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Cell division control protein 42 homolog (G25K GTP-binding protein)

 CDC42_HUMAN             Reviewed;         191 AA.
P60953; P21181; P25763; Q7L8R5; Q9UDI2;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 2.
25-OCT-2017, entry version 178.
RecName: Full=Cell division control protein 42 homolog;
AltName: Full=G25K GTP-binding protein;
Flags: Precursor;
Name=CDC42;
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 1).
TISSUE=Fetal brain;
PubMed=2122236; DOI=10.1128/MCB.10.11.5977;
Munemitsu S., Innis M.A., Clark R., McCormick F., Ullrich A.,
Polakis P.;
"Molecular cloning and expression of a G25K cDNA, the human homolog of
the yeast cell cycle gene CDC42.";
Mol. Cell. Biol. 10:5977-5982(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=2124704; DOI=10.1073/pnas.87.24.9853;
Shinjo K., Koland J.G., Hart M.J., Narasimhan V., Johnson D.I.,
Evans T., Cerione R.A.;
"Molecular cloning of the gene for the human placental GTP-binding
protein Gp (G25K): identification of this GTP-binding protein as the
human homolog of the yeast cell-division-cycle protein CDC42.";
Proc. Natl. Acad. Sci. U.S.A. 87:9853-9857(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Rhodes S., Huckle E.;
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Placenta;
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.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cervix, Placenta, and Uterus;
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).
[8]
PROTEIN SEQUENCE OF 67-83 (ISOFORM 2), PARTIAL PROTEIN SEQUENCE
(ISOFORM 1), AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 97-107; 134-144 AND 167-183 (ISOFORM 2).
TISSUE=Neutrophil;
PubMed=8504089; DOI=10.1021/bi00072a029;
Kwong C.H., Malech H.L., Rotrosen D., Leto T.L.;
"Regulation of the human neutrophil NADPH oxidase by rho-related G-
proteins.";
Biochemistry 32:5711-5717(1993).
[10]
PARTIAL PROTEIN SEQUENCE.
PubMed=2496687; DOI=10.1016/0006-291X(89)91615-X;
Polakis P.G., Snyderman R., Evans T.;
"Characterization of G25K, a GTP-binding protein containing a novel
putative nucleotide binding domain.";
Biochem. Biophys. Res. Commun. 160:25-32(1989).
[11]
INTERACTION WITH ARHGDIB.
PubMed=7512369; DOI=10.1002/gcc.2870080408;
Adra C.N., Ko J., Leonard D., Wirth L.J., Cerione R.A., Lim B.;
"Identification of a novel protein with GDP dissociation inhibitor
activity for the ras-like proteins CDC42Hs and rac I.";
Genes Chromosomes Cancer 8:253-261(1993).
[12]
INTERACTION WITH CDC42EP1; CDC42EP2; CDC42EP3 AND CDC42EP5.
TISSUE=Embryo;
PubMed=10490598; DOI=10.1128/MCB.19.10.6585;
Joberty G., Perlungher R.R., Macara I.G.;
"The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
proteins.";
Mol. Cell. Biol. 19:6585-6597(1999).
[13]
INTERACTION WITH CSPG4.
PubMed=10587647; DOI=10.1038/70302;
Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L.,
Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.;
"Melanoma chondroitin sulphate proteoglycan regulates cell spreading
through Cdc42, Ack-1 and p130cas.";
Nat. Cell Biol. 1:507-513(1999).
[14]
INTERACTION WITH CDC42SE1 AND CDC42SE2.
PubMed=10816584; DOI=10.1074/jbc.M002832200;
Pirone D.M., Fukuhara S., Gutkind J.S., Burbelo P.D.;
"SPECs, small binding proteins for Cdc42.";
J. Biol. Chem. 275:22650-22656(2000).
[15]
INTERACTION WITH PARD6A, AND MUTAGENESIS OF GLY-12.
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).
[16]
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).
[17]
INTERACTION WITH PARD6A; PARD6B AND PARD6G, SUBUNIT OF A COMPLEX
CONTAINING PRKCI AND PARD6B, AND MUTAGENESIS OF THR-17 AND GLN-61.
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).
[18]
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).
[19]
INTERACTION WITH DOCK9, AND ACTIVATION BY DOCK9.
PubMed=12172552; DOI=10.1038/ncb835;
Meller N., Irani-Tehrani M., Kiosses W.B., Del Pozo M.A.,
Schwartz M.A.;
"Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho
proteins.";
Nat. Cell Biol. 4:639-647(2002).
[20]
PHOSPHORYLATION AT TYR-64 BY SRC.
