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Ras-related C3 botulinum toxin substrate 1 (Cell migration-inducing gene 5 protein) (Ras-like protein TC25) (p21-Rac1)

 RAC1_HUMAN              Reviewed;         192 AA.
P63000; O95501; P15154; Q3Y4D3; Q5JAA8; Q9BTB4;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 1.
22-NOV-2017, entry version 173.
RecName: Full=Ras-related C3 botulinum toxin substrate 1;
AltName: Full=Cell migration-inducing gene 5 protein;
AltName: Full=Ras-like protein TC25;
AltName: Full=p21-Rac1;
Flags: Precursor;
Name=RAC1; Synonyms=TC25; ORFNames=MIG5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=2674130;
Didsbury J., Weber R.F., Bokoch G.M., Evans T., Snyderman R.;
"Rac, a novel ras-related family of proteins that are botulinum toxin
substrates.";
J. Biol. Chem. 264:16378-16382(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=2108320; DOI=10.1128/MCB.10.4.1793;
Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.;
"Characterization of four novel ras-like genes expressed in a human
teratocarcinoma cell line.";
Mol. Cell. Biol. 10:1793-1798(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B).
PubMed=11062023; DOI=10.1006/bbrc.2000.3743;
Matos P., Skaug J., Marques B., Beck S., Verissimo F., Gespach C.,
Boavida M.G., Scherer S.W., Jordan P.;
"Small GTPase Rac1: structure, localization, and expression of the
human gene.";
Biochem. Biophys. Res. Commun. 277:741-751(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
TISSUE=Colon, and Skin;
PubMed=10597294; DOI=10.1038/sj.onc.1203233;
Jordan P., Brazao R., Boavida M.G., Gespach C., Chastre E.;
"Cloning of a novel human Rac1b splice variant with increased
expression in colorectal tumors.";
Oncogene 18:6835-6839(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Schnelzer A., Knaus U., Prechtel D., Dehne K., Harbeck N., Gerhard M.,
Schmitt M., Lengyel E.;
"Mutations and altered expression of Rac1 in human breast cancer
-- characterization of a new Rac1 isoform, Rac1ins.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Kim J.W.;
"Identification of a human migration-inducing gene.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT
ILE-135.
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Pancreas, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
ISOPRENYLATION AT CYS-189.
PubMed=1903399;
Kinsella B.T., Erdman R.A., Maltese W.A.;
"Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins
encoded by rac1, rac2, and ralA.";
J. Biol. Chem. 266:9786-9794(1991).
[13]
FUNCTION.
PubMed=1643658; DOI=10.1016/0092-8674(92)90164-8;
Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., Hall A.;
"The small GTP-binding protein rac regulates growth factor-induced
membrane ruffling.";
Cell 70:401-410(1992).
[14]
INTERACTION WITH RALBP1.
PubMed=7673236; DOI=10.1074/jbc.270.38.22473;
Jullien-Flores V., Dorseuil O., Romero F., Letourneur F.,
Saragosti S., Berger R., Tavitian A., Gacon G., Camonis J.H.;
"Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with
CDC42/Rac GTPase-activating protein activity.";
J. Biol. Chem. 270:22473-22477(1995).
[15]
FUNCTION, AND INTERACTION WITH PKN2.
PubMed=9121475; DOI=10.1128/MCB.17.4.2247;
Vincent S., Settleman J.;
"The PRK2 kinase is a potential effector target of both Rho and Rac
GTPases and regulates actin cytoskeletal organization.";
Mol. Cell. Biol. 17:2247-2256(1997).
[16]
INTERACTION WITH ARHGEF2.
PubMed=9857026; DOI=10.1074/jbc.273.52.34954;
Ren Y., Li R., Zheng Y., Busch H.;
"Cloning and characterization of GEF-H1, a microtubule-associated
guanine nucleotide exchange factor for Rac and Rho GTPases.";
J. Biol. Chem. 273:34954-34960(1998).
[17]
INTERACTION WITH DOCK2.
PubMed=10559471; DOI=10.1016/S0167-4889(99)00133-0;
Nishihara H., Kobayashi S., Hashimoto Y., Ohba F., Mochizuki N.,
Kurata T., Nagashima K., Matsuda M.;
"Non-adherent cell-specific expression of DOCK2, a member of the human
CDM-family proteins.";
Biochim. Biophys. Acta 1452:179-187(1999).
[18]
INTERACTION WITH PARD6A, AND MUTAGENESIS OF GLN-61.
PubMed=10954424;
Johansson A.-S., Driessens M., Aspenstroem P.;
"The mammalian homologue of the Caenorhabditis elegans polarity
protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and
Rac1.";
J. Cell Sci. 113:3267-3275(2000).
[19]
INTERACTION WITH BAIAP2.
PubMed=11130076; DOI=10.1038/35047107;
Miki H., Yamaguchi H., Suetsugu S., Takenawa T.;
"IRSp53 is an essential intermediate between Rac and WAVE in the
regulation of membrane ruffling.";
Nature 408:732-735(2000).
[20]
INTERACTION WITH PLXNB1.
PubMed=11035813; DOI=10.1073/pnas.220421797;
Vikis H.G., Li W., He Z., Guan K.-L.;
"The semaphorin receptor plexin-B1 specifically interacts with active
Rac in a ligand-dependent manner.";
Proc. Natl. Acad. Sci. U.S.A. 97:12457-12462(2000).
[21]
INTERACTION WITH PARD6A; PARD6B AND PARD6G; PRKCI AND PRKCZ, AND
MUTAGENESIS OF GLY-12 AND THR-17.
PubMed=11260256; DOI=10.1046/j.1365-2443.2001.00404.x;
Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.;
"Human homologues of the Caenorhabditis elegans cell polarity protein
PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to
atypical protein kinase C.";
Genes Cells 6:107-119(2001).
[22]
ACTIVATION BY PREX1.
PubMed=11955434; DOI=10.1016/S0092-8674(02)00663-3;
Welch H.C.E., Coadwell W.J., Ellson C.D., Ferguson G.J., Andrews S.R.,
Erdjument-Bromage H., Tempst P., Hawkins P.T., Stephens L.R.;
"P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-
nucleotide exchange factor for Rac.";
Cell 108:809-821(2002).
[23]
INTERACTION WITH ITGB1BP1.
