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P60953 (CDC42_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division control protein 42 homolog
Alternative name(s):
G25K GTP-binding protein
Gene names
Name:CDC42
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.21 Ref.22 Ref.23

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.

Subunit structure

The GTP-bound form interacts with CCPG1 By similarity. Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4, CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-dependent manner). Interacts with activated CSPG4 and with BAIAP2. Interacts with Zizimin1/DOCK9 and Zizimin2/DOCK11, which activate it by exchanging GDP for GTP. Interacts with NET1 and ARHGAP33/TCGAP. Part of a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ. Interacts with USP6. May interact with ARHGEF16; responsible for the activation of CDC42 by the viral protein HPV16 E6. Interacts with NEK6. Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with ITGB1BP1. Interacts with ARHGDIA; this interaction inactivates and stabilizes CDC42. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.27 Ref.29 Ref.30

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Midbody. Note: Localizes to spindle during prometaphase cells. Moves to the central spindle as cells progressed through anaphase to telophase. Localizes at the end of cytokinesis in the intercellular bridge formed between two daughter cells. Its localization is regulated by the activities of guanine nucleotide exchange factor ECT2 and GTPase activating protein RACGAP1. Colocalizes with NEK6 in the centrosome. Ref.22 Ref.27

Post-translational modification

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.

Phosphorylated by SRC in an EGF-dependent manner, this stimulates the binding of the Rho-GDP dissociation inhibitor RhoGDI. Ref.19

Sequence similarities

Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMLipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

GTP catabolic process

Traceable author statement PubMed 11035016. Source: GOC

Golgi organization

Inferred from sequence or structural similarity. Source: BHF-UCL

T cell costimulation

Traceable author statement. Source: Reactome

actin cytoskeleton organization

Inferred from direct assay PubMed 11035016. Source: UniProtKB

actin filament branching

Inferred from electronic annotation. Source: Ensembl

actin filament bundle assembly

Inferred from electronic annotation. Source: Ensembl

adherens junction organization

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

cardiac conduction system development

Inferred from electronic annotation. Source: Ensembl

cellular protein localization

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

epithelial cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

epithelial-mesenchymal cell signaling

Inferred from electronic annotation. Source: Ensembl

establishment of Golgi localization

Inferred from sequence or structural similarity. Source: BHF-UCL

establishment or maintenance of apical/basal cell polarity

Inferred from electronic annotation. Source: Ensembl

establishment or maintenance of cell polarity

Traceable author statement Ref.16. Source: UniProtKB

filopodium assembly

Inferred from electronic annotation. Source: Ensembl

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

hair follicle placode formation

Inferred from electronic annotation. Source: Ensembl

heart contraction

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

keratinization

Inferred from electronic annotation. Source: Ensembl

keratinocyte development

Inferred from electronic annotation. Source: Ensembl

macrophage differentiation

Traceable author statement Ref.16. Source: UniProtKB

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

muscle cell differentiation

Traceable author statement. Source: Reactome

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein complex assembly

Inferred from physical interaction PubMed 11584266. Source: UniProtKB

neuron fate determination

Inferred from electronic annotation. Source: Ensembl

nuclear migration

Inferred from electronic annotation. Source: Ensembl

organelle transport along microtubule

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokinesis

Inferred from mutant phenotype Ref.22. Source: UniProtKB

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of hair follicle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of intracellular protein transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of metalloenzyme activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of muscle cell differentiation

Traceable author statement. Source: Reactome

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of pseudopodium assembly

Inferred from direct assay PubMed 11035016. Source: UniProtKB

positive regulation of substrate adhesion-dependent cell spreading

Inferred from direct assay Ref.17. Source: UniProtKB

positive regulation of synapse structural plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of attachment of spindle microtubules to kinetochore

Inferred from mutant phenotype Ref.22. Source: UniProtKB

regulation of filopodium assembly

Inferred from direct assay Ref.21. Source: UniProtKB

regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of protein heterodimerization activity