PubMed=14506284; DOI=10.1074/jbc.M307021200;
Tu S., Wu W.J., Wang J., Cerione R.A.;
"Epidermal growth factor-dependent regulation of Cdc42 is mediated by
the Src tyrosine kinase.";
J. Biol. Chem. 278:49293-49300(2003).
[21]
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).
[22]
FUNCTION, AND MUTAGENESIS OF GLY-12 AND THR-17.
PubMed=14978216; DOI=10.1091/mbc.E03-07-0493;
Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.;
"Regulation of dendritic branching and filopodia formation in
hippocampal neurons by specific acylated protein motifs.";
Mol. Biol. Cell 15:2205-2217(2004).
[23]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15642749; DOI=10.1083/jcb.200408085;
Oceguera-Yanez F., Kimura K., Yasuda S., Higashida C., Kitamura T.,
Hiraoka Y., Haraguchi T., Narumiya S.;
"Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in
mitosis.";
J. Cell Biol. 168:221-232(2005).
[24]
FUNCTION IN CELL MIGRATION, AND INTERACTION WITH BCAR1; TNK2 AND CRK.
PubMed=17038317; DOI=10.1074/jbc.M604342200;
Modzelewska K., Newman L.P., Desai R., Keely P.J.;
"Ack1 mediates Cdc42-dependent cell migration and signaling to
p130Cas.";
J. Biol. Chem. 281:37527-37535(2006).
[25]
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).
[26]
AMPYLATION AT TYR-32 (MICROBIAL INFECTION), 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).
[27]
INTERACTION WITH FNBP1L.
PubMed=19798448; DOI=10.1371/journal.pgen.1000675;
Giuliani C., Troglio F., Bai Z., Patel F.B., Zucconi A.,
Malabarba M.G., Disanza A., Stradal T.B., Cassata G., Confalonieri S.,
Hardin J.D., Soto M.C., Grant B.D., Scita G.;
"Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics
and membrane trafficking during Caenorhabditis elegans oocyte growth
and embryonic epidermal morphogenesis.";
PLoS Genet. 5:E1000675-E1000675(2009).
[28]
AMPYLATION AT THR-35 (MICROBIAL INFECTION).
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).
[29]
SUBCELLULAR LOCATION, AND INTERACTION WITH NEK6.
PubMed=20873783; DOI=10.1021/pr100562w;
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C.,
Santana Bernachi J., Paes Leme A.F., Kobarg J.;
"Characterization of hNek6 interactome reveals an important role for
its short N-terminal domain and colocalization with proteins at the
centrosome.";
J. Proteome Res. 9:6298-6316(2010).
[30]
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).
[31]
INTERACTION WITH ARHGEF16.
PubMed=21139582; DOI=10.1038/sj.bjc.6606026;
Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L.,
Hampson I.N.;
"The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which
activates Cdc42.";
Br. J. Cancer 104:324-331(2011).
[32]
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).
[33]
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).
[34]
FUNCTION.
PubMed=26465210; DOI=10.1038/ncomms9623;
Schlam D., Bagshaw R.D., Freeman S.A., Collins R.F., Pawson T.,
Fairn G.D., Grinstein S.;
"Phosphoinositide 3-kinase enables phagocytosis of large particles by
terminating actin assembly through Rac/Cdc42 GTPase-activating
proteins.";
Nat. Commun. 6:8623-8623(2015).
[35]
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).
[36]
STRUCTURE BY NMR.
PubMed=9220962; DOI=10.1021/bi970694x;
Feltham J.L., Dotsch V., Raza S., Manor D., Cerione R.A.,
Sutcliffe M.J., Wagner G., Oswald R.E.;
"Definition of the switch surface in the solution structure of
Cdc42Hs.";
Biochemistry 36:8755-8766(1997).
[37]
STRUCTURE BY NMR.
PubMed=9760238; DOI=10.1021/bi981352+;
Guo W., Sutcliffe M.J., Cerione R.A., Oswald R.E.;
"Identification of the binding surface on Cdc42Hs for p21-activated
kinase.";
Biochemistry 37:14030-14037(1998).
[38]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH RHOGAP.
PubMed=9262406; DOI=10.1038/41805;
Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D.,
Laue E., Gamblin S.J., Smerdon S.J.;
"Crystal structure of a small G protein in complex with the GTPase-
activating protein rhoGAP.";
Nature 388:693-697(1997).
[39]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF VAL-12 MUTANT.
PubMed=10211824; DOI=10.1110/ps.8.4.778;
Rudolph M.G., Wittinghofer A., Vetter I.R.;
"Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray
diffraction and fluorescence spectroscopy: two different nucleotide
states in one crystal.";
Protein Sci. 8:778-787(1999).