PubMed=11807099; DOI=10.1083/jcb.200108030;
Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F.,
Silengo L., Eva A., Tarone G.;
"The integrin cytoplasmic domain-associated protein ICAP-1 binds and
regulates Rho family GTPases during cell spreading.";
J. Cell Biol. 156:377-387(2002).
[24]
SUBUNIT OF A COMPLEX CONTAINING ELMO1 AND DOCK1.
PubMed=12134158; DOI=10.1038/ncb824;
Brugnera E., Haney L., Grimsley C., Lu M., Walk S.F.,
Tosello-Trampont A.-C., Macara I.G., Madhani H., Fink G.R.,
Ravichandran K.S.;
"Unconventional Rac-GEF activity is mediated through the Dock180-ELMO
complex.";
Nat. Cell Biol. 4:574-582(2002).
[25]
INTERACTION WITH NOXA1.
PubMed=12716910; DOI=10.1074/jbc.M212856200;
Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H.,
Sumimoto H.;
"Novel human homologues of p47phox and p67phox participate in
activation of superoxide-producing NADPH oxidases.";
J. Biol. Chem. 278:25234-25246(2003).
[26]
INTERACTION WITH USP6.
PubMed=12612085; DOI=10.1128/MCB.23.6.2151-2161.2003;
Masuda-Robens J.M., Kutney S.N., Qi H., Chou M.M.;
"The TRE17 oncogene encodes a component of a novel effector pathway
for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling.";
Mol. Cell. Biol. 23:2151-2161(2003).
[27]
INTERACTION WITH DSCAM.
PubMed=15169762; DOI=10.1074/jbc.M401878200;
Li W., Guan K.L.;
"The Down syndrome cell adhesion molecule (DSCAM) interacts with and
activates Pak.";
J. Biol. Chem. 279:32824-32831(2004).
[28]
INTERACTION WITH S100A8 AND CALPROTECTIN.
PubMed=15642721; DOI=10.1096/fj.04-2377fje;
Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C.,
Doussiere J.;
"The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase
activation by interaction with p67phox and Rac-2.";
FASEB J. 19:467-469(2005).
[29]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[30]
INTERACTION WITH DOCK7.
PubMed=16982419; DOI=10.1016/j.neuron.2006.07.020;
Watabe-Uchida M., John K.A., Janas J.A., Newey S.E., Van Aelst L.;
"The Rac activator DOCK7 regulates neuronal polarity through local
phosphorylation of stathmin/Op18.";
Neuron 51:727-739(2006).
[31]
INTERACTION WITH DEF6, AND DOMAIN.
PubMed=17121847; DOI=10.1074/jbc.M605153200;
Oka T., Ihara S., Fukui Y.;
"Cooperation of DEF6 with activated Rac in regulating cell
morphology.";
J. Biol. Chem. 282:2011-2018(2007).
[32]
INTERACTION WITH BAIAP2L1.
PubMed=17430976; DOI=10.1242/jcs.001776;
Millard T.H., Dawson J., Machesky L.M.;
"Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator
with distinct filament bundling properties.";
J. Cell Sci. 120:1663-1672(2007).
[33]
INTERACTION WITH SPATA13.
PubMed=17145773; DOI=10.1128/MCB.01608-06;
Hamann M.J., Lubking C.M., Luchini D.N., Billadeau D.D.;
"Asef2 functions as a Cdc42 exchange factor and is stimulated by the
release of an autoinhibitory module from a concealed C-terminal
activation element.";
Mol. Cell. Biol. 27:1380-1393(2007).
[34]
INTERACTION WITH RAPH1, AND MUTAGENESIS OF GLN-61.
PubMed=18499456; DOI=10.1016/j.cub.2008.04.050;
Quinn C.C., Pfeil D.S., Wadsworth W.G.;
"CED-10/Rac1 mediates axon guidance by regulating the asymmetric
distribution of MIG-10/lamellipodin.";
Curr. Biol. 18:808-813(2008).
[35]
UBIQUITINATION AT LYS-147.
PubMed=18093184; DOI=10.1111/j.1742-4658.2007.06209.x;
Visvikis O., Lores P., Boyer L., Chardin P., Lemichez E., Gacon G.;
"Activated Rac1, but not the tumorigenic variant Rac1b, is
ubiquitinated on Lys 147 through a JNK-regulated process.";
FEBS J. 275:386-396(2008).
[36]
FUNCTION, AND MUTAGENESIS OF GLY-12 AND THR-17.
PubMed=19029984; DOI=10.1038/nm.1879;
Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H.,
Tanaka H., Miyoshi J., Takai Y., Fujita T.;
"Modification of mineralocorticoid receptor function by Rac1 GTPase:
implication in proteinuric kidney disease.";
Nat. Med. 14:1370-1376(2008).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 (ISOFORM B), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[38]
FUNCTION.
PubMed=19934221; DOI=10.1242/jcs.053728;
Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L.,
Webb D.J.;
"The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin
dynamics and thereby regulate cell migration.";
J. Cell Sci. 122:4535-4546(2009).
[39]
INTERACTION WITH MTSS1L.
PubMed=20875796; DOI=10.1016/j.bbrc.2010.09.087;
Zheng D., Niu S., Yu D., Zhan X.H., Zeng X., Cui B., Chen Y., Yoon J.,
Martin S.S., Lu X., Zhan X.;
"Abba promotes PDGF-mediated membrane ruffling through activation of
the small GTPase Rac1.";
Biochem. Biophys. Res. Commun. 401:527-532(2010).
[40]
INTERACTION WITH UNKL.
PubMed=20148946; DOI=10.1111/j.1742-4658.2010.07575.x;
Lores P., Visvikis O., Luna R., Lemichez E., Gacon G.;
"The SWI/SNF protein BAF60b is ubiquitinated through a signalling
process involving Rac GTPase and the RING finger protein Unkempt.";
FEBS J. 277:1453-1464(2010).
[41]
FUNCTION, AND INTERACTION WITH ITGB4.
PubMed=19403692; DOI=10.1091/mbc.E09-01-0051;
Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.;
"BPAG1e maintains keratinocyte polarity through beta4 integrin-
mediated modulation of Rac1 and cofilin activities.";
Mol. Biol. Cell 20:2954-2962(2009).