Inferred from electronic annotation. Source: Ensembl

regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

regulation of protein stability

Inferred from electronic annotation. Source: Ensembl

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

sprouting angiogenesis

Inferred from electronic annotation. Source: Ensembl

submandibular salivary gland formation

Inferred from electronic annotation. Source: Ensembl

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentGolgi membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

apical part of cell

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337. Source: UniProt

filopodium

Inferred from direct assay PubMed 11035016. Source: UniProtKB

membrane

Inferred from direct assay Ref.17. Source: UniProtKB

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay Ref.22. Source: UniProtKB

mitotic spindle

Inferred from direct assay Ref.22. Source: UniProtKB

neuron projection

Inferred from direct assay PubMed 21048939. Source: BHF-UCL

neuronal cell body

Inferred from direct assay PubMed 21048939. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.16. Source: UniProtKB

secretory granule

Inferred from electronic annotation. Source: Ensembl

spindle midzone

Inferred from direct assay Ref.22. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Traceable author statement PubMed 11035016. Source: UniProtKB

apolipoprotein A-I receptor binding

Inferred from physical interaction PubMed 16443932. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 9748241. Source: IntAct

protein kinase binding

Inferred from direct assay Ref.26. Source: BHF-UCL

thioesterase binding

Inferred from physical interaction Ref.20. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P60953-2)

Also known as: Placental;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P60953-1)

Also known as: Brain;

The sequence of this isoform differs from the canonical sequence as follows:
     163-163: K → R
     182-191: PKKSRRCVLL → TQPKRKCCIF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Cell division control protein 42 homolog
PRO_0000030425
Propeptide189 – 1913Removed in mature form
PRO_0000030426

Regions

Nucleotide binding10 – 178GTP
Nucleotide binding57 – 615GTP By similarity
Nucleotide binding115 – 1184GTP
Motif32 – 409Effector region Potential

Amino acid modifications

Modified residue321O-AMP-tyrosine; by Haemophilus IbpA
Modified residue351O-AMP-threonine; by Vibrio VopS
Modified residue641Phosphotyrosine; by SRC Ref.19
Modified residue1881Cysteine methyl ester By similarity
Lipidation1881S-geranylgeranyl cysteine By similarity

Natural variations

Alternative sequence1631K → R in isoform 1.
VSP_040583
Alternative sequence182 – 19110PKKSRRCVLL → TQPKRKCCIF in isoform 1.
VSP_040584

Experimental info

Mutagenesis121G → V: Constitutively active. Interacts with PARD6 proteins. Does not inhibit filopodia formation. No effect on NR3C2 transcriptional activity. Ref.14 Ref.21 Ref.24
Mutagenesis171T → N: Constitutively inactive. Does not interact with PARD6 proteins. Inhibits filopodia formation. No effect on NR3C2 transcriptional activity. Ref.16 Ref.21 Ref.24
Mutagenesis321Y → F: Abolishes AMPylation by Haemophilus IbpA. Ref.25
Mutagenesis611Q → L: Constitutively active. Interacts with PARD6 proteins. Ref.16

Secondary structure

........................................... 191
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (Placental) [UniParc].

Last modified February 8, 2011. Version 2.
Checksum: 51A437E22A4D8FFF

FASTA19121,259
        10         20         30         40         50         60 
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG 

        70         80         90        100        110        120 
QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR 

       130        140        150        160        170        180 
DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP 

       190 
EPKKSRRCVL L 

« Hide

Isoform 1 (Brain) [UniParc] [UniParc].

Checksum: 34B44F9225EC106B
Show »