[40]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Kongsaeree P., Cerione R.A., Clardy J.C.;
"The structure determination of CDC42Hs and GDP complex.";
Submitted (JUN-1997) to the PDB data bank.
[41] {ECO:0000244|PDB:1DOA}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-188, ISOPRENYLATION AT
CYS-188, AND METHYLATION AT CYS-188.
PubMed=10676816; DOI=10.1016/S0092-8674(00)80670-4;
Hoffman G.R., Nassar N., Cerione R.A.;
"Structure of the Rho family GTP-binding protein Cdc42 in complex with
the multifunctional regulator RhoGDI.";
Cell 100:345-356(2000).
[42]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-188 IN COMPLEX WITH DOCK9.
PubMed=19745154; DOI=10.1126/science.1174468;
Yang J., Zhang Z., Roe S.M., Marshall C.J., Barford D.;
"Activation of Rho GTPases by DOCK exchange factors is mediated by a
nucleotide sensor.";
Science 325:1398-1402(2009).
[43]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-181 IN COMPLEX WITH
H.SOMNUS IBPA AND GDP, AND AMPYLATION AT TYR-32 (MICROBIAL INFECTION).
PubMed=20622875; DOI=10.1038/nsmb.1867;
Xiao J., Worby C.A., Mattoo S., Sankaran B., Dixon J.E.;
"Structural basis of Fic-mediated adenylylation.";
Nat. Struct. Mol. Biol. 17:1004-1010(2010).
[44]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-188 IN COMPLEX WITH MOUSE
DOCK8, AND ENZYME REGULATION.
PubMed=22461490; DOI=10.1182/blood-2012-01-407098;
Harada Y., Tanaka Y., Terasawa M., Pieczyk M., Habiro K., Katakai T.,
Hanawa-Suetsugu K., Kukimoto-Niino M., Nishizaki T., Shirouzu M.,
Duan X., Uruno T., Nishikimi A., Sanematsu F., Yokoyama S.,
Stein J.V., Kinashi T., Fukui Y.;
"DOCK8 is a Cdc42 activator critical for interstitial dendritic cell
migration during immune responses.";
Blood 119:4451-4461(2012).
[45]
INVOLVEMENT IN TKS, AND VARIANT TKS CYS-64.
PubMed=26386261; DOI=10.1002/ajmg.a.37275;
Takenouchi T., Kosaki R., Niizuma T., Hata K., Kosaki K.;
"Macrothrombocytopenia and developmental delay with a de novo CDC42
mutation: Yet another locus for thrombocytopenia and developmental
delay.";
Am. J. Med. Genet. A 167A:2822-2825(2015).
[46]
VARIANT TKS CYS-64.
PubMed=26708094; DOI=10.1002/ajmg.a.37526;
Takenouchi T., Okamoto N., Ida S., Uehara T., Kosaki K.;
"Further evidence of a mutation in CDC42 as a cause of a recognizable
syndromic form of thrombocytopenia.";
Am. J. Med. Genet. A 170:852-855(2016).
-!- FUNCTION: Plasma membrane-associated small GTPase which cycles
between an active GTP-bound and an inactive GDP-bound state. In
active state binds to a variety of effector proteins to regulate
cellular responses. Involved in epithelial cell polarization
processes. Regulates the bipolar attachment of spindle
microtubules to kinetochores before chromosome congression in
metaphase. Plays a role in the extension and maintenance of the
formation of thin, actin-rich surface projections called
filopodia. Mediates CDC42-dependent cell migration. Required for
DOCK10-mediated spine formation in Purkinje cells and hippocampal
neurons. Facilitates filopodia formation upon DOCK11-activation
(By similarity). Also plays a role in phagocytosis through
organization of the F-actin cytoskeleton associated with forming
phagocytic cups. {ECO:0000250|UniProtKB:P60766,
ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15642749,
ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:26465210}.
-!- 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.
{ECO:0000269|PubMed:12172552}.
-!- SUBUNIT: Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4,
CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-
dependent manner) (PubMed:10490598, PubMed:10816584,
PubMed:10954424, PubMed:11260256). Interacts with activated CSPG4
and with BAIAP2 (PubMed:10587647, PubMed:11130076). Interacts with
activated CSPG4 and with BAIAP2 (By similarity). Interacts with
DOCK11/Zizimin2; the interaction activates CDC42 by exchanging GDP
for GTP (By similarity). Interacts with DOCK9; the interaction
activates CDC42 by exchanging GDP for GTP (PubMed:12172552,
PubMed:19745154). Interacts with DOCK8 (via DHR-2 domain); the
interaction activates CDC42 by exchanging GDP for GTP
(PubMed:12172552). Interacts with IQGAP1 (By similarity).
Interacts with NET1 and ARHGAP33/TCGAP (By similarity). Part of a
complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ
(PubMed:11260256). The GTP-bound form interacts with CCPG1 (By
similarity). Interacts with USP6 (PubMed:12612085). Interacts with
NEK6 (PubMed:20873783). Part of a collagen stimulated complex
involved in cell migration composed of CDC42, CRK, TNK2 and
BCAR1/p130cas (PubMed:17038317). Interacts with ITGB1BP1
(PubMed:11807099). Interacts with ARHGDIA; this interaction
inactivates and stabilizes CDC42 (PubMed:23434736). Interacts with
ARHGDIB; this maintains CDC42 in the inactive, GDP-bound form
(PubMed:7512369). Interacts (in GTP-bound form) with FNBP1L and
ABI1, but only in the presence of FNBP1L (PubMed:19798448). May
interact with ARHGEF16; responsible for the activation of CDC42 by
the viral protein HPV16 E6 (PubMed:21139582).
{ECO:0000250|UniProtKB:P60766, ECO:0000269|PubMed:10490598,
ECO:0000269|PubMed:10587647, ECO:0000269|PubMed:10816584,
ECO:0000269|PubMed:10954424, ECO:0000269|PubMed:11130076,
ECO:0000269|PubMed:11260256, ECO:0000269|PubMed:11807099,
ECO:0000269|PubMed:12172552, ECO:0000269|PubMed:12612085,
ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:19745154,
ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:20873783,
ECO:0000269|PubMed:21139582, ECO:0000269|PubMed:22461490,
ECO:0000269|PubMed:23434736, ECO:0000269|PubMed:7512369}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-81752, EBI-81752;
O95477:ABCA1; NbExp=2; IntAct=EBI-81752, EBI-784112;
Q07960:ARHGAP1; NbExp=3; IntAct=EBI-287394, EBI-602762;
Q14155:ARHGEF7; NbExp=3; IntAct=EBI-287394, EBI-717515;
Q9UQB8:BAIAP2; NbExp=2; IntAct=EBI-287394, EBI-525456;
Q9UQB8-4:BAIAP2; NbExp=5; IntAct=EBI-287394, EBI-6174091;
Q9VEX9:Bin1 (xeno); NbExp=2; IntAct=EBI-81752, EBI-129424;
Q5VT25:CDC42BPA; NbExp=5; IntAct=EBI-81752, EBI-689171;
Q00587:CDC42EP1; NbExp=6; IntAct=EBI-81752, EBI-744130;
O14613:CDC42EP2; NbExp=9; IntAct=EBI-81752, EBI-3438291;
Q9R8E4:ERS085404_04285 (xeno); NbExp=5; IntAct=EBI-287394, EBI-15794593;
P46940:IQGAP1; NbExp=4; IntAct=EBI-81752, EBI-297509;
Q15811:ITSN1; NbExp=2; IntAct=EBI-3625591, EBI-602041;
Q5S007:LRRK2; NbExp=3; IntAct=EBI-81752, EBI-5323863;
Q16584:MAP3K11; NbExp=3; IntAct=EBI-81752, EBI-49961;
P45983:MAPK8; NbExp=2; IntAct=EBI-81752, EBI-286483;
Q96L34:MARK4; NbExp=2; IntAct=EBI-81752, EBI-302319;
Q64096:Mcf2l (xeno); NbExp=4; IntAct=EBI-287394, EBI-602123;
Q13153:PAK1; NbExp=12; IntAct=EBI-81752, EBI-1307;
Q13177:PAK2; NbExp=4; IntAct=EBI-81752, EBI-1045887;
O75914:PAK3; NbExp=2; IntAct=EBI-287394, EBI-3389553;
Q61036:Pak3 (xeno); NbExp=3; IntAct=EBI-81752, EBI-457317;
O96013:PAK4; NbExp=2; IntAct=EBI-81752, EBI-713738;
Q9P286:PAK5; NbExp=3; IntAct=EBI-81752, EBI-741896;
Q9NPB6:PARD6A; NbExp=7; IntAct=EBI-81752, EBI-81876;
Q9BYG5:PARD6B; NbExp=12; IntAct=EBI-81752, EBI-295391;
Q9JK83:Pard6b (xeno); NbExp=6; IntAct=EBI-81752, EBI-81861;
Q9BYG4:PARD6G; NbExp=5; IntAct=EBI-81752, EBI-295417;
Q8TCU6:PREX1; NbExp=2; IntAct=EBI-287394, EBI-1046542;
P41743:PRKCI; NbExp=5; IntAct=EBI-81752, EBI-286199;
A0A0H3NA16:sopB (xeno); NbExp=2; IntAct=EBI-81752, EBI-10726187;
O30916:sopB (xeno); NbExp=5; IntAct=EBI-81752, EBI-11167349;
O52623:sopE (xeno); NbExp=2; IntAct=EBI-81752, EBI-602254;
Q07912:TNK2; NbExp=2; IntAct=EBI-287394, EBI-603457;
P42768:WAS; NbExp=9; IntAct=EBI-81752, EBI-346375;
O00401:WASL; NbExp=3; IntAct=EBI-81752, EBI-957615;
O08816:Wasl (xeno); NbExp=2; IntAct=EBI-81752, EBI-6142604;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:15642749}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:15642749}. Midbody
{ECO:0000269|PubMed:15642749}. Note=Localizes to spindle during
prometaphase cells. Moves to the central spindle as cells
progressed through anaphase to telophase (PubMed:15642749).
Localizes at the end of cytokinesis in the intercellular bridge
formed between two daughter cells (PubMed:15642749). Its
localization is regulated by the activities of guanine nucleotide
exchange factor ECT2 and GTPase activating protein RACGAP1
(PubMed:15642749). Colocalizes with NEK6 in the centrosome
(PubMed:20873783). In its active GTP-bound form localizes to the
leading edge membrane of migrating dendritic cells (By
similarity). {ECO:0000250|UniProtKB:P60766,
ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:20873783}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=Placental;
IsoId=P60953-2, P21181-4;
Sequence=Displayed;
Name=1; Synonyms=Brain;
IsoId=P60953-1, P21181-1;
Sequence=VSP_040583, VSP_040584;
-!- 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, ECO:0000269|PubMed:20622875}.
-!- PTM: Phosphorylated by SRC in an EGF-dependent manner, this
stimulates the binding of the Rho-GDP dissociation inhibitor
RhoGDI. {ECO:0000269|PubMed:14506284}.
-!- 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 CDC42 and leads to
actin disassembly. {ECO:0000269|PubMed:24141704}.
-!- DISEASE: Takenouchi-Kosaki syndrome (TKS) [MIM:616737]: A syndrome
characterized by macrothrombocytopenia, lymphedema, mental
retardation, developmental delay, and distinctive facial features.
{ECO:0000269|PubMed:26386261, ECO:0000269|PubMed:26708094}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CDC42 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CDC42ID40012ch1p36.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdc42/";
-----------------------------------------------------------------------
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EMBL; M35543; AAA52494.1; -; mRNA.
EMBL; M57298; AAA52592.1; -; mRNA.
EMBL; AL121734; CAB57325.1; -; mRNA.
EMBL; AL121735; CAB57326.1; -; mRNA.
EMBL; AF498962; AAM21109.1; -; mRNA.
EMBL; AF498963; AAM21110.1; -; mRNA.
EMBL; AY673602; AAT70721.1; -; Genomic_DNA.
EMBL; AL031281; CAB52602.1; -; Genomic_DNA.
EMBL; AL031281; CAD92551.1; -; Genomic_DNA.
EMBL; BC002711; AAH02711.1; -; mRNA.
EMBL; BC003682; AAH03682.1; -; mRNA.
EMBL; BC018266; AAH18266.1; -; mRNA.
CCDS; CCDS221.1; -.
CCDS; CCDS222.1; -. [P60953-1]
PIR; A36382; A36382.
PIR; A39265; A39265.
RefSeq; NP_001034891.1; NM_001039802.1. [P60953-2]
RefSeq; NP_001782.1; NM_001791.3. [P60953-2]
RefSeq; NP_426359.1; NM_044472.2. [P60953-1]
UniGene; Hs.467637; -.
PDB; 1A4R; X-ray; 2.50 A; A/B=1-191.
PDB; 1AJE; NMR; -; A=1-187.
PDB; 1AM4; X-ray; 2.70 A; D/E/F=2-177.
PDB; 1AN0; X-ray; 2.80 A; A/B=1-190.
PDB; 1CEE; NMR; -; A=1-179.
PDB; 1CF4; NMR; -; A=1-184.
PDB; 1DOA; X-ray; 2.60 A; A=1-188.
PDB; 1E0A; NMR; -; A=1-184.
PDB; 1EES; NMR; -; A=1-178.
PDB; 1GRN; X-ray; 2.10 A; A=1-191.
PDB; 1GZS; X-ray; 2.30 A; A/C=1-178.
PDB; 1KI1; X-ray; 2.30 A; A/C=1-188.
PDB; 1KZ7; X-ray; 2.40 A; B/D=1-188.
PDB; 1KZG; X-ray; 2.60 A; B/D=1-188.
PDB; 1NF3; X-ray; 2.10 A; A/B=2-191.
PDB; 2ASE; NMR; -; A=1-178.
PDB; 2DFK; X-ray; 2.15 A; B/D=1-191.
PDB; 2KB0; NMR; -; A=1-178.
PDB; 2NGR; X-ray; 1.90 A; A=1-191.
PDB; 2ODB; X-ray; 2.40 A; A=1-181.
PDB; 2QRZ; X-ray; 2.40 A; A/B=1-189.
PDB; 2WM9; X-ray; 2.20 A; B=1-188.
PDB; 2WMN; X-ray; 2.39 A; B=1-188.
PDB; 2WMO; X-ray; 2.20 A; B=1-188.
PDB; 3GCG; X-ray; 2.30 A; A=2-178.
PDB; 3QBV; X-ray; 2.65 A; A/C=1-178.
PDB; 3VHL; X-ray; 2.08 A; B=1-188.
PDB; 4DID; X-ray; 2.35 A; A=1-183.
PDB; 4ITR; X-ray; 2.30 A; C/D=1-191.
PDB; 4JS0; X-ray; 1.90 A; A=1-178.
PDB; 4YC7; X-ray; 2.50 A; A=1-179.
PDB; 4YDH; X-ray; 3.80 A; B/D=1-179.
PDB; 5CJP; X-ray; 2.60 A; A/B/C/D=1-177.
PDB; 5FI1; X-ray; 3.20 A; B=1-191.
PDB; 5HZK; X-ray; 3.30 A; A/C=1-181.
PDBsum; 1A4R; -.
PDBsum; 1AJE; -.
PDBsum; 1AM4; -.
PDBsum; 1AN0; -.
PDBsum; 1CEE; -.
PDBsum; 1CF4; -.
PDBsum; 1DOA; -.
PDBsum; 1E0A; -.
PDBsum; 1EES; -.
PDBsum; 1GRN; -.
PDBsum; 1GZS; -.
PDBsum; 1KI1; -.
PDBsum; 1KZ7; -.
PDBsum; 1KZG; -.
PDBsum; 1NF3; -.
PDBsum; 2ASE; -.
PDBsum; 2DFK; -.
PDBsum; 2KB0; -.
PDBsum; 2NGR; -.
PDBsum; 2ODB; -.
PDBsum; 2QRZ; -.
PDBsum; 2WM9; -.
PDBsum; 2WMN; -.
PDBsum; 2WMO; -.
PDBsum; 3GCG; -.
PDBsum; 3QBV; -.
PDBsum; 3VHL; -.
PDBsum; 4DID; -.
PDBsum; 4ITR; -.
PDBsum; 4JS0; -.
PDBsum; 4YC7; -.
PDBsum; 4YDH; -.
PDBsum; 5CJP; -.
PDBsum; 5FI1; -.
PDBsum; 5HZK; -.
ProteinModelPortal; P60953; -.
SMR; P60953; -.
BioGrid; 107433; 205.
CORUM; P60953; -.
DIP; DIP-31097N; -.
ELM; P60953; -.
IntAct; P60953; 187.
MINT; MINT-94609; -.
STRING; 9606.ENSP00000314458; -.
BindingDB; P60953; -.
ChEMBL; CHEMBL6088; -.
DrugBank; DB02623; Aminophosphonic Acid-Guanylate Ester.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
iPTMnet; P60953; -.
PhosphoSitePlus; P60953; -.
SwissPalm; P60953; -.
BioMuta; CDC42; -.
DMDM; 322510015; -.
EPD; P60953; -.
PaxDb; P60953; -.
PeptideAtlas; P60953; -.
PRIDE; P60953; -.
TopDownProteomics; P60953-2; -. [P60953-2]
DNASU; 998; -.
Ensembl; ENST00000315554; ENSP00000314458; ENSG00000070831. [P60953-1]
Ensembl; ENST00000344548; ENSP00000341072; ENSG00000070831. [P60953-2]
Ensembl; ENST00000400259; ENSP00000383118; ENSG00000070831. [P60953-2]
GeneID; 998; -.
KEGG; hsa:998; -.
UCSC; uc001bfp.4; human.
CTD; 998; -.
DisGeNET; 998; -.
EuPathDB; HostDB:ENSG00000070831.15; -.
GeneCards; CDC42; -.
HGNC; HGNC:1736; CDC42.
HPA; CAB004360; -.
MalaCards; CDC42; -.
MIM; 116952; gene.
MIM; 616737; phenotype.
neXtProt; NX_P60953; -.
OpenTargets; ENSG00000070831; -.
PharmGKB; PA26266; -.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000118978; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; P60953; -.
KO; K04393; -.
OMA; MQTLKCV; -.
OrthoDB; EOG091G0KCM; -.
PhylomeDB; P60953; -.
TreeFam; TF101109; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-182971; EGFR downregulation.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-375170; CDO in myogenesis.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-HSA-418885; DCC mediated attractive signaling.
Reactome; R-HSA-428543; Inactivation of Cdc42 and Rac.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
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-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P60953; -.
SIGNOR; P60953; -.
ChiTaRS; CDC42; human.
EvolutionaryTrace; P60953; -.
GeneWiki; CDC42; -.
GenomeRNAi; 998; -.
PMAP-CutDB; P60953; -.
PRO; PR:P60953; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000070831; -.
CleanEx; HS_CDC42; -.
ExpressionAtlas; P60953; baseline and differential.
Genevisible; P60953; HS.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; ISS:BHF-UCL.
GO; GO:0017119; C:Golgi transport complex; IMP:CAFA.
GO; GO:0031256; C:leading edge membrane; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
GO; GO:0000322; C:storage vacuole; IEA:Ensembl.
GO; GO:0034191; F:apolipoprotein A-I receptor binding; IPI:BHF-UCL.
GO; GO:0032427; F:GBD domain binding; IPI:CAFA.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0030742; F:GTP-dependent protein binding; IEA:Ensembl.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0051022; F:Rho GDP-dissociation inhibitor binding; IEA:Ensembl.
GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:AgBase.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0090135; P:actin filament branching; IEA:Ensembl.
GO; GO:0051017; P:actin filament bundle assembly; IEA:Ensembl.
GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
GO; GO:0034332; P:adherens junction organization; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0003161; P:cardiac conduction system development; IEA:Ensembl.
GO; GO:0032488; P:Cdc42 protein signal transduction; IEA:Ensembl.
GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB.
GO; GO:0034613; P:cellular protein localization; IEA:Ensembl.
GO; GO:0036336; P:dendritic cell migration; IEA:Ensembl.
GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
GO; GO:0060684; P:epithelial-mesenchymal cell signaling; IEA:Ensembl.
GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:UniProtKB.
GO; GO:0051683; P:establishment of Golgi localization; ISS:BHF-UCL.
GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
GO; GO:0007030; P:Golgi organization; ISS:BHF-UCL.
GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
GO; GO:0060789; P:hair follicle placode formation; IEA:Ensembl.
GO; GO:0060047; P:heart contraction; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0031424; P:keratinization; IEA:Ensembl.
GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
GO; GO:0030225; P:macrophage differentiation; TAS:UniProtKB.
GO; GO:0099563; P:modification of synaptic structure; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0031333; P:negative regulation of protein complex assembly; IPI:UniProtKB.
GO; GO:0048664; P:neuron fate determination; IEA:Ensembl.
GO; GO:0038189; P:neuropilin signaling pathway; IMP:BHF-UCL.
GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
GO; GO:0072384; P:organelle transport along microtubule; ISS:BHF-UCL.
GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IMP:AgBase.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0071338; P:positive regulation of hair follicle cell proliferation; IEA:Ensembl.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:CAFA.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; IDA:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:BHF-UCL.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0051835; P:positive regulation of synapse structural plasticity; IEA:Ensembl.
GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
GO; GO:0010591; P:regulation of lamellipodium assembly; IGI:CAFA.
GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:Ensembl.
GO; GO:0042176; P:regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0043497; P:regulation of protein heterodimerization activity; IEA:Ensembl.
GO; GO:0045859; P:regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
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:0002040; P:sprouting angiogenesis; IEA:Ensembl.
GO; GO:0060661; P:submandibular salivary gland formation; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; IEP: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:0039694; P:viral RNA genome replication; IMP:ParkinsonsUK-UCL.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
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; Alternative splicing; Cell membrane; Complete proteome;
Cytoplasm; Cytoskeleton; Differentiation; Direct protein sequencing;
Disease mutation; Glycoprotein; GTP-binding; Lipoprotein; Membrane;
Mental retardation; Methylation; Neurogenesis; Nucleotide-binding;
Phosphoprotein; Prenylation; Reference proteome.
CHAIN 1 188 Cell division control protein 42 homolog.
