(data stored in SCRATCH zone)

SWISSPROT: CDC42_HUMAN

ID   CDC42_HUMAN             Reviewed;         191 AA.
AC   P60953; P21181; P25763; Q7L8R5; Q9UDI2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   08-MAY-2019, entry version 195.
DE   RecName: Full=Cell division control protein 42 homolog;
DE   AltName: Full=G25K GTP-binding protein;
DE   Flags: Precursor;
GN   Name=CDC42;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=2122236; DOI=10.1128/MCB.10.11.5977;
RA   Munemitsu S., Innis M.A., Clark R., McCormick F., Ullrich A.,
RA   Polakis P.;
RT   "Molecular cloning and expression of a G25K cDNA, the human homolog of
RT   the yeast cell cycle gene CDC42.";
RL   Mol. Cell. Biol. 10:5977-5982(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
RX   PubMed=2124704; DOI=10.1073/pnas.87.24.9853;
RA   Shinjo K., Koland J.G., Hart M.J., Narasimhan V., Johnson D.I.,
RA   Evans T., Cerione R.A.;
RT   "Molecular cloning of the gene for the human placental GTP-binding
RT   protein Gp (G25K): identification of this GTP-binding protein as the
RT   human homolog of the yeast cell-division-cycle protein CDC42.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9853-9857(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RA   Rhodes S., Huckle E.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Placenta;
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction
RT   sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Cervix, Placenta, and Uterus;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 67-83 (ISOFORM 2), PARTIAL PROTEIN SEQUENCE
RP   (ISOFORM 1), AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [9]
RP   PROTEIN SEQUENCE OF 97-107; 134-144 AND 167-183 (ISOFORM 2).
RC   TISSUE=Neutrophil;
RX   PubMed=8504089; DOI=10.1021/bi00072a029;
RA   Kwong C.H., Malech H.L., Rotrosen D., Leto T.L.;
RT   "Regulation of the human neutrophil NADPH oxidase by rho-related G-
RT   proteins.";
RL   Biochemistry 32:5711-5717(1993).
RN   [10]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2496687; DOI=10.1016/0006-291X(89)91615-X;
RA   Polakis P.G., Snyderman R., Evans T.;
RT   "Characterization of G25K, a GTP-binding protein containing a novel
RT   putative nucleotide binding domain.";
RL   Biochem. Biophys. Res. Commun. 160:25-32(1989).
RN   [11]
RP   INTERACTION WITH ARHGDIB.
RX   PubMed=7512369; DOI=10.1002/gcc.2870080408;
RA   Adra C.N., Ko J., Leonard D., Wirth L.J., Cerione R.A., Lim B.;
RT   "Identification of a novel protein with GDP dissociation inhibitor
RT   activity for the ras-like proteins CDC42Hs and rac I.";
RL   Genes Chromosomes Cancer 8:253-261(1993).
RN   [12]
RP   INTERACTION WITH CDC42EP1; CDC42EP2; CDC42EP3 AND CDC42EP5.
RC   TISSUE=Embryo;
RX   PubMed=10490598; DOI=10.1128/MCB.19.10.6585;
RA   Joberty G., Perlungher R.R., Macara I.G.;
RT   "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
RT   proteins.";
RL   Mol. Cell. Biol. 19:6585-6597(1999).
RN   [13]
RP   INTERACTION WITH CSPG4.
RX   PubMed=10587647; DOI=10.1038/70302;
RA   Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L.,
RA   Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.;
RT   "Melanoma chondroitin sulphate proteoglycan regulates cell spreading
RT   through Cdc42, Ack-1 and p130cas.";
RL   Nat. Cell Biol. 1:507-513(1999).
RN   [14]
RP   INTERACTION WITH CDC42SE1 AND CDC42SE2.
RX   PubMed=10816584; DOI=10.1074/jbc.M002832200;
RA   Pirone D.M., Fukuhara S., Gutkind J.S., Burbelo P.D.;
RT   "SPECs, small binding proteins for Cdc42.";
RL   J. Biol. Chem. 275:22650-22656(2000).
RN   [15]
RP   INTERACTION WITH PARD6A, AND MUTAGENESIS OF GLY-12.
RX   PubMed=10954424;
RA   Johansson A.-S., Driessens M., Aspenstroem P.;
RT   "The mammalian homologue of the Caenorhabditis elegans polarity
RT   protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and
RT   Rac1.";
RL   J. Cell Sci. 113:3267-3275(2000).
RN   [16]
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
RT   regulation of membrane ruffling.";
RL   Nature 408:732-735(2000).
RN   [17]
RP   INTERACTION WITH PARD6A; PARD6B AND PARD6G, SUBUNIT OF A COMPLEX
RP   CONTAINING PRKCI AND PARD6B, AND MUTAGENESIS OF THR-17 AND GLN-61.
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
RT   PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to
RT   atypical protein kinase C.";
RL   Genes Cells 6:107-119(2001).
RN   [18]
RP   INTERACTION WITH ITGB1BP1.
RX   PubMed=11807099; DOI=10.1083/jcb.200108030;
RA   Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F.,
RA   Silengo L., 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   [19]
RP   INTERACTION WITH DOCK9, AND ACTIVATION BY DOCK9.