[42]
AMPYLATION AT TYR-32 (MICROBIAL INFECTION), IDENTIFICATION BY MASS
SPECTROMETRY, AND MUTAGENESIS OF TYR-32.
PubMed=19362538; DOI=10.1016/j.molcel.2009.03.008;
Worby C.A., Mattoo S., Kruger R.P., Corbeil L.B., Koller A.,
Mendez J.C., Zekarias B., Lazar C., Dixon J.E.;
"The fic domain: regulation of cell signaling by adenylylation.";
Mol. Cell 34:93-103(2009).
[43]
AMPYLATION AT THR-35 (MICROBIAL INFECTION), IDENTIFICATION BY MASS
SPECTROMETRY, AND MUTAGENESIS OF THR-35.
PubMed=19039103; DOI=10.1126/science.1166382;
Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.;
"AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding
and downstream signaling.";
Science 323:269-272(2009).
[44]
INTERACTION WITH TBC1D2.
PubMed=20116244; DOI=10.1016/j.cub.2009.12.053;
Frasa M.A., Maximiano F.C., Smolarczyk K., Francis R.E., Betson M.E.,
Lozano E., Goldenring J., Seabra M.C., Rak A., Ahmadian M.R.,
Braga V.M.;
"Armus is a Rac1 effector that inactivates Rab7 and regulates E-
cadherin degradation.";
Curr. Biol. 20:198-208(2010).
[45]
FUNCTION.
PubMed=20696765; DOI=10.1074/jbc.M110.120451;
Li X., Lee A.Y.;
"Semaphorin 5A and plexin-B3 inhibit human glioma cell motility
through RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
J. Biol. Chem. 285:32436-32445(2010).
[46]
FUNCTION, INTERACTION WITH PPP5C, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF THR-17; GLY-30; THR-35 AND GLN-61.
PubMed=19948726; DOI=10.1074/jbc.M109.088427;
Chatterjee A., Wang L., Armstrong D.L., Rossie S.;
"Activated Rac1 GTPase translocates protein phosphatase 5 to the cell
membrane and stimulates phosphatase activity in vitro.";
J. Biol. Chem. 285:3872-3882(2010).
[47]
INTERACTION WITH ARHGEF16.
PubMed=20679435; DOI=10.1083/jcb.201005141;
Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S.,
Negishi M., Katoh H.;
"Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent
mechanism.";
J. Cell Biol. 190:461-477(2010).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[49]
ENZYME REGULATION.
PubMed=21565175; DOI=10.1016/j.bbrc.2011.04.116;
Naji L., Pacholsky D., Aspenstrom P.;
"ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics
and cell adhesion.";
Biochem. Biophys. Res. Commun. 409:96-102(2011).
[50]
UBIQUITINATION.
PubMed=22036506; DOI=10.1016/j.devcel.2011.08.015;
Torrino S., Visvikis O., Doye A., Boyer L., Stefani C., Munro P.,
Bertoglio J., Gacon G., Mettouchi A., Lemichez E.;
"The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation of active
Rac1.";
Dev. Cell 21:959-965(2011).
[51]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PACSIN2.
PubMed=21693584; DOI=10.1242/jcs.080630;
de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C.,
Hensbergen P.J., Deelder A.M., Plomann M., Hordijk P.L.;
"The F-BAR domain protein PACSIN2 associates with Rac1 and regulates
cell spreading and migration.";
J. Cell Sci. 124:2375-2388(2011).
[52]
INTERACTION WITH PKN2.
PubMed=20974804; DOI=10.1128/MCB.01001-10;
Wallace S.W., Magalhaes A., Hall A.;
"The Rho target PRK2 regulates apical junction formation in human
bronchial epithelial cells.";
Mol. Cell. Biol. 31:81-91(2011).
[53]
INTERACTION WITH FARP1.
PubMed=23209303; DOI=10.1083/jcb.201205041;
Cheadle L., Biederer T.;
"The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal
dynamics and transsynaptic organization.";
J. Cell Biol. 199:985-1001(2012).
[54]
INTERACTION WITH ARHGDIA.
PubMed=23434736; DOI=10.1136/jmedgenet-2012-101442;
Gupta I.R., Baldwin C., Auguste D., Ha K.C., El Andalousi J.,
Fahiminiya S., Bitzan M., Bernard C., Akbari M.R., Narod S.A.,
Rosenblatt D.S., Majewski J., Takano T.;
"ARHGDIA: a novel gene implicated in nephrotic syndrome.";
J. Med. Genet. 50:330-338(2013).
[55]
FUNCTION.
PubMed=23633677; DOI=10.1126/scisignal.2003627;
Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B.,
Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A.,
Bonecchi R., Locati M.;
"Beta-arrestin-dependent activation of the cofilin pathway is required
for the scavenging activity of the atypical chemokine receptor D6.";
Sci. Signal. 6:RA30-RA30(2013).
[56]
GLYCOSYLATION AT TYR-32 (MICROBIAL INFECTION).
PubMed=24141704; DOI=10.1038/nsmb.2688;
Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
Aktories K.;
"A bacterial toxin catalyzing tyrosine glycosylation of Rho and
deamidation of Gq and Gi proteins.";
Nat. Struct. Mol. Biol. 20:1273-1280(2013).
[57]
INTERACTION WITH FARP2.
PubMed=23375260; DOI=10.1016/j.str.2013.01.001;
He X., Kuo Y.C., Rosche T.J., Zhang X.;
"Structural basis for autoinhibition of the guanine nucleotide
exchange factor FARP2.";
Structure 21:355-364(2013).
[58]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[59]
X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 1-184 IN COMPLEX WITH GTP
ANALOG.
PubMed=9033596; DOI=10.1038/nsb0297-147;
Hirshberg M., Stockley R.W., Dodson G., Webb M.R.;
"The crystal structure of human rac1, a member of the rho-family
complexed with a GTP analogue.";
Nat. Struct. Biol. 4:147-152(1997).
[60]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT LEU-61 IN COMPLEX WITH
GTP AND NCF2.
PubMed=11090627; DOI=10.1016/S1097-2765(05)00091-2;
Lapouge K., Smith S.J., Walker P.A., Gamblin S.J., Smerdon S.J.,
Rittinger K.;
"Structure of the TPR domain of p67phox in complex with Rac.GTP.";
Mol. Cell 6:899-907(2000).