FASTA19121,311

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42."
Munemitsu S., Innis M.A., Clark R., McCormick F., Ullrich A., Polakis P.
Mol. Cell. Biol. 10:5977-5982(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[2]"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."
Shinjo K., Koland J.G., Hart M.J., Narasimhan V., Johnson D.I., Evans T., Cerione R.A.
Proc. Natl. Acad. Sci. U.S.A. 87:9853-9857(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[3]Rhodes S., Huckle E.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[4]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Placenta.
[5]NIEHS SNPs program
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Cervix, Placenta and Uterus.
[8]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 67-83 (ISOFORM 2), PARTIAL PROTEIN SEQUENCE (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]"Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins."
Kwong C.H., Malech H.L., Rotrosen D., Leto T.L.
Biochemistry 32:5711-5717(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 97-107; 134-144 AND 167-183 (ISOFORM 2).
Tissue: Neutrophil.
[10]"Characterization of G25K, a GTP-binding protein containing a novel putative nucleotide binding domain."
Polakis P.G., Snyderman R., Evans T.
Biochem. Biophys. Res. Commun. 160:25-32(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[11]"The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins."
Joberty G., Perlungher R.R., Macara I.G.
Mol. Cell. Biol. 19:6585-6597(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC42EP1; CDC42EP2; CDC42EP3 AND CDC42EP5.
Tissue: Embryo.
[12]"Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas."
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.
Nat. Cell Biol. 1:507-513(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSPG4.
[13]"SPECs, small binding proteins for Cdc42."
Pirone D.M., Fukuhara S., Gutkind J.S., Burbelo P.D.
J. Biol. Chem. 275:22650-22656(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC42SE1 AND CDC42SE2.
[14]"The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1."
Johansson A.-S., Driessens M., Aspenstroem P.
J. Cell Sci. 113:3267-3275(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARD6A, MUTAGENESIS OF GLY-12.
[15]"IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling."
Miki H., Yamaguchi H., Suetsugu S., Takenawa T.
Nature 408:732-735(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP2.
[16]"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."
Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.
Genes Cells 6:107-119(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G, SUBUNIT OF A COMPLEX CONTAINING PRKCI AND PARD6B, MUTAGENESIS OF THR-17 AND GLN-61.
[17]"The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading."
Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L., Eva A., Tarone G.
J. Cell Biol. 156:377-387(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB1BP1.
[18]"Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins."
Meller N., Irani-Tehrani M., Kiosses W.B., Del Pozo M.A., Schwartz M.A.
Nat. Cell Biol. 4:639-647(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOCK9, ACTIVATION BY DOCK9.
[19]"Epidermal growth factor-dependent regulation of Cdc42 is mediated by the Src tyrosine kinase."
Tu S., Wu W.J., Wang J., Cerione R.A.
J. Biol. Chem. 278:49293-49300(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-64 BY SRC.
[20]"The TRE17 oncogene encodes a component of a novel effector pathway for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling."
Masuda-Robens J.M., Kutney S.N., Qi H., Chou M.M.
Mol. Cell. Biol. 23:2151-2161(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP6.
[21]"Regulation of dendritic branching and filopodia formation in hippocampal neurons by specific acylated protein motifs."
Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.
Mol. Biol. Cell 15:2205-2217(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-12 AND THR-17.
[22]"Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis."
Oceguera-Yanez F., Kimura K., Yasuda S., Higashida C., Kitamura T., Hiraoka Y., Haraguchi T., Narumiya S.
J. Cell Biol. 168:221-232(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[23]"Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas."
Modzelewska K., Newman L.P., Desai R., Keely P.J.
J. Biol. Chem. 281:37527-37535(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH BCAR1; TNK2 AND CRK.
[24]"Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease."
Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H., Miyoshi J., Takai Y., Fujita T.
Nat. Med. 14:1370-1376(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-12 AND THR-17.
[25]"The fic domain: regulation of cell signaling by adenylylation."
Worby C.A., Mattoo S., Kruger R.P., Corbeil L.B., Koller A., Mendez J.C., Zekarias B., Lazar C., Dixon J.E.
Mol. Cell 34:93-103(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: AMPYLATION AT TYR-32, MUTAGENESIS OF TYR-32.
[26]"AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling."
Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.
Science 323:269-272(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: AMPYLATION AT THR-35.
[27]"Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which activates Cdc42."
Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L., Hampson I.N.
Br. J. Cancer 104:324-331(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF16.
[30]"ARHGDIA: a novel gene implicated in nephrotic syndrome."
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.
J. Med. Genet. 50:330-338(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGDIA.
[31]"Definition of the switch surface in the solution structure of Cdc42Hs."
Feltham J.L., Dotsch V., Raza S., Manor D., Cerione R.A., Sutcliffe M.J., Wagner G., Oswald R.E.
Biochemistry 36:8755-8766(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[32]"Identification of the binding surface on Cdc42Hs for p21-activated kinase."
Guo W., Sutcliffe M.J., Cerione R.A., Oswald R.E.
Biochemistry 37:14030-14037(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[33]"Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP."
Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D., Laue E., Gamblin S.J., Smerdon S.J.
Nature 388:693-697(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH RHOGAP.
[34]"Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: two different nucleotide states in one crystal."
Rudolph M.G., Wittinghofer A., Vetter I.R.
Protein Sci. 8:778-787(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF VAL-12 MUTANT.
[35]"The structure determination of CDC42Hs and GDP complex."
Kongsaeree P., Cerione R.A., Clardy J.C.
Submitted (JUN-1997) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[36]"Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor."
Yang J., Zhang Z., Roe S.M., Marshall C.J., Barford D.
Science 325:1398-1402(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-188 IN COMPLEX WITH DOCK9.
[37]"Structural basis of Fic-mediated adenylylation."
Xiao J., Worby C.A., Mattoo S., Sankaran B., Dixon J.E.
Nat. Struct. Mol. Biol. 17:1004-1010(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-181 IN COMPLEX WITH H.SOMNUS IBPA AND GDP, AMPYLATION AT TYR-32.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35543 mRNA. Translation: AAA52494.1.
M57298 mRNA. Translation: AAA52592.1.
AL121734 mRNA. Translation: CAB57325.1.
AL121735 mRNA. Translation: CAB57326.1.
AF498962 mRNA. Translation: AAM21109.1.
AF498963 mRNA. Translation: AAM21110.1.
AY673602 Genomic DNA. Translation: AAT70721.1.
AL031281 Genomic DNA. Translation: CAB52602.1.
AL031281 Genomic DNA. Translation: CAD92551.1.
BC002711 mRNA. Translation: AAH02711.1.
BC003682 mRNA. Translation: AAH03682.1.
BC018266 mRNA. Translation: AAH18266.1.
PIRA36382.
A39265.
RefSeqNP_001034891.1. NM_001039802.1.
NP_001782.1. NM_001791.3.
NP_426359.1. NM_044472.2.
UniGeneHs.467637.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4RX-ray2.50A/B1-191[»]
1AJENMR-A1-187[»]
1AM4X-ray2.70D/E/F2-177[»]
1AN0X-ray2.80A/B2-190[»]
1CEENMR-A1-179[»]
1CF4NMR-A1-184[»]
1DOAX-ray2.60A1-188[»]
1E0ANMR-A1-184[»]
1EESNMR-A1-178[»]
1GRNX-ray2.10A1-191[»]
1GZSX-ray2.30A/C1-178[»]
1KI1X-ray2.30A/C1-187[»]
1KZ7X-ray2.40B/D1-187[»]
1KZGX-ray2.60B/D1-187[»]
1NF3X-ray2.10A/B2-191[»]
2ASENMR-A1-178[»]
2DFKX-ray2.15B/D1-191[»]
2KB0NMR-A1-178[»]
2NGRX-ray1.90A1-191[»]
2ODBX-ray2.40A1-191[»]
2QRZX-ray2.40A/B1-189[»]
2WM9X-ray2.20B1-188[»]
2WMNX-ray2.39B1-188[»]
2WMOX-ray2.20B1-188[»]
3GCGX-ray2.30A2-178[»]
3QBVX-ray2.65A/C1-178[»]
3VHLX-ray2.08B1-187[»]
4DIDX-ray2.35A1-183[»]
4ITRX-ray2.30C/D1-191[»]
4JS0X-ray1.90A1-178[»]
ProteinModelPortalP60953.
SMRP60953. Positions 1-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107433. 139 interactions.
DIPDIP-31097N.
IntActP60953. 114 interactions.
MINTMINT-94609.
STRING9606.ENSP00000314458.