RX   PubMed=12172552; DOI=10.1038/ncb835;
RA   Meller N., Irani-Tehrani M., Kiosses W.B., Del Pozo M.A.,
RA   Schwartz M.A.;
RT   "Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho
RT   proteins.";
RL   Nat. Cell Biol. 4:639-647(2002).
RN   [20]
RP   PHOSPHORYLATION AT TYR-64 BY SRC.
RX   PubMed=14506284; DOI=10.1074/jbc.M307021200;
RA   Tu S., Wu W.J., Wang J., Cerione R.A.;
RT   "Epidermal growth factor-dependent regulation of Cdc42 is mediated by
RT   the Src tyrosine kinase.";
RL   J. Biol. Chem. 278:49293-49300(2003).
RN   [21]
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
RT   for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling.";
RL   Mol. Cell. Biol. 23:2151-2161(2003).
RN   [22]
RP   FUNCTION, AND MUTAGENESIS OF GLY-12 AND THR-17.
RX   PubMed=14978216; DOI=10.1091/mbc.E03-07-0493;
RA   Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.;
RT   "Regulation of dendritic branching and filopodia formation in
RT   hippocampal neurons by specific acylated protein motifs.";
RL   Mol. Biol. Cell 15:2205-2217(2004).
RN   [23]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15642749; DOI=10.1083/jcb.200408085;
RA   Oceguera-Yanez F., Kimura K., Yasuda S., Higashida C., Kitamura T.,
RA   Hiraoka Y., Haraguchi T., Narumiya S.;
RT   "Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in
RT   mitosis.";
RL   J. Cell Biol. 168:221-232(2005).
RN   [24]
RP   FUNCTION IN CELL MIGRATION, AND INTERACTION WITH BCAR1; TNK2 AND CRK.
RX   PubMed=17038317; DOI=10.1074/jbc.M604342200;
RA   Modzelewska K., Newman L.P., Desai R., Keely P.J.;
RT   "Ack1 mediates Cdc42-dependent cell migration and signaling to
RT   p130Cas.";
RL   J. Biol. Chem. 281:37527-37535(2006).
RN   [25]
RP   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.,
RA   Tanaka H., 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   [26]
RP   AMPYLATION AT TYR-32 (MICROBIAL INFECTION), 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.,
RA   Mendez J.C., 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   [27]
RP   INTERACTION WITH FNBP1L.
RX   PubMed=19798448; DOI=10.1371/journal.pgen.1000675;
RA   Giuliani C., Troglio F., Bai Z., Patel F.B., Zucconi A.,
RA   Malabarba M.G., Disanza A., Stradal T.B., Cassata G., Confalonieri S.,
RA   Hardin J.D., Soto M.C., Grant B.D., Scita G.;
RT   "Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics
RT   and membrane trafficking during Caenorhabditis elegans oocyte growth
RT   and embryonic epidermal morphogenesis.";
RL   PLoS Genet. 5:E1000675-E1000675(2009).
RN   [28]
RP   AMPYLATION AT THR-35 (MICROBIAL INFECTION).
RX   PubMed=19039103; DOI=10.1126/science.1166382;
RA   Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.;
RT   "AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding
RT   and downstream signaling.";
RL   Science 323:269-272(2009).
RN   [29]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH NEK6.
RX   PubMed=20873783; DOI=10.1021/pr100562w;
RA   Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C.,
RA   Santana Bernachi J., Paes Leme A.F., Kobarg J.;
RT   "Characterization of hNek6 interactome reveals an important role for
RT   its short N-terminal domain and colocalization with proteins at the
RT   centrosome.";
RL   J. Proteome Res. 9:6298-6316(2010).
RN   [30]
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.,
RA   Buerckstuemmer T., 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   [31]
RP   INTERACTION WITH ARHGEF16.
RX   PubMed=21139582; DOI=10.1038/sj.bjc.6606026;
RA   Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L.,
RA   Hampson I.N.;
RT   "The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which
RT   activates Cdc42.";
RL   Br. J. Cancer 104:324-331(2011).
RN   [32]
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   [33]
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
RT   deamidation of Gq and Gi proteins.";
RL   Nat. Struct. Mol. Biol. 20:1273-1280(2013).
RN   [34]
RP   FUNCTION.
RX   PubMed=26465210; DOI=10.1038/ncomms9623;
RA   Schlam D., Bagshaw R.D., Freeman S.A., Collins R.F., Pawson T.,
RA   Fairn G.D., Grinstein S.;
RT   "Phosphoinositide 3-kinase enables phagocytosis of large particles by
RT   terminating actin assembly through Rac/Cdc42 GTPase-activating
RT   proteins.";
RL   Nat. Commun. 6:8623-8623(2015).
RN   [35]
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.,
RA   Ayoub D., 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   [36]
RP   STRUCTURE BY NMR.
RX   PubMed=9220962; DOI=10.1021/bi970694x;
RA   Feltham J.L., Dotsch V., Raza S., Manor D., Cerione R.A.,
RA   Sutcliffe M.J., Wagner G., Oswald R.E.;
RT   "Definition of the switch surface in the solution structure of
RT   Cdc42Hs.";
RL   Biochemistry 36:8755-8766(1997).
RN   [37]
RP   STRUCTURE BY NMR.
RX   PubMed=9760238; DOI=10.1021/bi981352+;
RA   Guo W., Sutcliffe M.J., Cerione R.A., Oswald R.E.;
RT   "Identification of the binding surface on Cdc42Hs for p21-activated
RT   kinase.";
RL   Biochemistry 37:14030-14037(1998).
RN   [38]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH RHOGAP.
RX   PubMed=9262406; DOI=10.1038/41805;
RA   Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D.,
RA   Laue E., Gamblin S.J., Smerdon S.J.;
RT   "Crystal structure of a small G protein in complex with the GTPase-
RT   activating protein rhoGAP.";
RL   Nature 388:693-697(1997).
RN   [39]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF VAL-12 MUTANT.
RX   PubMed=10211824; DOI=10.1110/ps.8.4.778;
RA   Rudolph M.G., Wittinghofer A., Vetter I.R.;
RT   "Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray
RT   diffraction and fluorescence spectroscopy: two different nucleotide
RT   states in one crystal.";
RL   Protein Sci. 8:778-787(1999).
RN   [40]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RA   Kongsaeree P., Cerione R.A., Clardy J.C.;
RT   "The structure determination of CDC42Hs and GDP complex.";
RL   Submitted (JUN-1997) to the PDB data bank.
RN   [41] {ECO:0000244|PDB:1DOA}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-188, ISOPRENYLATION AT
RP   CYS-188, AND METHYLATION AT CYS-188.
RX   PubMed=10676816; DOI=10.1016/S0092-8674(00)80670-4;
RA   Hoffman G.R., Nassar N., Cerione R.A.;
RT   "Structure of the Rho family GTP-binding protein Cdc42 in complex with
RT   the multifunctional regulator RhoGDI.";
RL   Cell 100:345-356(2000).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-188 IN COMPLEX WITH DOCK9.
RX   PubMed=19745154; DOI=10.1126/science.1174468;
RA   Yang J., Zhang Z., Roe S.M., Marshall C.J., Barford D.;
RT   "Activation of Rho GTPases by DOCK exchange factors is mediated by a
RT   nucleotide sensor.";
RL   Science 325:1398-1402(2009).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-181 IN COMPLEX WITH
RP   H.SOMNUS IBPA AND GDP, AND AMPYLATION AT TYR-32 (MICROBIAL INFECTION).
RX   PubMed=20622875; DOI=10.1038/nsmb.1867;
RA   Xiao J., Worby C.A., Mattoo S., Sankaran B., Dixon J.E.;
RT   "Structural basis of Fic-mediated adenylylation.";
RL   Nat. Struct. Mol. Biol. 17:1004-1010(2010).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-188 IN COMPLEX WITH MOUSE
RP   DOCK8, AND ACTIVITY REGULATION.
RX   PubMed=22461490; DOI=10.1182/blood-2012-01-407098;
RA   Harada Y., Tanaka Y., Terasawa M., Pieczyk M., Habiro K., Katakai T.,
RA   Hanawa-Suetsugu K., Kukimoto-Niino M., Nishizaki T., Shirouzu M.,
RA   Duan X., Uruno T., Nishikimi A., Sanematsu F., Yokoyama S.,
RA   Stein J.V., Kinashi T., Fukui Y.;
RT   "DOCK8 is a Cdc42 activator critical for interstitial dendritic cell
RT   migration during immune responses.";
RL   Blood 119:4451-4461(2012).
RN   [45]
RP   INVOLVEMENT IN TKS, AND VARIANT TKS CYS-64.
RX   PubMed=26386261; DOI=10.1002/ajmg.a.37275;
RA   Takenouchi T., Kosaki R., Niizuma T., Hata K., Kosaki K.;
RT   "Macrothrombocytopenia and developmental delay with a de novo CDC42
RT   mutation: Yet another locus for thrombocytopenia and developmental
RT   delay.";
RL   Am. J. Med. Genet. A 167A:2822-2825(2015).
RN   [46]
RP   VARIANT TKS CYS-64.
RX   PubMed=26708094; DOI=10.1002/ajmg.a.37526;
RA   Takenouchi T., Okamoto N., Ida S., Uehara T., Kosaki K.;
RT   "Further evidence of a mutation in CDC42 as a cause of a recognizable
RT   syndromic form of thrombocytopenia.";
RL   Am. J. Med. Genet. A 170:852-855(2016).
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles
CC       between an active GTP-bound and an inactive GDP-bound state. In
CC       active state binds to a variety of effector proteins to regulate
CC       cellular responses. Involved in epithelial cell polarization
CC       processes. Regulates the bipolar attachment of spindle
CC       microtubules to kinetochores before chromosome congression in
CC       metaphase. Plays a role in the extension and maintenance of the
CC       formation of thin, actin-rich surface projections called
CC       filopodia. Mediates CDC42-dependent cell migration. Required for
CC       DOCK10-mediated spine formation in Purkinje cells and hippocampal
CC       neurons. Facilitates filopodia formation upon DOCK11-activation
CC       (By similarity). Also plays a role in phagocytosis through
CC       organization of the F-actin cytoskeleton associated with forming
CC       phagocytic cups. {ECO:0000250|UniProtKB:P60766,
CC       ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15642749,
CC       ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:26465210}.
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange
CC       factors (GEFs) which promote the exchange of bound GDP for free
CC       GTP, GTPase activating proteins (GAPs) which increase the GTP
CC       hydrolysis activity, and GDP dissociation inhibitors which inhibit
CC       the dissociation of the nucleotide from the GTPase.
CC       {ECO:0000269|PubMed:12172552}.
CC   -!- SUBUNIT: Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4,
CC       CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-
CC       dependent manner) (PubMed:10490598, PubMed:10816584,
CC       PubMed:10954424, PubMed:11260256). Interacts with activated CSPG4
CC       and with BAIAP2 (PubMed:10587647, PubMed:11130076). Interacts with
CC       activated CSPG4 and with BAIAP2 (By similarity). Interacts with
CC       DOCK11/Zizimin2; the interaction activates CDC42 by exchanging GDP
CC       for GTP (By similarity). Interacts with DOCK9; the interaction
CC       activates CDC42 by exchanging GDP for GTP (PubMed:12172552,
CC       PubMed:19745154). Interacts with DOCK8 (via DHR-2 domain); the
CC       interaction activates CDC42 by exchanging GDP for GTP
CC       (PubMed:12172552). Interacts with IQGAP1 (By similarity).
CC       Interacts with NET1 and ARHGAP33/TCGAP (By similarity). Part of a
CC       complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ
CC       (PubMed:11260256). The GTP-bound form interacts with CCPG1 (By
CC       similarity). Interacts with USP6 (PubMed:12612085). Interacts with
CC       NEK6 (PubMed:20873783). Part of a collagen stimulated complex
CC       involved in cell migration composed of CDC42, CRK, TNK2 and
CC       BCAR1/p130cas (PubMed:17038317). Interacts with ITGB1BP1
CC       (PubMed:11807099). Interacts with ARHGDIA; this interaction
CC       inactivates and stabilizes CDC42 (PubMed:23434736). Interacts with
CC       ARHGDIB; this maintains CDC42 in the inactive, GDP-bound form
CC       (PubMed:7512369). Interacts (in GTP-bound form) with FNBP1L and
CC       ABI1, but only in the presence of FNBP1L (PubMed:19798448). May
CC       interact with ARHGEF16; responsible for the activation of CDC42 by
CC       the viral protein HPV16 E6 (PubMed:21139582).
CC       {ECO:0000250|UniProtKB:P60766, ECO:0000269|PubMed:10490598,
CC       ECO:0000269|PubMed:10587647, ECO:0000269|PubMed:10816584,
CC       ECO:0000269|PubMed:10954424, ECO:0000269|PubMed:11130076,
CC       ECO:0000269|PubMed:11260256, ECO:0000269|PubMed:11807099,
CC       ECO:0000269|PubMed:12172552, ECO:0000269|PubMed:12612085,
CC       ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:19745154,
CC       ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:20873783,
CC       ECO:0000269|PubMed:21139582, ECO:0000269|PubMed:22461490,
CC       ECO:0000269|PubMed:23434736, ECO:0000269|PubMed:7512369}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-81752, EBI-81752;
CC       O95477:ABCA1; NbExp=2; IntAct=EBI-81752, EBI-784112;
CC       P25054:APC; NbExp=9; IntAct=EBI-81752, EBI-727707;
CC       Q07960:ARHGAP1; NbExp=3; IntAct=EBI-287394, EBI-602762;
CC       Q14155:ARHGEF7; NbExp=3; IntAct=EBI-287394, EBI-717515;
CC       Q9UQB8:BAIAP2; NbExp=2; IntAct=EBI-81752, EBI-525456;
CC       Q9UQB8-4:BAIAP2; NbExp=5; IntAct=EBI-287394, EBI-6174091;
CC       Q9VEX9:Bin1 (xeno); NbExp=2; IntAct=EBI-81752, EBI-129424;
CC       Q5VT25:CDC42BPA; NbExp=5; IntAct=EBI-81752, EBI-689171;
CC       Q00587:CDC42EP1; NbExp=6; IntAct=EBI-81752, EBI-744130;
CC       O14613:CDC42EP2; NbExp=7; IntAct=EBI-81752, EBI-3438291;
CC       P46940:IQGAP1; NbExp=4; IntAct=EBI-81752, EBI-297509;
CC       Q15811:ITSN1; NbExp=2; IntAct=EBI-3625591, EBI-602041;
CC       Q5S007:LRRK2; NbExp=3; IntAct=EBI-81752, EBI-5323863;
CC       Q9R8E4:map (xeno); NbExp=5; IntAct=EBI-287394, EBI-15794593;
CC       Q16584:MAP3K11; NbExp=3; IntAct=EBI-81752, EBI-49961;
CC       P45983:MAPK8; NbExp=2; IntAct=EBI-81752, EBI-286483;
CC       Q96L34:MARK4; NbExp=2; IntAct=EBI-81752, EBI-302319;
CC       Q64096:Mcf2l (xeno); NbExp=4; IntAct=EBI-287394, EBI-602123;
CC       Q13153:PAK1; NbExp=12; IntAct=EBI-81752, EBI-1307;
CC       Q13177:PAK2; NbExp=6; IntAct=EBI-81752, EBI-1045887;
CC       O75914:PAK3; NbExp=2; IntAct=EBI-287394, EBI-3389553;
CC       Q61036:Pak3 (xeno); NbExp=3; IntAct=EBI-81752, EBI-457317;
CC       O96013:PAK4; NbExp=2; IntAct=EBI-81752, EBI-713738;
CC       Q9P286:PAK5; NbExp=3; IntAct=EBI-81752, EBI-741896;
CC       Q9NPB6:PARD6A; NbExp=7; IntAct=EBI-81752, EBI-81876;
CC       Q9BYG5:PARD6B; NbExp=14; IntAct=EBI-81752, EBI-295391;
CC       Q9JK83:Pard6b (xeno); NbExp=6; IntAct=EBI-81752, EBI-81861;
CC       Q9BYG4:PARD6G; NbExp=5; IntAct=EBI-81752, EBI-295417;
CC       Q8TCU6:PREX1; NbExp=2; IntAct=EBI-287394, EBI-1046542;
CC       P41743:PRKCI; NbExp=5; IntAct=EBI-81752, EBI-286199;
CC       A0A0H3NA16:sopB (xeno); NbExp=2; IntAct=EBI-81752, EBI-10726187;
CC       O30916:sopB (xeno); NbExp=5; IntAct=EBI-81752, EBI-11167349;
CC       O52623:sopE (xeno); NbExp=2; IntAct=EBI-81752, EBI-602254;
CC       Q07912:TNK2; NbExp=2; IntAct=EBI-287394, EBI-603457;
CC       P42768:WAS; NbExp=9; IntAct=EBI-81752, EBI-346375;
CC       O00401:WASL; NbExp=3; IntAct=EBI-81752, EBI-957615;
CC       O08816:Wasl (xeno); NbExp=2; IntAct=EBI-81752, EBI-6142604;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:15642749}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:15642749}. Midbody
CC       {ECO:0000269|PubMed:15642749}. Note=Localizes to spindle during
CC       prometaphase cells. Moves to the central spindle as cells
CC       progressed through anaphase to telophase (PubMed:15642749).
CC       Localizes at the end of cytokinesis in the intercellular bridge
CC       formed between two daughter cells (PubMed:15642749). Its
CC       localization is regulated by the activities of guanine nucleotide
CC       exchange factor ECT2 and GTPase activating protein RACGAP1
CC       (PubMed:15642749). Colocalizes with NEK6 in the centrosome
CC       (PubMed:20873783). In its active GTP-bound form localizes to the
CC       leading edge membrane of migrating dendritic cells (By
CC       similarity). {ECO:0000250|UniProtKB:P60766,
CC       ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:20873783}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=Placental;
CC         IsoId=P60953-2, P21181-4;
CC         Sequence=Displayed;
CC       Name=1; Synonyms=Brain;
CC         IsoId=P60953-1, P21181-1;
CC         Sequence=VSP_040583, VSP_040584;
CC   -!- PTM: (Microbial infection) AMPylation at Tyr-32 and Thr-35 are
CC       mediated by bacterial enzymes in case of infection by H.somnus and
CC       V.parahaemolyticus, respectively. AMPylation occurs in the
CC       effector region and leads to inactivation of the GTPase activity
CC       by preventing the interaction with downstream effectors, thereby
CC       inhibiting actin assembly in infected cells. It is unclear whether
CC       some human enzyme mediates AMPylation; FICD has such ability in
CC       vitro but additional experiments remain to be done to confirm
CC       results in vivo. {ECO:0000269|PubMed:19039103,
CC       ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:20622875}.
CC   -!- PTM: Phosphorylated by SRC in an EGF-dependent manner, this
CC       stimulates the binding of the Rho-GDP dissociation inhibitor
CC       RhoGDI. {ECO:0000269|PubMed:14506284}.
CC   -!- PTM: (Microbial infection) Glycosylated at Tyr-32 by Photorhabdus
CC       asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230
CC       inhibits downstream signaling by an impaired interaction with
CC       diverse regulator and effector proteins of CDC42 and leads to
CC       actin disassembly. {ECO:0000269|PubMed:24141704}.
CC   -!- DISEASE: Takenouchi-Kosaki syndrome (TKS) [MIM:616737]: A syndrome
CC       characterized by macrothrombocytopenia, lymphedema, mental
CC       retardation, developmental delay, and distinctive facial features.
CC       {ECO:0000269|PubMed:26386261, ECO:0000269|PubMed:26708094}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       CDC42 subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CDC42ID40012ch1p36.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/cdc42/";
DR   EMBL; M35543; AAA52494.1; -; mRNA.
DR   EMBL; M57298; AAA52592.1; -; mRNA.
DR   EMBL; AL121734; CAB57325.1; -; mRNA.
DR   EMBL; AL121735; CAB57326.1; -; mRNA.
DR   EMBL; AF498962; AAM21109.1; -; mRNA.
DR   EMBL; AF498963; AAM21110.1; -; mRNA.
DR   EMBL; AY673602; AAT70721.1; -; Genomic_DNA.
DR   EMBL; AL031281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002711; AAH02711.1; -; mRNA.
DR   EMBL; BC003682; AAH03682.1; -; mRNA.
DR   EMBL; BC018266; AAH18266.1; -; mRNA.
DR   CCDS; CCDS221.1; -.
DR   CCDS; CCDS222.1; -. [P60953-1]
DR   PIR; A36382; A36382.
DR   PIR; A39265; A39265.
DR   RefSeq; NP_001034891.1; NM_001039802.1. [P60953-2]
DR   RefSeq; NP_001782.1; NM_001791.3. [P60953-2]
DR   RefSeq; NP_426359.1; NM_044472.2. [P60953-1]
DR   PDB; 1A4R; X-ray; 2.50 A; A/B=1-191.
DR   PDB; 1AJE; NMR; -; A=1-187.
DR   PDB; 1AM4; X-ray; 2.70 A; D/E/F=2-177.
DR   PDB; 1AN0; X-ray; 2.80 A; A/B=1-190.
DR   PDB; 1CEE; NMR; -; A=1-179.
DR   PDB; 1CF4; NMR; -; A=1-184.
DR   PDB; 1DOA; X-ray; 2.60 A; A=1-188.
DR   PDB; 1E0A; NMR; -; A=1-184.
DR   PDB; 1EES; NMR; -; A=1-178.
DR   PDB; 1GRN; X-ray; 2.10 A; A=1-191.
DR   PDB; 1GZS; X-ray; 2.30 A; A/C=1-178.
DR   PDB; 1KI1; X-ray; 2.30 A; A/C=1-188.
DR   PDB; 1KZ7; X-ray; 2.40 A; B/D=1-188.
DR   PDB; 1KZG; X-ray; 2.60 A; B/D=1-188.
DR   PDB; 1NF3; X-ray; 2.10 A; A/B=2-191.
DR   PDB; 2ASE; NMR; -; A=1-178.
DR   PDB; 2DFK; X-ray; 2.15 A; B/D=1-191.
DR   PDB; 2KB0; NMR; -; A=1-178.
DR   PDB; 2NGR; X-ray; 1.90 A; A=1-191.
DR   PDB; 2ODB; X-ray; 2.40 A; A=1-191.
DR   PDB; 2QRZ; X-ray; 2.40 A; A/B=1-189.
DR   PDB; 2WM9; X-ray; 2.20 A; B=1-188.
DR   PDB; 2WMN; X-ray; 2.39 A; B=1-188.
DR   PDB; 2WMO; X-ray; 2.20 A; B=1-188.
DR   PDB; 3GCG; X-ray; 2.30 A; A=2-178.
DR   PDB; 3QBV; X-ray; 2.65 A; A/C=1-178.
DR   PDB; 3VHL; X-ray; 2.08 A; B=1-188.
DR   PDB; 4DID; X-ray; 2.35 A; A=1-183.
DR   PDB; 4ITR; X-ray; 2.30 A; C/D=1-191.
DR   PDB; 4JS0; X-ray; 1.90 A; A=1-178.
DR   PDB; 4YC7; X-ray; 2.50 A; A=1-179.
DR   PDB; 4YDH; X-ray; 3.80 A; B/D=1-179.
DR   PDB; 5CJP; X-ray; 2.60 A; A/B/C/D=1-177.
DR   PDB; 5FI1; X-ray; 3.20 A; B=1-191.
DR   PDB; 5HZK; X-ray; 3.30 A; A/C=1-181.
DR   PDB; 5UPK; X-ray; 2.40 A; C=1-177.
DR   PDB; 5UPL; X-ray; 3.00 A; B=1-177.
DR   PDBsum; 1A4R; -.
DR   PDBsum; 1AJE; -.
DR   PDBsum; 1AM4; -.
DR   PDBsum; 1AN0; -.
DR   PDBsum; 1CEE; -.
DR   PDBsum; 1CF4; -.
DR   PDBsum; 1DOA; -.
DR   PDBsum; 1E0A; -.
DR   PDBsum; 1EES; -.
DR   PDBsum; 1GRN; -.
DR   PDBsum; 1GZS; -.
DR   PDBsum; 1KI1; -.
DR   PDBsum; 1KZ7; -.
DR   PDBsum; 1KZG; -.
DR   PDBsum; 1NF3; -.
DR   PDBsum; 2ASE; -.
DR   PDBsum; 2DFK; -.
DR   PDBsum; 2KB0; -.
DR   PDBsum; 2NGR; -.
DR   PDBsum; 2ODB; -.
DR   PDBsum; 2QRZ; -.
DR   PDBsum; 2WM9; -.
DR   PDBsum; 2WMN; -.
DR   PDBsum; 2WMO; -.
DR   PDBsum; 3GCG; -.
DR   PDBsum; 3QBV; -.
DR   PDBsum; 3VHL; -.
DR   PDBsum; 4DID; -.
DR   PDBsum; 4ITR; -.
DR   PDBsum; 4JS0; -.
DR   PDBsum; 4YC7; -.
DR   PDBsum; 4YDH; -.
DR   PDBsum; 5CJP; -.
DR   PDBsum; 5FI1; -.
DR   PDBsum; 5HZK; -.
DR   PDBsum; 5UPK; -.
DR   PDBsum; 5UPL; -.
DR   SMR; P60953; -.
DR   BioGrid; 107433; 223.
DR   CORUM; P60953; -.
DR   DIP; DIP-31097N; -.
DR   ELM; P60953; -.
DR   IntAct; P60953; 221.
DR   MINT; P60953; -.
DR   STRING; 9606.ENSP00000383118; -.
DR   BindingDB; P60953; -.
DR   ChEMBL; CHEMBL6088; -.
DR   DrugBank; DB02623; Aminophosphonic Acid-Guanylate Ester.
DR   DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR   MoonDB; P60953; Predicted.
DR   iPTMnet; P60953; -.
DR   PhosphoSitePlus; P60953; -.
DR   SwissPalm; P60953; -.
DR   BioMuta; CDC42; -.
DR   DMDM; 322510015; -.
DR   EPD; P60953; -.
DR   jPOST; P60953; -.
DR   PaxDb; P60953; -.
DR   PeptideAtlas; P60953; -.
DR   PRIDE; P60953; -.
DR   ProteomicsDB; 57238; -.
DR   ProteomicsDB; 57239; -. [P60953-1]
DR   TopDownProteomics; P60953-2; -. [P60953-2]
DR   DNASU; 998; -.
DR   Ensembl; ENST00000315554; ENSP00000314458; ENSG00000070831. [P60953-1]
DR   Ensembl; ENST00000344548; ENSP00000341072; ENSG00000070831. [P60953-2]
DR   Ensembl; ENST00000400259; ENSP00000383118; ENSG00000070831. [P60953-2]
DR   GeneID; 998; -.
DR   KEGG; hsa:998; -.
DR   UCSC; uc001bfp.4; human.
DR   CTD; 998; -.
DR   DisGeNET; 998; -.
DR   GeneCards; CDC42; -.
DR   HGNC; HGNC:1736; CDC42.
DR   HPA; CAB004360; -.
DR   HPA; HPA069590; -.
DR   MalaCards; CDC42; -.
DR   MIM; 116952; gene.
DR   MIM; 616737; phenotype.
DR   neXtProt; NX_P60953; -.
DR   OpenTargets; ENSG00000070831; -.
DR   Orphanet; 487796; Macrothrombocytopenia-lymphedema-developmental delay-facial dysmorphism-camptodactyly syndrome.
DR   PharmGKB; PA26266; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   eggNOG; COG1100; LUCA.
DR   GeneTree; ENSGT00940000153675; -.
DR   HOGENOM; HOG000233974; -.
DR   InParanoid; P60953; -.
DR   KO; K04393; -.
DR   OMA; HEQGERL; -.
DR   OrthoDB; 1091615at2759; -.
DR   PhylomeDB; P60953; -.
DR   TreeFam; TF101109; -.
DR   Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR   Reactome; R-HSA-182971; EGFR downregulation.
DR   Reactome; R-HSA-194840; Rho GTPase cycle.
DR   Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
DR   Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-HSA-418885; DCC mediated attractive signaling.
DR   Reactome; R-HSA-428543; Inactivation of CDC42 and RAC1.
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-525793; Myogenesis.
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-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR   Reactome; R-HSA-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR   SignaLink; P60953; -.
DR   SIGNOR; P60953; -.
DR   ChiTaRS; CDC42; human.
DR   EvolutionaryTrace; P60953; -.
DR   GeneWiki; CDC42; -.
DR   GenomeRNAi; 998; -.
DR   PMAP-CutDB; P60953; -.
DR   PRO; PR:P60953; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000070831; Expressed in 231 organ(s), highest expression level in testis.
DR   ExpressionAtlas; P60953; baseline and differential.
DR   Genevisible; P60953; HS.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0043197; C:dendritic spine; IDA:SynGO.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:BHF-UCL.
DR   GO; GO:0017119; C:Golgi transport complex; IMP:CAFA.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR   GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR   GO; GO:0034191; F:apolipoprotein A-I receptor binding; IPI:BHF-UCL.
DR   GO; GO:0032427; F:GBD domain binding; IPI:CAFA.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
DR   GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:AgBase.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR   GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB.
DR   GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR   GO; GO:0051683; P:establishment of Golgi localization; ISS:BHF-UCL.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0007030; P:Golgi organization; ISS:BHF-UCL.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0030225; P:macrophage differentiation; TAS:UniProtKB.
DR   GO; GO:0099563; P:modification of synaptic structure; IBA:GO_Central.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0031333; P:negative regulation of protein complex assembly; IPI:UniProtKB.
DR   GO; GO:0038189; P:neuropilin signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0072384; P:organelle transport along microtubule; ISS:BHF-UCL.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR   GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:AgBase.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:BHF-UCL.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:CAFA.
DR   GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
DR   GO; GO:0031274; P:positive regulation of pseudopodium assembly; IDA:UniProtKB.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:BHF-UCL.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR   GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
DR   GO; GO:0010591; P:regulation of lamellipodium assembly; IGI:CAFA.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0051492; P:regulation of stress fiber assembly; IGI:CAFA.
DR   GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR   GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR   GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0039694; P:viral RNA genome replication; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR   CDD; cd01874; Cdc42; 1.
DR   InterPro; IPR037874; Cdc42.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   Pfam; PF00071; Ras; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P60953.
DR   SWISS-2DPAGE; P60953.
KW   3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Differentiation; Direct protein sequencing;
KW   Disease mutation; Glycoprotein; GTP-binding; Lipoprotein; Membrane;
KW   Mental retardation; Methylation; Neurogenesis; Nucleotide-binding;
KW   Phosphoprotein; Prenylation; Reference proteome.
FT   CHAIN         1    188       Cell division control protein 42 homolog.
FT                                /FTId=PRO_0000030425.
FT   PROPEP      189    191       Removed in mature form.
FT                                /FTId=PRO_0000030426.
FT   NP_BIND      10     17       GTP.
FT   NP_BIND      57     61       GTP. {ECO:0000250}.
FT   NP_BIND     115    118       GTP.
FT   MOTIF        32     40       Effector region. {ECO:0000255}.
FT   MOD_RES      32     32       O-AMP-tyrosine; by Haemophilus IbpA;
FT                                alternate. {ECO:0000269|PubMed:19362538,
FT                                ECO:0000269|PubMed:20622875}.
FT   MOD_RES      35     35       O-AMP-threonine; by Vibrio VopS.
FT                                {ECO:0000269|PubMed:19039103}.
FT   MOD_RES      64     64       Phosphotyrosine; by SRC.
FT                                {ECO:0000269|PubMed:14506284}.
FT   MOD_RES     188    188       Cysteine methyl ester.
FT                                {ECO:0000244|PDB:1DOA,
FT                                ECO:0000269|PubMed:10676816}.
FT   LIPID       188    188       S-geranylgeranyl cysteine.
FT                                {ECO:0000244|PDB:1DOA,
FT                                ECO:0000269|PubMed:10676816}.
FT   CARBOHYD     32     32       O-linked (GlcNAc) tyrosine; by
FT                                Photorhabdus PAU_02230; alternate.
FT                                {ECO:0000269|PubMed:24141704}.
FT   VAR_SEQ     163    163       K -> R (in isoform 1).
FT                                {ECO:0000303|PubMed:2122236,
FT                                ECO:0000303|Ref.3, ECO:0000303|Ref.4}.
FT                                /FTId=VSP_040583.
FT   VAR_SEQ     182    191       PKKSRRCVLL -> TQPKRKCCIF (in isoform 1).
FT                                {ECO:0000303|PubMed:2122236,
FT                                ECO:0000303|Ref.3, ECO:0000303|Ref.4}.
FT                                /FTId=VSP_040584.
FT   VARIANT      64     64       Y -> C (in TKS; dbSNP:rs864309721).
FT                                {ECO:0000269|PubMed:26386261,
FT                                ECO:0000269|PubMed:26708094}.
FT                                /FTId=VAR_076337.
FT   MUTAGEN      12     12       G->V: Constitutively active. Interacts
FT                                with PARD6 proteins. Does not inhibit
FT                                filopodia formation. No effect on NR3C2
FT                                transcriptional activity.
FT                                {ECO:0000269|PubMed:10954424,
FT                                ECO:0000269|PubMed:14978216,
FT                                ECO:0000269|PubMed:19029984}.
FT   MUTAGEN      17     17       T->N: Constitutively inactive. Does not
FT                                interact with PARD6 proteins. Inhibits
FT                                filopodia formation. No effect on NR3C2
FT                                transcriptional activity.
FT                                {ECO:0000269|PubMed:11260256,
FT                                ECO:0000269|PubMed:14978216,
FT                                ECO:0000269|PubMed:19029984}.
FT   MUTAGEN      32     32       Y->F: Abolishes AMPylation by Haemophilus
FT                                IbpA. {ECO:0000269|PubMed:19362538}.
FT   MUTAGEN      61     61       Q->L: Constitutively active. Interacts
FT                                with PARD6 proteins.
FT                                {ECO:0000269|PubMed:11260256}.
FT   STRAND        2     11       {ECO:0000244|PDB:2NGR}.
FT   STRAND       12     14       {ECO:0000244|PDB:5UPL}.
FT   HELIX        16     25       {ECO:0000244|PDB:2NGR}.
FT   HELIX        29     31       {ECO:0000244|PDB:3VHL}.
FT   STRAND       36     46       {ECO:0000244|PDB:2NGR}.
FT   STRAND       49     58       {ECO:0000244|PDB:2NGR}.
FT   HELIX        62     64       {ECO:0000244|PDB:2NGR}.
FT   TURN         65     67       {ECO:0000244|PDB:2NGR}.
FT   HELIX        68     71       {ECO:0000244|PDB:2NGR}.
FT   STRAND       72     74       {ECO:0000244|PDB:3QBV}.
FT   STRAND       76     83       {ECO:0000244|PDB:2NGR}.
FT   HELIX        87     95       {ECO:0000244|PDB:2NGR}.
FT   HELIX        97    104       {ECO:0000244|PDB:2NGR}.
FT   STRAND      105    107       {ECO:0000244|PDB:2WMN}.
FT   STRAND      110    115       {ECO:0000244|PDB:2NGR}.
FT   HELIX       117    121       {ECO:0000244|PDB:2NGR}.
FT   HELIX       123    130       {ECO:0000244|PDB:2NGR}.
FT   TURN        131    133       {ECO:0000244|PDB:2NGR}.
FT   HELIX       139    148       {ECO:0000244|PDB:2NGR}.
FT   STRAND      154    156       {ECO:0000244|PDB:2NGR}.
FT   TURN        159    161       {ECO:0000244|PDB:2NGR}.
FT   TURN        162    164       {ECO:0000244|PDB:2KB0}.
FT   HELIX       165    176       {ECO:0000244|PDB:2NGR}.
FT   STRAND      179    181       {ECO:0000244|PDB:1NF3}.
FT   TURN        184    186       {ECO:0000244|PDB:1NF3}.
SQ   SEQUENCE   191 AA;  21259 MW;  51A437E22A4D8FFF CRC64;
     MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG
     QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR
     DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP
     EPKKSRRCVL L
//

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