[61]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-177 IN COMPLEX WITH TIAM1.
PubMed=11130063; DOI=10.1038/35047014;
Worthylake D.K., Rossman K.L., Sondek J.;
"Crystal structure of Rac1 in complex with the guanine nucleotide
exchange region of Tiam1.";
Nature 408:682-688(2000).
[62]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-184 IN COMPLEX WITH
SALMONELLA SPTP.
PubMed=11163217; DOI=10.1016/S1097-2765(00)00141-6;
Stebbins C.E., Galan J.E.;
"Modulation of host signaling by a bacterial mimic: structure of the
Salmonella effector SptP bound to Rac1.";
Mol. Cell 6:1449-1460(2000).
[63]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-176 IN COMPLEX WITH GTP
ANALOG AND P.AERUGINOSA EXOS.
PubMed=11135665; DOI=10.1038/83007;
Wuertele M., Wolf E., Pederson K.J., Buchwald G., Ahmadian M.R.,
Barbieri J.T., Wittinghofer A.;
"How the Pseudomonas aeruginosa ExoS toxin downregulates Rac.";
Nat. Struct. Biol. 8:23-26(2001).
[64]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ARHGDIA.
PubMed=11513578; DOI=10.1021/bi010288k;
Grizot S., Faure J., Fieschi F., Vignais P.V., Dagher M.-C.,
Pebay-Peyroula E.;
"Crystal structure of the Rac1-RhoGDI complex involved in NADPH
oxidase activation.";
Biochemistry 40:10007-10013(2001).
[65]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND
ARFIP2.
PubMed=11346801; DOI=10.1038/35075620;
Tarricone C., Xiao B., Justin N., Walker P.A., Rittinger K.,
Gamblin S.J., Smerdon S.J.;
"The structural basis of Arfaptin-mediated cross-talk between Rac and
Arf signalling pathways.";
Nature 411:215-219(2001).
[66]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF ISOFORM B, AND
CHARACTERIZATION (ISOFORM B).
PubMed=14625275; DOI=10.1074/jbc.M310281200;
Fiegen D., Haeusler L.C., Blumenstein L., Herbrand U., Dvorsky R.,
Vetter I.R., Ahmadian M.R.;
"Alternative splicing of Rac1 generates Rac1b, a self-activating
GTPase.";
J. Biol. Chem. 279:4743-4749(2004).
[67]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-184 IN COMPLEX WITH
Y.PSEUDOTUBERCULOSIS YPKA.
PubMed=16959567; DOI=10.1016/j.cell.2006.06.056;
Prehna G., Ivanov M.I., Bliska J.B., Stebbins C.E.;
"Yersinia virulence depends on mimicry of host Rho-family nucleotide
dissociation inhibitors.";
Cell 126:869-880(2006).
[68]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-177 IN COMPLEX WITH GTP
ANALOG AND PLCB2, AND MUTAGENESIS OF PHE-37; TRP-56; LEU-67 AND
LEU-70.
PubMed=17115053; DOI=10.1038/nsmb1175;
Jezyk M.R., Snyder J.T., Gershberg S., Worthylake D.K., Harden T.K.,
Sondek J.;
"Crystal structure of Rac1 bound to its effector phospholipase C-
beta2.";
Nat. Struct. Mol. Biol. 13:1135-1140(2006).
[69]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-177 IN COMPLEX WITH DOCK2.
PubMed=21613211; DOI=10.1074/jbc.M111.236455;
Kulkarni K., Yang J., Zhang Z., Barford D.;
"Multiple factors confer specific Cdc42 and Rac protein activation by
dedicator of cytokinesis (DOCK) nucleotide exchange factors.";
J. Biol. Chem. 286:25341-25351(2011).
-!- FUNCTION: Plasma membrane-associated small GTPase which cycles
between active GTP-bound and inactive GDP-bound states. In its
active state, binds to a variety of effector proteins to regulate
cellular responses such as secretory processes, phagocytosis of
apoptotic cells, epithelial cell polarization and growth-factor
induced formation of membrane ruffles. Rac1 p21/rho GDI
heterodimer is the active component of the cytosolic factor sigma
1, which is involved in stimulation of the NADPH oxidase activity
in macrophages. Essential for the SPATA13-mediated regulation of
cell migration and adhesion assembly and disassembly. Stimulates
PKN2 kinase activity. In concert with RAB7A, plays a role in
regulating the formation of RBs (ruffled borders) in osteoclasts.
In glioma cells, promotes cell migration and invasion. In
podocytes, promotes nuclear shuttling of NR3C2; this modulation is
required for a proper kidney functioning. Required for atypical
chemokine receptor ACKR2-induced LIMK1-PAK1-dependent
phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2
from endosomal compartment to cell membrane, increasing its
efficiency in chemokine uptake and degradation. In synapses, seems
to mediate the regulation of F-actin cluster formation performed
by SHANK3.
-!- FUNCTION: Isoform B has an accelerated GEF-independent GDP/GTP
exchange and an impaired GTP hydrolysis, which is restored
partially by GTPase-activating proteins. It is able to bind to the
GTPase-binding domain of PAK but not full-length PAK in a GTP-
dependent manner, suggesting that the insertion does not
completely abolish effector interaction.
-!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
factors (GEFs) which promote the exchange of bound GDP for free
GTP, GTPase activating proteins (GAPs) which increase the GTP
hydrolysis activity, and GDP dissociation inhibitors which inhibit
the dissociation of the nucleotide from the GTPase. GTP hydrolysis
is stimulated by ARHGAP30. {ECO:0000269|PubMed:21565175}.
-!- SUBUNIT: Interacts with NISCH. Interacts with PIP5K1A. Interacts
with the GTP-bound form of RAB7A. Interacts with SRGAP2. Interacts
with CYFIP1/SRA-1. Interacts with PLXNB3. Interacts with ARHGDIA;
the interaction is induced by SEMA5A, mediated through PLXNB3 and
inactivates and stabilizes RAC1. Interacts (GTP-bound form
preferentially) with PKN2 (via the REM repeats); the interaction
stimulates autophosphorylation and phosphorylation of PKN2.
Interacts with the GEF proteins PREX1, RASGRF2, FARP1, FARP2,
DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and
GTP, and therefore activate it. Interacts with PARD6A, PARD6B and
PARD6G in a GTP-dependent manner. Part of a quaternary complex
containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G)
and some atypical PKC protein (PRKCI or PRKCZ), which plays a
central role in epithelial cell polarization. Found in a trimeric
complex composed of DOCK1 and ELMO1, which plays a central role in
phagocytosis of apoptotic cells. Interacts with RALBP1 via its
effector domain. Interacts with PLXNB1. Probably found in a
ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with
DSCAM; the interaction requires PAK1. Part of a complex with
MAP2K3, MAP3K3, CCM2 and DEF6. Interacts with BAIAP2, BAIAP2L1 and
DEF6. Interacts with Y.pseudotuberculosis YPKA and PLCB2.
Interacts with NOXA1. Interacts with ARHGEF2. Interacts with
TBC1D2. Interacts with UNKL. Interacts with USP6. Interacts with
SPATA13. Interacts with ARHGEF16; mediates activation of RAC1 by
EPHA2. Interacts with ITGB4. Interacts with S100A8 and
calprotectin (S100A8/9). Interacts with PACSIN2. Interacts with
ITGB1BP1. Interacts (when active) with PPP5C (via TPR repeats);
activates PPP5C phosphatase activity and translocates PPP5C to the
cell membrane. Interacts with RAPH1 (via Ras associating and PH
domains) (PubMed:18499456). Interacts with MTSS1L (via IMD
domain); this interaction may be important to potentiate PDGF-
induced RAC1 activation (PubMed:20875796).
{ECO:0000269|PubMed:10559471, ECO:0000269|PubMed:10954424,
ECO:0000269|PubMed:11035813, ECO:0000269|PubMed:11090627,
ECO:0000269|PubMed:11130063, ECO:0000269|PubMed:11130076,
ECO:0000269|PubMed:11135665, ECO:0000269|PubMed:11163217,
ECO:0000269|PubMed:11260256, ECO:0000269|PubMed:11346801,
ECO:0000269|PubMed:11513578, ECO:0000269|PubMed:11807099,
ECO:0000269|PubMed:12134158, ECO:0000269|PubMed:12612085,
ECO:0000269|PubMed:12716910, ECO:0000269|PubMed:15169762,
ECO:0000269|PubMed:15642721, ECO:0000269|PubMed:16959567,
ECO:0000269|PubMed:16982419, ECO:0000269|PubMed:17115053,
ECO:0000269|PubMed:17121847, ECO:0000269|PubMed:17145773,
ECO:0000269|PubMed:17430976, ECO:0000269|PubMed:18499456,
ECO:0000269|PubMed:19403692, ECO:0000269|PubMed:19948726,
ECO:0000269|PubMed:20116244, ECO:0000269|PubMed:20148946,
ECO:0000269|PubMed:20679435, ECO:0000269|PubMed:20875796,
ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:21613211,
ECO:0000269|PubMed:21693584, ECO:0000269|PubMed:23209303,
ECO:0000269|PubMed:23375260, ECO:0000269|PubMed:23434736,
ECO:0000269|PubMed:7673236, ECO:0000269|PubMed:9033596,
ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9857026}.
-!- INTERACTION:
P53365:ARFIP2; NbExp=9; IntAct=EBI-413628, EBI-638194;
Q92619:ARHGAP45; NbExp=3; IntAct=EBI-413628, EBI-2825900;
P52565:ARHGDIA; NbExp=7; IntAct=EBI-413628, EBI-712693;
Q14155:ARHGEF7; NbExp=8; IntAct=EBI-413628, EBI-717515;
Q9UQB8:BAIAP2; NbExp=4; IntAct=EBI-413628, EBI-525456;
Q13490:BIRC2; NbExp=2; IntAct=EBI-413628, EBI-514538;
Q03135:CAV1; NbExp=2; IntAct=EBI-413628, EBI-603614;
Q9UJX2:CDC23; NbExp=3; IntAct=EBI-413628, EBI-396137;
P52757:CHN2; NbExp=4; IntAct=EBI-413628, EBI-714925;
Q14185:DOCK1; NbExp=10; IntAct=EBI-413628, EBI-446740;
Q92608:DOCK2; NbExp=3; IntAct=EBI-413628, EBI-448771;
O75369:FLNB; NbExp=2; IntAct=EBI-413628, EBI-352089;
P46940:IQGAP1; NbExp=4; IntAct=EBI-413628, EBI-297509;
Q6A162:KRT40; NbExp=3; IntAct=EBI-413628, EBI-10171697;
Q5S007:LRRK2; NbExp=5; IntAct=EBI-413628, EBI-5323863;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-413628, EBI-741037;
Q01968:OCRL; NbExp=3; IntAct=EBI-413628, EBI-6148898;
Q13153:PAK1; NbExp=25; IntAct=EBI-413628, EBI-1307;
Q13177:PAK2; NbExp=4; IntAct=EBI-413628, EBI-1045887;
O75914:PAK3; NbExp=2; IntAct=EBI-413628, EBI-3389553;
Q9NPB6:PARD6A; NbExp=2; IntAct=EBI-413628, EBI-81876;
Q9BYG5:PARD6B; NbExp=3; IntAct=EBI-413628, EBI-295391;
Q9BYG4:PARD6G; NbExp=2; IntAct=EBI-413628, EBI-295417;
P19174:PLCG1; NbExp=7; IntAct=EBI-413628, EBI-79387;
Q8TCU6:PREX1; NbExp=2; IntAct=EBI-7212896, EBI-1046542;
P41743:PRKCI; NbExp=3; IntAct=EBI-413628, EBI-286199;
Q01105:SET; NbExp=8; IntAct=EBI-413628, EBI-1053182;
Q7Z6J0:SH3RF1; NbExp=2; IntAct=EBI-413628, EBI-311339;
Q8TEJ3:SH3RF3; NbExp=6; IntAct=EBI-413628, EBI-7975674;
Q98PK8:smc (xeno); NbExp=5; IntAct=EBI-413628, EBI-12740386;
Q6P589:TNFAIP8L2; NbExp=6; IntAct=EBI-7212896, EBI-9073209;
O75962-4:TRIO; NbExp=2; IntAct=EBI-7212896, EBI-15915736;
Q9H9P5:UNKL; NbExp=2; IntAct=EBI-413628, EBI-7797561;
Q9Y6N9:USH1C; NbExp=3; IntAct=EBI-413628, EBI-954308;
P15498:VAV1; NbExp=2; IntAct=EBI-413628, EBI-625518;
P98170:XIAP; NbExp=3; IntAct=EBI-413628, EBI-517127;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome
{ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:19948726,
ECO:0000269|PubMed:21693584}. Cytoplasm {ECO:0000250}. Note=Inner
surface of plasma membrane possibly with attachment requiring
prenylation of the C-terminal cysteine (By similarity). Identified
by mass spectrometry in melanosome fractions from stage I to stage
IV. Found in the ruffled border (a late endosomal-like compartment
in the plasma membrane) of bone-resorbing osteoclasts (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A; Synonyms=Rac1A;
IsoId=P63000-1, P15154-1;
Sequence=Displayed;
Name=B; Synonyms=Rac1B, Rac1ins;
IsoId=P63000-2, P15154-2;
Sequence=VSP_005710;
Note=Contains a phosphoserine at position 71.