/FTId=PRO_0000030425.
PROPEP 189 191 Removed in mature form.
/FTId=PRO_0000030426.
NP_BIND 10 17 GTP.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 115 118 GTP.
MOTIF 32 40 Effector region. {ECO:0000255}.
MOD_RES 32 32 O-AMP-tyrosine; by Haemophilus IbpA;
alternate. {ECO:0000269|PubMed:19362538,
ECO:0000269|PubMed:20622875}.
MOD_RES 35 35 O-AMP-threonine; by Vibrio VopS.
{ECO:0000269|PubMed:19039103}.
MOD_RES 64 64 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:14506284}.
MOD_RES 188 188 Cysteine methyl ester.
{ECO:0000244|PDB:1DOA,
ECO:0000269|PubMed:10676816}.
LIPID 188 188 S-geranylgeranyl cysteine.
{ECO:0000244|PDB:1DOA,
ECO:0000269|PubMed:10676816}.
CARBOHYD 32 32 O-linked (GlcNAc) tyrosine; by
Photorhabdus PAU_02230; alternate.
{ECO:0000269|PubMed:24141704}.
VAR_SEQ 163 163 K -> R (in isoform 1).
{ECO:0000303|PubMed:2122236,
ECO:0000303|Ref.3, ECO:0000303|Ref.4}.
/FTId=VSP_040583.
VAR_SEQ 182 191 PKKSRRCVLL -> TQPKRKCCIF (in isoform 1).
{ECO:0000303|PubMed:2122236,
ECO:0000303|Ref.3, ECO:0000303|Ref.4}.
/FTId=VSP_040584.
VARIANT 64 64 Y -> C (in TKS; dbSNP:rs864309721).
{ECO:0000269|PubMed:26386261,
ECO:0000269|PubMed:26708094}.
/FTId=VAR_076337.
MUTAGEN 12 12 G->V: Constitutively active. Interacts
with PARD6 proteins. Does not inhibit
filopodia formation. No effect on NR3C2
transcriptional activity.
{ECO:0000269|PubMed:10954424,
ECO:0000269|PubMed:14978216,
ECO:0000269|PubMed:19029984}.
MUTAGEN 17 17 T->N: Constitutively inactive. Does not
interact with PARD6 proteins. Inhibits
filopodia formation. No effect on NR3C2
transcriptional activity.
{ECO:0000269|PubMed:11260256,
ECO:0000269|PubMed:14978216,
ECO:0000269|PubMed:19029984}.
MUTAGEN 32 32 Y->F: Abolishes AMPylation by Haemophilus
IbpA. {ECO:0000269|PubMed:19362538}.
MUTAGEN 61 61 Q->L: Constitutively active. Interacts
with PARD6 proteins.
{ECO:0000269|PubMed:11260256}.
STRAND 2 11 {ECO:0000244|PDB:2NGR}.
TURN 12 14 {ECO:0000244|PDB:1AJE}.
HELIX 16 25 {ECO:0000244|PDB:2NGR}.
HELIX 29 31 {ECO:0000244|PDB:3VHL}.
STRAND 36 46 {ECO:0000244|PDB:2NGR}.
STRAND 49 58 {ECO:0000244|PDB:2NGR}.
HELIX 62 64 {ECO:0000244|PDB:2NGR}.
TURN 65 67 {ECO:0000244|PDB:2NGR}.
HELIX 68 71 {ECO:0000244|PDB:2NGR}.
STRAND 72 74 {ECO:0000244|PDB:3QBV}.
STRAND 76 83 {ECO:0000244|PDB:2NGR}.
HELIX 87 95 {ECO:0000244|PDB:2NGR}.
HELIX 97 104 {ECO:0000244|PDB:2NGR}.
STRAND 105 107 {ECO:0000244|PDB:2WMN}.
STRAND 110 115 {ECO:0000244|PDB:2NGR}.
HELIX 117 121 {ECO:0000244|PDB:2NGR}.
HELIX 123 130 {ECO:0000244|PDB:2NGR}.
TURN 131 133 {ECO:0000244|PDB:2NGR}.
HELIX 139 148 {ECO:0000244|PDB:2NGR}.
STRAND 154 156 {ECO:0000244|PDB:2NGR}.
TURN 159 161 {ECO:0000244|PDB:2NGR}.
TURN 162 164 {ECO:0000244|PDB:2KB0}.
HELIX 165 176 {ECO:0000244|PDB:2NGR}.
STRAND 179 181 {ECO:0000244|PDB:1NF3}.
TURN 184 186 {ECO:0000244|PDB:1NF3}.
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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