Chemistry

BindingDBP60953.
ChEMBLCHEMBL6088.

PTM databases

PhosphoSiteP60953.

Polymorphism databases

DMDM322510015.

Proteomic databases

PaxDbP60953.
PRIDEP60953.

Protocols and materials databases

DNASU998.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315554; ENSP00000314458; ENSG00000070831. [P60953-1]
ENST00000344548; ENSP00000341072; ENSG00000070831. [P60953-2]
ENST00000400259; ENSP00000383118; ENSG00000070831. [P60953-2]
GeneID998.
KEGGhsa:998.
UCSCuc001bfp.3. human. [P60953-1]
uc001bfq.3. human.

Organism-specific databases

CTD998.
GeneCardsGC01P022379.
HGNCHGNC:1736. CDC42.
HPACAB004360.
MIM116952. gene.
neXtProtNX_P60953.
PharmGKBPA26266.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233974.
HOVERGENHBG009351.
KOK04393.
OMAITMEQGE.
PhylomeDBP60953.
TreeFamTF101109.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_195021. Developmental Biology.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP60953.

Gene expression databases

ArrayExpressP60953.
BgeeP60953.
CleanExHS_CDC42.
GenevestigatorP60953.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDC42. human.
EvolutionaryTraceP60953.
GeneWikiCDC42.
GenomeRNAi998.
NextBio4192.
PMAP-CutDBP60953.
PROP60953.
SOURCESearch...

Entry information

Entry nameCDC42_HUMAN
AccessionPrimary (citable) accession number: P60953
Secondary accession number(s): P21181 expand/collapse secondary AC list , P25763, Q7L8R5, Q9UDI2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 8, 2011
Last modified: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM