-dependent manner (By similarity). In macrophages,
CC cytoplasmic location increases upon CSF1 stimulation (By similarity).
CC Activation by GTP-binding promotes nuclear localization
CC (PubMed:12551911). {ECO:0000250|UniProtKB:P63001,
CC ECO:0000250|UniProtKB:Q6RUV5, ECO:0000269|PubMed:12551911,
CC ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:1903399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=Rac1A;
CC IsoId=P63000-1, P15154-1; Sequence=Displayed;
CC Name=B; Synonyms=Rac1B, Rac1ins;
CC IsoId=P63000-2, P15154-2; Sequence=VSP_005710;
CC -!- TISSUE SPECIFICITY: Isoform B is predominantly identified in skin and
CC epithelial tissues from the intestinal tract. Its expression is
CC elevated in colorectal tumors at various stages of neoplastic
CC progression, as compared to their respective adjacent tissues.
CC -!- DOMAIN: The effector region mediates interaction with DEF6.
CC {ECO:0000269|PubMed:17121847}.
CC -!- PTM: GTP-bound active form is ubiquitinated at Lys-147 by HACE1,
CC leading to its degradation by the proteasome.
CC {ECO:0000269|PubMed:18093184, ECO:0000269|PubMed:22036506,
CC ECO:0000269|PubMed:38332367}.
CC -!- PTM: Phosphorylated by AKT at Ser-71. {ECO:0000269|PubMed:10617634}.
CC -!- PTM: Ubiquitinated at Lys-166 in a FBXL19-mediated manner; leading to
CC proteasomal degradation. {ECO:0000269|PubMed:23512198}.
CC -!- PTM: (Microbial infection) AMPylation at Tyr-32 and Thr-35 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-32 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 Rac and leads to actin disassembly.
CC {ECO:0000269|PubMed:24141704}.
CC -!- PTM: (Microbial infection) Glucosylated at Thr-35 by C.difficile toxins
CC TcdA and TcdB in the colonic epithelium, and by P.sordellii toxin TcsL
CC in the vascular endothelium (PubMed:19744486, PubMed:24905543,
CC PubMed:7775453, PubMed:7777059, PubMed:8626575). Monoglucosylation
CC completely prevents the recognition of the downstream effector,
CC blocking the GTPases in their inactive form, leading to actin
CC cytoskeleton disruption and cell death, resulting in the loss of
CC colonic epithelial barrier function (PubMed:7775453, PubMed:7777059).
CC {ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:24905543,
CC ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059,
CC ECO:0000269|PubMed:8626575}.
CC -!- PTM: (Microbial infection) Glycosylated (O-GlcNAcylated) at Thr-35 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) Palmitoylated by the N-epsilon-fatty
CC acyltransferase F2 chain of V.cholerae toxin RtxA (PubMed:29074776).
CC Palmitoylation inhibits activation by guanine nucleotide exchange
CC factors (GEFs), preventing Rho GTPase signaling (PubMed:29074776).
CC {ECO:0000269|PubMed:29074776}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 48
CC (MRD48) [MIM:617751]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD48
CC patients manifest global developmental delay and moderate to severe
CC intellectual disability. {ECO:0000269|PubMed:28886345}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- CAUTION: The interaction between DSCAM, PAK1 and RAC1 has been
CC described. This article has been withdrawn by the authors.
CC {ECO:0000305|PubMed:15169762, ECO:0000305|PubMed:26048998}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ80485.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; M29870; AAA36537.1; -; mRNA.
DR EMBL; M31467; AAA36544.1; -; mRNA.
DR EMBL; AJ132694; CAA10732.1; -; mRNA.
DR EMBL; AJ132695; CAB53579.5; -; Genomic_DNA.
DR EMBL; AJ132695; CAA10733.6; -; Genomic_DNA.
DR EMBL; AF136373; AAD30547.1; -; mRNA.
DR EMBL; AY279384; AAQ16632.1; -; mRNA.
DR EMBL; AF498964; AAM21111.1; -; mRNA.
DR EMBL; BT007121; AAP35785.1; -; mRNA.
DR EMBL; DQ165078; AAZ80485.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC009412; AAS07511.1; -; Genomic_DNA.
DR EMBL; AC009412; AAS07512.1; -; Genomic_DNA.
DR EMBL; BC004247; AAH04247.1; -; mRNA.
DR EMBL; BC050687; AAH50687.1; -; mRNA.
DR EMBL; BC107748; AAI07749.1; -; mRNA.
DR CCDS; CCDS5348.1; -.
DR CCDS; CCDS5349.1; -. [P63000-2]
DR PIR; A34788; TVHUC1.
DR RefSeq; NP_008839.2; NM_006908.4. [P63000-1]
DR RefSeq; NP_061485.1; NM_018890.3. [P63000-2]
DR PDB; 1E96; X-ray; 2.40 A; A=2-192.
DR PDB; 1FOE; X-ray; 2.80 A; B/D/F/H=1-177.
DR PDB; 1G4U; X-ray; 2.30 A; R=1-184.
DR PDB; 1HE1; X-ray; 2.00 A; C/D=2-176.
DR PDB; 1HH4; X-ray; 2.70 A; A/B=2-192.
DR PDB; 1I4D; X-ray; 2.50 A; D=1-192.
DR PDB; 1I4L; X-ray; 2.70 A; D=1-192.
DR PDB; 1I4T; X-ray; 2.60 A; D=1-192.
DR PDB; 1MH1; X-ray; 1.38 A; A=2-184.
DR PDB; 1RYF; X-ray; 1.75 A; A/B=1-182.
DR PDB; 1RYH; X-ray; 1.75 A; A/B=1-182.
DR PDB; 2FJU; X-ray; 2.20 A; A=1-177.
DR PDB; 2H7V; X-ray; 2.60 A; A/B=1-184.
DR PDB; 2NZ8; X-ray; 2.00 A; A=1-177.
DR PDB; 2P2L; X-ray; 1.90 A; A/B/C=1-184.
DR PDB; 2RMK; NMR; -; A=1-192.
DR PDB; 2VRW; X-ray; 1.85 A; A=1-184.
DR PDB; 2WKP; X-ray; 1.90 A; A=4-180.
DR PDB; 2WKQ; X-ray; 1.60 A; A=4-180.
DR PDB; 2WKR; X-ray; 2.20 A; A=4-180.
DR PDB; 2YIN; X-ray; 2.70 A; C/D=1-177.
DR PDB; 3B13; X-ray; 3.01 A; B/D=1-177.
DR PDB; 3BJI; X-ray; 2.60 A; C/D=1-177.
DR PDB; 3RYT; X-ray; 3.58 A; C=1-177.
DR PDB; 3SBD; X-ray; 2.10 A; A/B=2-177.
DR PDB; 3SBE; X-ray; 2.60 A; A=2-177.
DR PDB; 3SU8; X-ray; 3.20 A; A=1-177.
DR PDB; 3SUA; X-ray; 4.39 A; A/B/C=1-177.
DR PDB; 3TH5; X-ray; 2.30 A; A/B=2-177.
DR PDB; 4GZL; X-ray; 2.00 A; A/B=2-177.
DR PDB; 4GZM; X-ray; 2.80 A; A/B=2-177.
DR PDB; 4YON; X-ray; 1.95 A; B=1-177.
DR PDB; 5FI0; X-ray; 3.28 A; B/D/F/H=1-192.
DR PDB; 5HZH; X-ray; 2.60 A; A=1-180.
DR PDB; 5N6O; X-ray; 2.59 A; A/B=2-177.
DR PDB; 5O33; X-ray; 1.64 A; A=1-177.
DR PDB; 5QQD; X-ray; 1.91 A; A=1-177.
DR PDB; 5QQE; X-ray; 1.95 A; A=1-177.
DR PDB; 5QQF; X-ray; 2.26 A; A=1-177.
DR PDB; 5QQG; X-ray; 2.23 A; A=1-177.
DR PDB; 5QQH; X-ray; 2.09 A; A=1-177.
DR PDB; 5QQI; X-ray; 2.08 A; A=1-177.
DR PDB; 5QQJ; X-ray; 1.90 A; A=1-177.
DR PDB; 5QQK; X-ray; 2.24 A; A=1-177.
DR PDB; 5QQL; X-ray; 2.25 A; A=1-177.
DR PDB; 5QQM; X-ray; 2.02 A; A=1-177.
DR PDB; 5QQN; X-ray; 2.26 A; A=1-177.
DR PDB; 5QU9; X-ray; 2.00 A; A=1-177.
DR PDB; 6AGP; NMR; -; A=1-181.
DR PDB; 6BC1; X-ray; 2.90 A; A/B=2-177.
DR PDB; 6TGC; EM; 4.10 A; C/F=1-192.
DR PDB; 6X1G; X-ray; 1.60 A; B/D=1-177.
DR PDB; 7AJK; X-ray; 3.10 A; BBB=2-177.
DR PDB; 7DPA; EM; 3.80 A; B/E=1-177.
DR PDB; 7SJ4; EM; 2.86 A; B=1-192.
DR PDB; 7USD; EM; 3.00 A; F=1-188.
DR PDB; 7USE; EM; 3.00 A; F/G=1-188.
DR PDB; 8I5V; X-ray; 1.73 A; B=1-177.
DR PDB; 8I5W; X-ray; 2.43 A; B=1-177.
DR PDB; 8Q0N; EM; 4.20 A; C=1-192.
DR PDB; 8WEJ; EM; 2.79 A; E=1-192.
DR PDB; 8ZJ2; EM; 4.66 A; C/G=1-177.
DR PDB; 8ZJI; EM; 4.23 A; C/F=1-177.
DR PDB; 8ZJJ; EM; 4.23 A; C/F=1-177.
DR PDB; 8ZJK; EM; 4.23 A; C/F=1-177.
DR PDB; 8ZJL; EM; 4.31 A; C/F=1-177.
DR PDB; 8ZJM; EM; 4.52 A; C/F=1-177.
DR PDBsum; 1E96; -.
DR PDBsum; 1FOE; -.
DR PDBsum; 1G4U; -.
DR PDBsum; 1HE1; -.
DR PDBsum; 1HH4; -.
DR PDBsum; 1I4D; -.
DR PDBsum; 1I4L; -.
DR PDBsum; 1I4T; -.
DR PDBsum; 1MH1; -.
DR PDBsum; 1RYF; -.
DR PDBsum; 1RYH; -.
DR PDBsum; 2FJU; -.
DR PDBsum; 2H7V; -.
DR PDBsum; 2NZ8; -.
DR PDBsum; 2P2L; -.
DR PDBsum; 2RMK; -.
DR PDBsum; 2VRW; -.
DR PDBsum; 2WKP; -.
DR PDBsum; 2WKQ; -.
DR PDBsum; 2WKR; -.
DR PDBsum; 2YIN; -.
DR PDBsum; 3B13; -.
DR PDBsum; 3BJI; -.
DR PDBsum; 3RYT; -.
DR PDBsum; 3SBD; -.
DR PDBsum; 3SBE; -.
DR PDBsum; 3SU8; -.
DR PDBsum; 3SUA; -.
DR PDBsum; 3TH5; -.
DR PDBsum; 4GZL; -.
DR PDBsum; 4GZM; -.
DR PDBsum; 4YON; -.
DR PDBsum; 5FI0; -.
DR PDBsum; 5HZH; -.
DR PDBsum; 5N6O; -.
DR PDBsum; 5O33; -.
DR PDBsum; 5QQD; -.
DR PDBsum; 5QQE; -.
DR PDBsum; 5QQF; -.
DR PDBsum; 5QQG; -.
DR PDBsum; 5QQH; -.
DR PDBsum; 5QQI; -.
DR PDBsum; 5QQJ; -.
DR PDBsum; 5QQK; -.
DR PDBsum; 5QQL; -.
DR PDBsum; 5QQM; -.
DR PDBsum; 5QQN; -.
DR PDBsum; 5QU9; -.
DR PDBsum; 6AGP; -.
DR PDBsum; 6BC1; -.
DR PDBsum; 6TGC; -.
DR PDBsum; 6X1G; -.
DR PDBsum; 7AJK; -.
DR PDBsum; 7DPA; -.
DR PDBsum; 7SJ4; -.
DR PDBsum; 7USD; -.
DR PDBsum; 7USE; -.
DR PDBsum; 8I5V; -.
DR PDBsum; 8I5W; -.
DR PDBsum; 8Q0N; -.
DR PDBsum; 8WEJ; -.
DR PDBsum; 8ZJ2; -.
DR PDBsum; 8ZJI; -.
DR PDBsum; 8ZJJ; -.
DR PDBsum; 8ZJK; -.
DR PDBsum; 8ZJL; -.
DR PDBsum; 8ZJM; -.
DR AlphaFoldDB; P63000; -.
DR BMRB; P63000; -.
DR EMDB; EMD-10498; -.
DR EMDB; EMD-18056; -.
DR EMDB; EMD-25153; -.
DR EMDB; EMD-26733; -.
DR EMDB; EMD-26734; -.
DR EMDB; EMD-30802; -.
DR EMDB; EMD-37593; -.
DR EMDB; EMD-60136; -.
DR EMDB; EMD-60146; -.
DR EMDB; EMD-60147; -.
DR EMDB; EMD-60148; -.
DR EMDB; EMD-60149; -.
DR EMDB; EMD-60150; -.
DR SMR; P63000; -.
DR BioGRID; 111817; 1020.
DR ComplexPortal; CPX-1017; Phagocyte NADPH oxidase complex, RAC1 variant.
DR CORUM; P63000; -.
DR DIP; DIP-29260N; -.
DR IntAct; P63000; 277.
DR MINT; P63000; -.
DR STRING; 9606.ENSP00000348461; -.
DR BindingDB; P63000; -.
DR ChEMBL; CHEMBL6094; -.
DR DrugBank; DB00993; Azathioprine.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugCentral; P63000; -.
DR GlyCosmos; P63000; 2 sites, No reported glycans.
DR GlyGen; P63000; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P63000; -.
DR MetOSite; P63000; -.
DR PhosphoSitePlus; P63000; -.
DR SwissPalm; P63000; -.
DR BioMuta; RAC1; -.
DR DMDM; 51702787; -.
DR jPOST; P63000; -.
DR MassIVE; P63000; -.
DR PaxDb; 9606-ENSP00000348461; -.
DR PeptideAtlas; P63000; -.
DR ProteomicsDB; 57467; -.
DR ProteomicsDB; 57468; -. [P63000-2]
DR Pumba; P63000; -.
DR Antibodypedia; 4545; 869 antibodies from 41 providers.
DR CPTC; P63000; 2 antibodies.
DR DNASU; 5879; -.
DR Ensembl; ENST00000348035.9; ENSP00000258737.7; ENSG00000136238.20. [P63000-1]
DR Ensembl; ENST00000356142.4; ENSP00000348461.4; ENSG00000136238.20. [P63000-2]
DR GeneID; 5879; -.
DR KEGG; hsa:5879; -.
DR MANE-Select; ENST00000348035.9; ENSP00000258737.7; NM_006908.5; NP_008839.2.
DR UCSC; uc003spw.4; human.
DR AGR; HGNC:9801; -.
DR CTD; 5879; -.
DR DisGeNET; 5879; -.
DR GeneCards; RAC1; -.
DR HGNC; HGNC:9801; RAC1.
DR HPA; ENSG00000136238; Low tissue specificity.
DR MalaCards; RAC1; -.
DR MIM; 602048; gene.
DR MIM; 617751; phenotype.
DR neXtProt; NX_P63000; -.
DR OpenTargets; ENSG00000136238; -.
DR Orphanet; 500159; Microcephaly-corpus callosum and cerebellar vermis hypoplasia-facial dysmorphism-intellectual disability syndrom.
DR PharmGKB; PA34162; -.
DR VEuPathDB; HostDB:ENSG00000136238; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000153500; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P63000; -.
DR OMA; PFCDVFL; -.
DR OrthoDB; 8953216at2759; -.
DR PhylomeDB; P63000; -.
DR TreeFam; TF101109; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P63000; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-1433557; Signaling by SCF-KIT.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-164944; Nef and signal transduction.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-2424491; DAP12 signaling.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-3928664; Ephrin signaling.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-HSA-418885; DCC mediated attractive signaling.
DR Reactome; R-HSA-428540; Activation of RAC1.
DR Reactome; R-HSA-428543; Inactivation of CDC42 and RAC1.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
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-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9032759; NTRK2 activates RAC1.
DR Reactome; R-HSA-9032845; Activated NTRK2 signals through CDK5.
DR Reactome; R-HSA-9619229; Activation of RAC1 downstream of NMDARs.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P63000; -.
DR SIGNOR; P63000; -.
DR BioGRID-ORCS; 5879; 622 hits in 1180 CRISPR screens.
DR ChiTaRS; RAC1; human.
DR EvolutionaryTrace; P63000; -.
DR GeneWiki; RAC1; -.
DR GenomeRNAi; 5879; -.
DR Pharos; P63000; Tbio.
DR PRO; PR:P63000; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P63000; protein.
DR Bgee; ENSG00000136238; Expressed in esophagus squamous epithelium and 210 other cell types or tissues.
DR ExpressionAtlas; P63000; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
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; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043020; C:NADPH oxidase complex; NAS:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; IDA:FlyBase.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
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:1990606; F:membrane scission GTPase motor activity; IEA:RHEA.
DR GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; ISS:UniProtKB.
DR GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; TAS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IDA:UniProt.
DR GO; GO:0048870; P:cell motility; IDA:UniProtKB.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; NAS:BHF-UCL.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IMP:CAFA.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0051668; P:localization within membrane; IMP:BHF-UCL.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IDA:BHF-UCL.
DR GO; GO:0032707; P:negative regulation of interleukin-23 production; IDA:BHF-UCL.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; TAS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; IMP:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IGI:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:CAFA.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; TAS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
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:0008361; P:regulation of cell size; IMP:UniProtKB.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; TAS:BHF-UCL.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IGI:CAFA.
DR GO; GO:1902622; P:regulation of neutrophil migration; IBA:GO_Central.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISS:ARUK-UCL.
DR GO; GO:0060263; P:regulation of respiratory burst; IDA:BHF-UCL.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IGI:CAFA.
DR GO; GO:0045730; P:respiratory burst; NAS:ComplexPortal.
DR GO; GO:0009611; P:response to wounding; TAS:ProtInc.
DR GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
DR GO; GO:0031529; P:ruffle organization; IDA:MGI.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase-mediated signal transduction; IMP:BHF-UCL.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; IMP:BHF-UCL.
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 CDD; cd01871; Rac1_like; 1.
DR FunFam; 3.40.50.300:FF:000088; Ras-related C3 botulinum toxin substrate 1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR IDEAL; IID00312; -.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Disease variant; Glycoprotein; GTP-binding; Hydrolase;
KW Intellectual disability; Isopeptide bond; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein;
KW Prenylation; Proteomics identification; Reference proteome; Synapse;
KW Ubl conjugation.
FT CHAIN 1..189
FT /note="Ras-related C3 botulinum toxin substrate 1"
FT /id="PRO_0000042036"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:1903399"
FT /id="PRO_0000042037"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT MOTIF 179..188
FT /note="Polybasic region; required for nuclear import"
FT /evidence="ECO:0000269|PubMed:12551911"
FT BINDING 12
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:38332367,
FT ECO:0007744|PDB:8Q0N"
FT BINDING 13
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0000269|PubMed:38355798,
FT ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP,
FT ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR,
FT ECO:0007744|PDB:8Q0N, ECO:0007744|PDB:8WEJ"
FT BINDING 14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0007744|PDB:1E96,
FT ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ,
FT ECO:0007744|PDB:2WKR, ECO:0007744|PDB:8Q0N"
FT BINDING 15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0007744|PDB:1E96,
FT ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ,
FT ECO:0007744|PDB:2WKR, ECO:0007744|PDB:8Q0N"
FT BINDING 16
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0000269|PubMed:38355798,
FT ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP,
FT ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR,
FT ECO:0007744|PDB:8Q0N, ECO:0007744|PDB:8WEJ"
FT BINDING 17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0000269|PubMed:38355798,
FT ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP,
FT ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR,
FT ECO:0007744|PDB:8Q0N, ECO:0007744|PDB:8WEJ"
FT BINDING 18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0000269|PubMed:38355798,
FT ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP,
FT ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR,
FT ECO:0007744|PDB:8Q0N, ECO:0007744|PDB:8WEJ"
FT BINDING 31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0007744|PDB:1E96,
FT ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ,
FT ECO:0007744|PDB:2WKR, ECO:0007744|PDB:8Q0N"
FT BINDING 32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0007744|PDB:1E96,
FT ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ,
FT ECO:0007744|PDB:2WKR, ECO:0007744|PDB:8Q0N"
FT BINDING 34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0007744|PDB:1E96,
FT ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ,
FT ECO:0007744|PDB:2WKR, ECO:0007744|PDB:8Q0N"
FT BINDING 35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0000269|PubMed:38355798,
FT ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP,
FT ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR,
FT ECO:0007744|PDB:8Q0N, ECO:0007744|PDB:8WEJ"
FT BINDING 59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:38332367,
FT ECO:0007744|PDB:8Q0N"
FT BINDING 60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP,
FT ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR"
FT BINDING 116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0007744|PDB:1E96,
FT ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ,
FT ECO:0007744|PDB:2WKR, ECO:0007744|PDB:8Q0N"
FT BINDING 118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0007744|PDB:1E96,
FT ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ,
FT ECO:0007744|PDB:2WKR, ECO:0007744|PDB:8Q0N"
FT BINDING 119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:38332367,
FT ECO:0007744|PDB:8Q0N"
FT BINDING 158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:38355798,
FT ECO:0007744|PDB:8WEJ"
FT BINDING 159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0000269|PubMed:38355798,
FT ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP,
FT ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR,
FT ECO:0007744|PDB:8Q0N, ECO:0007744|PDB:8WEJ"
FT BINDING 160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11090627,
FT ECO:0000269|PubMed:38332367, ECO:0000269|PubMed:38355798,
FT ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP,
FT ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR,
FT ECO:0007744|PDB:8Q0N, ECO:0007744|PDB:8WEJ"
FT MOD_RES 32
FT /note="(Microbial infection) O-AMP-tyrosine; by Haemophilus
FT IbpA; alternate"
FT /evidence="ECO:0000269|PubMed:19362538"
FT MOD_RES 35
FT /note="(Microbial infection) O-AMP-threonine; by Vibrio
FT VopS"
FT /evidence="ECO:0000269|PubMed:19039103"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10617634"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P61585"
FT LIPID 183
FT /note="(Microbial infection) N6-palmitoyl lysine"
FT /evidence="ECO:0000269|PubMed:29074776"
FT LIPID 184
FT /note="(Microbial infection) N6-palmitoyl lysine"
FT /evidence="ECO:0000269|PubMed:29074776"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1903399"
FT CARBOHYD 32
FT /note="(Microbial infection) O-linked (GlcNAc) tyrosine; by
FT Photorhabdus PAU_02230; alternate"
FT /evidence="ECO:0000269|PubMed:24141704"
FT CARBOHYD 35
FT /note="(Microbial infection) O-alpha-linked (GlcNAc)
FT threonine; by C.novyi toxin TcdA; alternate"
FT /evidence="ECO:0000269|PubMed:8810274"
FT CARBOHYD 35
FT /note="(Microbial infection) O-linked (Glc) threonine; by
FT C.difficile toxins TcdA and TcdB, and by P.sordellii toxin
FT TcsL; alternate"
FT /evidence="ECO:0000269|PubMed:19744486,
FT ECO:0000269|PubMed:24905543, ECO:0000269|PubMed:7775453,
FT ECO:0000269|PubMed:7777059"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18093184,
FT ECO:0000269|PubMed:38332367"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23512198"
FT VAR_SEQ 75
FT /note="T -> TVGETYGKDITSRGKDKPIA (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10597294,
FT ECO:0000303|PubMed:11062023, ECO:0000303|Ref.5"
FT /id="VSP_005710"
FT VARIANT 18
FT /note="C -> Y (in MRD48; decreased substrate
FT adhesion-dependent cell spreading; dominant-negative
FT effect; reduced neuronal proliferation;
FT dbSNP:rs1554263326)"
FT /evidence="ECO:0000269|PubMed:28886345"
FT /id="VAR_080454"
FT VARIANT 26
FT /note="N -> D (in dbSNP:rs2115193158)"
FT /id="VAR_014540"
FT VARIANT 28
FT /note="F -> L (in dbSNP:rs2115193183)"
FT /id="VAR_014541"
FT VARIANT 39
FT /note="N -> S (in MRD48; decreased substrate
FT adhesion-dependent cell spreading; dominant-negative
FT effect; reduced neuronal proliferation;
FT dbSNP:rs1554263624)"
FT /evidence="ECO:0000269|PubMed:28886345"
FT /id="VAR_080455"
FT VARIANT 51
FT /note="V -> L (in MRD48; uncertain significance;
FT dbSNP:rs1554263625)"
FT /evidence="ECO:0000269|PubMed:28886345"
FT /id="VAR_080456"
FT VARIANT 51
FT /note="V -> M (in MRD48; decreased substrate
FT adhesion-dependent cell spreading; weak dominant-negative
FT effect; dbSNP:rs1554263625)"
FT /evidence="ECO:0000269|PubMed:28886345"
FT /id="VAR_080457"
FT VARIANT 59
FT /note="A -> T (in dbSNP:rs5837)"
FT /id="VAR_014542"
FT VARIANT 63
FT /note="D -> G (in dbSNP:rs5831)"
FT /id="VAR_014543"
FT VARIANT 64
FT /note="Y -> D (in MRD48; increased substrate
FT adhesion-dependent cell spreading; constitutively active;
FT dbSNP:rs1554263626)"
FT /evidence="ECO:0000269|PubMed:28886345"
FT /id="VAR_080458"
FT VARIANT 73
FT /note="P -> L (in MRD48; decreased substrate
FT adhesion-dependent cell spreading; weak dominant-negative
FT effect; dbSNP:rs2115201441)"
FT /evidence="ECO:0000269|PubMed:28886345"
FT /id="VAR_080459"
FT VARIANT 93
FT /note="V -> G (in dbSNP:rs5826)"
FT /id="VAR_014545"
FT VARIANT 93
FT /note="V -> I (in dbSNP:rs5825)"
FT /id="VAR_014544"
FT VARIANT 108
FT /note="T -> I (in dbSNP:rs2115217353)"
FT /id="VAR_014546"
FT VARIANT 130
FT /note="K -> R (in dbSNP:rs5828)"
FT /id="VAR_014547"
FT VARIANT 133
FT /note="K -> E (in dbSNP:rs5835)"
FT /id="VAR_014548"
FT VARIANT 135
FT /note="T -> I (in dbSNP:rs11540455)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_033303"
FT VARIANT 157
FT /note="C -> Y (in MRD48; decreased substrate
FT adhesion-dependent cell spreading; weak dominant-negative
FT effect; dbSNP:rs1554264268)"
FT /evidence="ECO:0000269|PubMed:28886345"
FT /id="VAR_080460"
FT VARIANT 180
FT /note="P -> S (in dbSNP:rs16063)"
FT /id="VAR_014549"
FT VARIANT 182
FT /note="V -> E (in dbSNP:rs5836)"
FT /id="VAR_014550"
FT MUTAGEN 12
FT /note="G->V: Constitutively active. Interacts with PARD6
FT proteins. Increases nuclear localization and up-regulates
FT transcriptional activity of NR3C2. Doesn't interact with
FT CYRIB. Increases interaction with GARRE1."
FT /evidence="ECO:0000269|PubMed:11260256,
FT ECO:0000269|PubMed:19029984, ECO:0000269|PubMed:30250061,
FT ECO:0000269|PubMed:31871319"
FT MUTAGEN 17
FT /note="T->N: Constitutively inactivated. Abolishes
FT interaction with PARD6 proteins. No effect on NR3C2
FT transcriptional activity. No interaction with PPP5C.
FT Doesn't activate PPP5C phosphatase activity and translocate
FT PPP5C to the plasma membrane. Doesn't interact with CYRIB."
FT /evidence="ECO:0000269|PubMed:11260256,
FT ECO:0000269|PubMed:19029984, ECO:0000269|PubMed:19948726,
FT ECO:0000269|PubMed:30250061"
FT MUTAGEN 30
FT /note="G->V: No interaction with PPP5C; when associated
FT with L-61. Translocates to the plasma membrane; also when
FT associated with L-61."
FT /evidence="ECO:0000269|PubMed:19948726"
FT MUTAGEN 32
FT /note="Y->F: Abolishes AMPylation by Haemophilus IbpA."