{ECO:0000244|PubMed:18669648};
-!- TISSUE SPECIFICITY: Isoform B is predominantly identified in skin
and epithelial tissues from the intestinal tract. Its expression
is elevated in colorectal tumors at various stages of neoplastic
progression, as compared to their respective adjacent tissues.
-!- DOMAIN: The effector region mediates interaction with DEF6.
{ECO:0000269|PubMed:17121847}.
-!- PTM: (Microbial infection) AMPylation at Tyr-32 and Thr-35 are
mediated by bacterial enzymes in case of infection by H.somnus and
V.parahaemolyticus, respectively. AMPylation occurs in the
effector region and leads to inactivation of the GTPase activity
by preventing the interaction with downstream effectors, thereby
inhibiting actin assembly in infected cells. It is unclear whether
some human enzyme mediates AMPylation; FICD has such ability in
vitro but additional experiments remain to be done to confirm
results in vivo. {ECO:0000269|PubMed:19039103,
ECO:0000269|PubMed:19362538}.
-!- PTM: GTP-bound active form is ubiquitinated by HACE1, leading to
its degradation by the proteasome. {ECO:0000269|PubMed:18093184,
ECO:0000269|PubMed:22036506}.
-!- PTM: (Microbial infection) Glycosylated at Tyr-32 by Photorhabdus
asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230
inhibits downstream signaling by an impaired interaction with
diverse regulator and effector proteins of Rac and leads to actin
disassembly. {ECO:0000269|PubMed:24141704}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAZ80485.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rac1/";
-----------------------------------------------------------------------
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EMBL; M29870; AAA36537.1; -; mRNA.
EMBL; M31467; AAA36544.1; -; mRNA.
EMBL; AJ132694; CAA10732.1; -; mRNA.
EMBL; AJ132695; CAB53579.5; -; Genomic_DNA.
EMBL; AJ132695; CAA10733.6; -; Genomic_DNA.
EMBL; AF136373; AAD30547.1; -; mRNA.
EMBL; AY279384; AAQ16632.1; -; mRNA.
EMBL; AF498964; AAM21111.1; -; mRNA.
EMBL; BT007121; AAP35785.1; -; mRNA.
EMBL; DQ165078; AAZ80485.1; ALT_INIT; Genomic_DNA.
EMBL; AC009412; AAS07511.1; -; Genomic_DNA.
EMBL; AC009412; AAS07512.1; -; Genomic_DNA.
EMBL; BC004247; AAH04247.1; -; mRNA.
EMBL; BC050687; AAH50687.1; -; mRNA.
EMBL; BC107748; AAI07749.1; -; mRNA.
CCDS; CCDS5348.1; -.
CCDS; CCDS5349.1; -. [P63000-2]
PIR; A34788; TVHUC1.
RefSeq; NP_008839.2; NM_006908.4. [P63000-1]
RefSeq; NP_061485.1; NM_018890.3. [P63000-2]
UniGene; Hs.413812; -.
PDB; 1E96; X-ray; 2.40 A; A=2-192.
PDB; 1FOE; X-ray; 2.80 A; B/D/F/H=1-177.
PDB; 1G4U; X-ray; 2.30 A; R=1-184.
PDB; 1HE1; X-ray; 2.00 A; C/D=2-176.
PDB; 1HH4; X-ray; 2.70 A; A/B=2-192.
PDB; 1I4D; X-ray; 2.50 A; D=1-192.
PDB; 1I4L; X-ray; 2.70 A; D=1-192.
PDB; 1I4T; X-ray; 2.60 A; D=1-192.
PDB; 1MH1; X-ray; 1.38 A; A=2-184.
PDB; 1RYF; X-ray; 1.75 A; A/B=1-182.
PDB; 1RYH; X-ray; 1.75 A; A/B=1-182.
PDB; 2FJU; X-ray; 2.20 A; A=1-177.
PDB; 2H7V; X-ray; 2.60 A; A/B=1-184.
PDB; 2NZ8; X-ray; 2.00 A; A=1-177.
PDB; 2P2L; X-ray; 1.90 A; A/B/C=1-184.
PDB; 2RMK; NMR; -; A=1-192.
PDB; 2VRW; X-ray; 1.85 A; A=1-184.
PDB; 2WKP; X-ray; 1.90 A; A=4-180.
PDB; 2WKQ; X-ray; 1.60 A; A=4-180.
PDB; 2WKR; X-ray; 2.20 A; A=4-180.
PDB; 2YIN; X-ray; 2.70 A; C/D=1-177.
PDB; 3B13; X-ray; 3.01 A; B/D=1-177.
PDB; 3BJI; X-ray; 2.60 A; C/D=1-177.
PDB; 3RYT; X-ray; 3.58 A; C=1-177.
PDB; 3SBD; X-ray; 2.10 A; A/B=2-177.
PDB; 3SBE; X-ray; 2.60 A; A=2-177.
PDB; 3SU8; X-ray; 3.20 A; A=1-177.
PDB; 3SUA; X-ray; 4.39 A; A/B/C=1-177.
PDB; 3TH5; X-ray; 2.30 A; A/B=2-177.
PDB; 4GZL; X-ray; 2.00 A; A/B=2-177.
PDB; 4GZM; X-ray; 2.80 A; A/B=2-177.
PDB; 4YON; X-ray; 1.95 A; B=1-177.
PDB; 5FI0; X-ray; 3.28 A; B/D/F/H=1-192.
PDB; 5HZH; X-ray; 2.60 A; A=1-180.
PDB; 5O33; X-ray; 1.64 A; A=1-177.
PDBsum; 1E96; -.
PDBsum; 1FOE; -.
PDBsum; 1G4U; -.
PDBsum; 1HE1; -.
PDBsum; 1HH4; -.
PDBsum; 1I4D; -.
PDBsum; 1I4L; -.
PDBsum; 1I4T; -.
PDBsum; 1MH1; -.
PDBsum; 1RYF; -.
PDBsum; 1RYH; -.
PDBsum; 2FJU; -.
PDBsum; 2H7V; -.
PDBsum; 2NZ8; -.
PDBsum; 2P2L; -.
PDBsum; 2RMK; -.
PDBsum; 2VRW; -.
PDBsum; 2WKP; -.
PDBsum; 2WKQ; -.
PDBsum; 2WKR; -.
PDBsum; 2YIN; -.
PDBsum; 3B13; -.
PDBsum; 3BJI; -.
PDBsum; 3RYT; -.
PDBsum; 3SBD; -.
PDBsum; 3SBE; -.
PDBsum; 3SU8; -.
PDBsum; 3SUA; -.
PDBsum; 3TH5; -.
PDBsum; 4GZL; -.
PDBsum; 4GZM; -.
PDBsum; 4YON; -.
PDBsum; 5FI0; -.
PDBsum; 5HZH; -.
PDBsum; 5O33; -.
ProteinModelPortal; P63000; -.
SMR; P63000; -.
BioGrid; 111817; 185.
CORUM; P63000; -.
DIP; DIP-29260N; -.
IntAct; P63000; 138.
MINT; MINT-4999291; -.
BindingDB; P63000; -.
ChEMBL; CHEMBL6094; -.
DrugBank; DB00514; Dextromethorphan.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
iPTMnet; P63000; -.
PhosphoSitePlus; P63000; -.
SwissPalm; P63000; -.
BioMuta; RAC1; -.
DMDM; 51702787; -.
EPD; P63000; -.
MaxQB; P63000; -.
PeptideAtlas; P63000; -.
PRIDE; P63000; -.
DNASU; 5879; -.
Ensembl; ENST00000348035; ENSP00000258737; ENSG00000136238. [P63000-1]
Ensembl; ENST00000356142; ENSP00000348461; ENSG00000136238. [P63000-2]
GeneID; 5879; -.
KEGG; hsa:5879; -.
UCSC; uc003spw.4; human.
CTD; 5879; -.
DisGeNET; 5879; -.
EuPathDB; HostDB:ENSG00000136238.17; -.
GeneCards; RAC1; -.
H-InvDB; HIX0031500; -.
HGNC; HGNC:9801; RAC1.
HPA; CAB035994; -.
HPA; HPA047820; -.
MIM; 602048; gene.
neXtProt; NX_P63000; -.
OpenTargets; ENSG00000136238; -.
PharmGKB; PA34162; -.
GeneTree; ENSGT00760000118978; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; P63000; -.
KO; K04392; -.
OMA; KAKWFPE; -.
PhylomeDB; P63000; -.
TreeFam; TF101109; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-164944; Nef and signal transduction.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-376172; DSCAM interactions.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928664; Ephrin signaling.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
Reactome; R-HSA-4086400; PCP/CE pathway.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-HSA-418885; DCC mediated attractive signaling.
Reactome; R-HSA-428540; Activation of RAC1.
Reactome; R-HSA-428543; Inactivation of CDC42 and RAC1.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5625900; RHO GTPases activate CIT.
Reactome; R-HSA-5625970; RHO GTPases activate KTN1.
Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P63000; -.
SIGNOR; P63000; -.
ChiTaRS; RAC1; human.
EvolutionaryTrace; P63000; -.
GeneWiki; RAC1; -.
GenomeRNAi; 5879; -.
PMAP-CutDB; P63000; -.
PRO; PR:P63000; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000136238; -.
CleanEx; HS_RAC1; -.
ExpressionAtlas; P63000; baseline and differential.
Genevisible; P63000; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:SynGO.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0005802; C:trans-Golgi network; IDA:FlyBase.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0017137; F:Rab GTPase binding; IEA:Ensembl.
GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; ISS:UniProtKB.
GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
GO; GO:0030041; P:actin filament polymerization; TAS:UniProtKB.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0048870; P:cell motility; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; NAS:BHF-UCL.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IMP:CAFA.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
GO; GO:0051668; P:localization within membrane; IMP:BHF-UCL.
GO; GO:0002551; P:mast cell chemotaxis; IEA:Ensembl.
GO; GO:0006928; P:movement of cell or subcellular component; TAS:ProtInc.
GO; GO:0032707; P:negative regulation of interleukin-23 production; IDA:BHF-UCL.
GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; TAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IGI:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:MGI.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:CAFA.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; TAS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl.
GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
GO; GO:0008361; P:regulation of cell size; IMP:UniProtKB.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; TAS:BHF-UCL.
GO; GO:0010591; P:regulation of lamellipodium assembly; IGI:CAFA.
GO; GO:0060263; P:regulation of respiratory burst; IDA:BHF-UCL.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0051492; P:regulation of stress fiber assembly; IGI:CAFA.
GO; GO:0009611; P:response to wounding; TAS:ProtInc.
GO; GO:0031529; P:ruffle organization; IDA:MGI.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Alternative splicing; Cell membrane;
Complete proteome; Cytoplasm; Glycoprotein; GTP-binding;
Isopeptide bond; Lipoprotein; Membrane; Methylation;
Nucleotide-binding; Phosphoprotein; Polymorphism; Prenylation;
Reference proteome; Ubl conjugation.
CHAIN 1 189 Ras-related C3 botulinum toxin substrate
1.
/FTId=PRO_0000042036.
PROPEP 190 192 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000042037.
NP_BIND 10 17 GTP. {ECO:0000250}.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 115 118 GTP. {ECO:0000250}.
MOTIF 32 40 Effector region. {ECO:0000255}.
MOD_RES 32 32 O-AMP-tyrosine; by Haemophilus IbpA;
alternate. {ECO:0000269|PubMed:19362538}.
MOD_RES 35 35 O-AMP-threonine; by Vibrio VopS.
{ECO:0000269|PubMed:19039103}.
MOD_RES 39 39 ADP-ribosylasparagine; by botulinum
toxin. {ECO:0000250}.
MOD_RES 189 189 Cysteine methyl ester. {ECO:0000250}.
LIPID 189 189 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:1903399}.
CARBOHYD 32 32 O-linked (GlcNAc) tyrosine; by
Photorhabdus PAU_02230; alternate.
{ECO:0000269|PubMed:24141704}.
CROSSLNK 147 147 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18093184}.
VAR_SEQ 75 75 T -> TVGETYGKDITSRGKDKPIA (in isoform B).
{ECO:0000303|PubMed:10597294,
ECO:0000303|PubMed:11062023,
ECO:0000303|Ref.5}.
/FTId=VSP_005710.
VARIANT 26 26 N -> D (in dbSNP:rs5830).
/FTId=VAR_014540.
VARIANT 28 28 F -> L (in dbSNP:rs5832).
/FTId=VAR_014541.
VARIANT 59 59 A -> T (in dbSNP:rs5837).
/FTId=VAR_014542.
VARIANT 63 63 D -> G (in dbSNP:rs5831).
/FTId=VAR_014543.
VARIANT 93 93 V -> G (in dbSNP:rs5826).
/FTId=VAR_014545.
VARIANT 93 93 V -> I (in dbSNP:rs5825).
/FTId=VAR_014544.
VARIANT 108 108 T -> I (in dbSNP:rs5838).
/FTId=VAR_014546.
VARIANT 130 130 K -> R (in dbSNP:rs5828).
/FTId=VAR_014547.
VARIANT 133 133 K -> E (in dbSNP:rs5835).
/FTId=VAR_014548.
VARIANT 135 135 T -> I (in dbSNP:rs11540455).
{ECO:0000269|Ref.7}.
/FTId=VAR_033303.
VARIANT 180 180 P -> S (in dbSNP:rs16063).
/FTId=VAR_014549.
VARIANT 182 182 V -> E (in dbSNP:rs5836).
/FTId=VAR_014550.
MUTAGEN 12 12 G->V: Constitutively active. Interacts
with PARD6 proteins. Increases nuclear
localization and up-regulates
transcriptional activity of NR3C2.
{ECO:0000269|PubMed:11260256,
ECO:0000269|PubMed:19029984}.
MUTAGEN 17 17 T->N: Constitutively inactivated.
Abolishes interaction with PARD6
proteins. No effect on NR3C2
transcriptional activity. No interaction
with PPP5C. Doesn't activate PPP5C
phosphatase activity and translocate
PPP5C to the plasma membrane.
{ECO:0000269|PubMed:11260256,
ECO:0000269|PubMed:19029984,
ECO:0000269|PubMed:19948726}.
MUTAGEN 30 30 G->V: No interaction with PPP5C; when
associated with L-61. Translocates to the
plasma membrane; also when associated
with L-61. {ECO:0000269|PubMed:19948726}.
MUTAGEN 32 32 Y->F: Abolishes AMPylation by Haemophilus
IbpA. {ECO:0000269|PubMed:19362538}.
MUTAGEN 35 35 T->A: Abolishes AMPylation by Vibrio
VopS. {ECO:0000269|PubMed:19039103,
ECO:0000269|PubMed:19948726}.
MUTAGEN 35 35 T->S: No interaction with PPP5C; when
associated with L-61. Translocates to the
plasma membrane; also when associated
with L-61. {ECO:0000269|PubMed:19039103,
ECO:0000269|PubMed:19948726}.
MUTAGEN 37 37 F->A: Strongly reduced interaction with
PLCB2. {ECO:0000269|PubMed:17115053}.
MUTAGEN 56 56 W->A: Strongly reduced interaction with
PLCB2. {ECO:0000269|PubMed:17115053}.
MUTAGEN 61 61 Q->L: Constitutively active. Interacts
with PARD6 proteins. Interacts with
PPP5C, activates its phosphatase activity
and translocates PPP5C to the plasma
membrane. No effect on interaction with
RAPH1. No interaction with PPP5C; when
associated with V-30 or S-35.
Translocates to the plasma membrane; also
when associated with V-30 or S-35.
{ECO:0000269|PubMed:10954424,
ECO:0000269|PubMed:18499456,
ECO:0000269|PubMed:19948726}.
MUTAGEN 67 67 L->A: Strongly reduced interaction with
PLCB2. {ECO:0000269|PubMed:17115053}.
MUTAGEN 70 70 L->A: Strongly reduced interaction with
PLCB2. {ECO:0000269|PubMed:17115053}.
CONFLICT 192 192 Missing (in Ref. 2; AAA36544).
{ECO:0000305}.
STRAND 2 9 {ECO:0000244|PDB:1MH1}.
HELIX 12 14 {ECO:0000244|PDB:4YON}.
HELIX 16 25 {ECO:0000244|PDB:1MH1}.
STRAND 31 36 {ECO:0000244|PDB:2P2L}.
STRAND 39 46 {ECO:0000244|PDB:1MH1}.
STRAND 49 56 {ECO:0000244|PDB:1MH1}.
HELIX 62 64 {ECO:0000244|PDB:1MH1}.
TURN 65 67 {ECO:0000244|PDB:1MH1}.
HELIX 68 71 {ECO:0000244|PDB:1MH1}.
STRAND 76 83 {ECO:0000244|PDB:1MH1}.
HELIX 87 95 {ECO:0000244|PDB:1MH1}.
HELIX 97 104 {ECO:0000244|PDB:1MH1}.
STRAND 106 108 {ECO:0000244|PDB:1RYF}.
STRAND 110 115 {ECO:0000244|PDB:1MH1}.
HELIX 117 120 {ECO:0000244|PDB:1MH1}.
HELIX 123 131 {ECO:0000244|PDB:1MH1}.
HELIX 139 148 {ECO:0000244|PDB:1MH1}.
STRAND 152 156 {ECO:0000244|PDB:1MH1}.
TURN 159 161 {ECO:0000244|PDB:1MH1}.
HELIX 165 176 {ECO:0000244|PDB:1MH1}.
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


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