FT /evidence="ECO:0000269|PubMed:19362538"
FT MUTAGEN 35
FT /note="T->A: Abolishes AMPylation by Vibrio VopS."
FT /evidence="ECO:0000269|PubMed:19039103,
FT ECO:0000269|PubMed:19948726"
FT MUTAGEN 35
FT /note="T->S: No interaction with PPP5C; when associated
FT with L-61. Translocates to the plasma membrane; also when
FT associated with L-61."
FT /evidence="ECO:0000269|PubMed:19039103,
FT ECO:0000269|PubMed:19948726"
FT MUTAGEN 37
FT /note="F->A: Strongly reduced interaction with PLCB2."
FT /evidence="ECO:0000269|PubMed:17115053"
FT MUTAGEN 56
FT /note="W->A: Strongly reduced interaction with PLCB2."
FT /evidence="ECO:0000269|PubMed:17115053"
FT MUTAGEN 61
FT /note="Q->L: Constitutively active. Interacts with PARD6
FT proteins. Interacts with PPP5C, activates its phosphatase
FT activity and translocates PPP5C to the plasma membrane. No
FT effect on interaction with RAPH1. Interacts with CYRIB. No
FT interaction with PPP5C; when associated with V-30 or S-35.
FT Translocates to the plasma membrane; also when associated
FT with V-30 or S-35."
FT /evidence="ECO:0000269|PubMed:10954424,
FT ECO:0000269|PubMed:18499456, ECO:0000269|PubMed:19948726,
FT ECO:0000269|PubMed:29074776, ECO:0000269|PubMed:30250061,
FT ECO:0000269|PubMed:38332367"
FT MUTAGEN 67
FT /note="L->A: Strongly reduced interaction with PLCB2."
FT /evidence="ECO:0000269|PubMed:17115053"
FT MUTAGEN 70
FT /note="L->A: Strongly reduced interaction with PLCB2."
FT /evidence="ECO:0000269|PubMed:17115053"
FT MUTAGEN 71
FT /note="S->A: Loss of AKT-mediated phosphorylation and
FT FBXL19-induced polyubiquitination."
FT /evidence="ECO:0000269|PubMed:10617634,
FT ECO:0000269|PubMed:23512198"
FT MUTAGEN 166
FT /note="K->R: Loss of FBXL19-induced polyubiquitination."
FT /evidence="ECO:0000269|PubMed:23512198"
FT MUTAGEN 183..188
FT /note="KKRKRK->AARARA: In 4KA mutant; abolished
FT palmitoylation by the V.cholerae toxin RtxA."
FT /evidence="ECO:0000269|PubMed:29074776"
FT MUTAGEN 183
FT /note="K->A: Slightly decreased palmitoylation by the
FT V.cholerae toxin RtxA."
FT /evidence="ECO:0000269|PubMed:29074776"
FT MUTAGEN 184
FT /note="K->A: Slightly decreased palmitoylation by the
FT V.cholerae toxin RtxA."
FT /evidence="ECO:0000269|PubMed:29074776"
FT MUTAGEN 185..187
FT /note="RKR->AKA: In 2RA mutant; does not affect
FT palmitoylation by the V.cholerae toxin RtxA."
FT /evidence="ECO:0000269|PubMed:29074776"
FT MUTAGEN 186
FT /note="K->A: Decreased palmitoylation by the V.cholerae
FT toxin RtxA."
FT /evidence="ECO:0000269|PubMed:29074776"
FT MUTAGEN 188
FT /note="K->A: Decreased palmitoylation by the V.cholerae
FT toxin RtxA."
FT /evidence="ECO:0000269|PubMed:29074776"
FT CONFLICT 192
FT /note="Missing (in Ref. 2; AAA36544)"
FT /evidence="ECO:0000305"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6X1G"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:8I5V"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1MH1"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1MH1"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1MH1"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:7USE"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:1MH1"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6X1G"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:1MH1"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1MH1"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1MH1"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:1MH1"
FT MOD_RES P63000-2:71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 192 AA; 21450 MW; ACEDF83A45E5EA67 CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR
DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSAL TQRGLKTVFD EAIRAVLCPP
PVKKRKRKCL LL
//