P60953 (CDC42_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell division control protein 42 homolog

Alternative name(s):
G25K GTP-binding protein

Gene names

Name:

CDC42

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.20 Ref.21 Ref.22
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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.22 Ref.25 Ref.27
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle. 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.21 Ref.25
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.18
Sequence similarities	Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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: Compara actin filament bundle assembly Inferred from electronic annotation. Source: Compara adherens junction organization Inferred from electronic annotation. Source: Compara axon guidance Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara cardiac conduction system development Inferred from electronic annotation. Source: Compara cellular protein localization Inferred from electronic annotation. Source: Compara epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome epithelial cell-cell adhesion Inferred from electronic annotation. Source: Compara epithelial-mesenchymal cell signaling Inferred from electronic annotation. Source: Compara 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: Compara establishment or maintenance of cell polarity Traceable author statement Ref.16. Source: UniProtKB filopodium assembly Inferred from electronic annotation. Source: Compara hair follicle morphogenesis Inferred from electronic annotation. Source: Compara hair follicle placode formation Inferred from electronic annotation. Source: Compara heart contraction Inferred from electronic annotation. Source: Compara keratinization Inferred from electronic annotation. Source: Compara keratinocyte development Inferred from electronic annotation. Source: Compara macrophage differentiation Traceable author statement Ref.16. Source: UniProtKB multicellular organism growth Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of protein complex assembly Inferred from physical interaction PubMed 11584266. Source: UniProtKB neuron fate determination Inferred from electronic annotation. Source: Compara nuclear migration Inferred from electronic annotation. Source: Compara organelle transport along microtubule Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of DNA replication Inferred from electronic annotation. Source: Compara positive regulation of JNK cascade Inferred from electronic annotation. Source: Compara positive regulation of cell cycle cytokinesis Inferred from mutant phenotype Ref.21. Source: UniProtKB positive regulation of gene expression Inferred from electronic annotation. Source: Compara positive regulation of hair follicle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of intracellular protein transport Inferred from electronic annotation. Source: Compara positive regulation of metalloenzyme activity Inferred from electronic annotation. Source: Compara positive regulation of muscle cell differentiation Traceable author statement. Source: Reactome positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase activity Inferred from electronic annotation. Source: Compara positive regulation of pseudopodium assembly Inferred from direct assay PubMed 11035016. Source: UniProtKB positive regulation of synapse structural plasticity Inferred from electronic annotation. Source: Compara regulation of attachment of spindle microtubules to kinetochore Inferred from mutant phenotype Ref.21. Source: UniProtKB regulation of filopodium assembly Inferred from direct assay Ref.20. Source: UniProtKB regulation of mitosis Inferred from electronic annotation. Source: Compara regulation of protein catabolic process Inferred from electronic annotation. Source: Compara regulation of protein heterodimerization activity Inferred from electronic annotation. Source: Compara regulation of protein kinase activity Inferred from electronic annotation. Source: Compara regulation of protein stability Inferred from electronic annotation. Source: Compara 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: Compara submandibular salivary gland formation Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Inferred from sequence or structural similarity. Source: BHF-UCL apical part of cell Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome filopodium Inferred from direct assay PubMed 11035016. Source: UniProtKB microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from direct assay Ref.21. Source: UniProtKB mitotic spindle Inferred from direct assay Ref.21. 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: Compara spindle midzone Inferred from direct assay Ref.21. Source: UniProtKB
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement PubMed 11035016. Source: UniProtKB protein kinase binding Inferred from direct assay Ref.24. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-81752,EBI-81752
ARHGAP1	Q07960	2	EBI-81752,EBI-602762
BAIAP2	Q9UQB8	2	EBI-287394,EBI-525456
Bin1	Q9VEX9	2	EBI-81752,EBI-129424	From a different organism.
CDC42BPA	Q5VT25	5	EBI-81752,EBI-689171
CDC42EP1	Q00587	3	EBI-81752,EBI-744130
IQGAP1	P46940	2	EBI-81752,EBI-297509
ITSN1	Q15811	2	EBI-3625591,EBI-602041
LRRK2	Q5S007	3	EBI-81752,EBI-5323863
MAP3K11	Q16584	2	EBI-81752,EBI-49961
MARK4	Q96L34	2	EBI-81752,EBI-302319
Mcf2l	Q64096	3	EBI-287394,EBI-602123	From a different organism.
PAK1	Q13153	5	EBI-81752,EBI-1307
PAK3	O75914	2	EBI-287394,EBI-3389553
PARD6A	Q9NPB6	7	EBI-81752,EBI-81876
PARD6B	Q9BYG5	7	EBI-81752,EBI-295391
Pard6b	Q9JK83	6	EBI-81752,EBI-81861	From a different organism.
PARD6G	Q9BYG4	5	EBI-81752,EBI-295417
PRKCI	P41743	5	EBI-81752,EBI-286199
sopE	O52623	2	EBI-81752,EBI-602254	From a different organism.
TNK2	Q07912	2	EBI-287394,EBI-603457
WAS	P42768	10	EBI-81752,EBI-346375
WASL	O00401	3	EBI-81752,EBI-957615
Wasl	O08816	2	EBI-81752,EBI-6142604	From a different organism.

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 188

188

Cell division control protein 42 homolog

PRO_0000030425

Propeptide

189 – 191

3

Removed in mature form

PRO_0000030426

Regions

Nucleotide binding

10 – 17

8

GTP

Nucleotide binding

57 – 61

5

GTP By similarity

Nucleotide binding

115 – 118

4

GTP

Motif

32 – 40

9

Effector region Potential

Amino acid modifications

Modified residue

32

1

O-AMP-tyrosine; by Haemophilus IbpA

Modified residue

35

1

O-AMP-threonine; by Vibrio VopS

Modified residue

64

1

Phosphotyrosine; by SRC Ref.18

Modified residue

188

1

Cysteine methyl ester By similarity

Lipidation

188

1

S-geranylgeranyl cysteine By similarity

Natural variations

Alternative sequence

163

1

K → R in isoform 1.

VSP_040583

Alternative sequence

182 – 191

10

PKKSRRCVLL → TQPKRKCCIF in isoform 1.

VSP_040584

Experimental info

Mutagenesis

12

1

G → V: Constitutively active. Interacts with PARD6 proteins. Does not inhibit filopodia formation. Ref.14 Ref.20

Mutagenesis

17

1

T → N: Constitutively inactive. Does not interact with PARD6 proteins. Inhibits filopodia formation. Ref.16 Ref.20

Mutagenesis

32

1

Y → F: Abolishes AMPylation by Haemophilus IbpA. Ref.23

Mutagenesis

61

1

Q → L: Constitutively active. Interacts with PARD6 proteins. Ref.16

Secondary structure

1

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191

Helix Strand Turn

Details...

Beta strand

2 – 11

10

Turn

12 – 14

3

Helix

16 – 25

10

Helix

29 – 31

3

Beta strand

36 – 46

11

Beta strand

49 – 58

10

Helix

62 – 64

3

Turn

65 – 67

3

Helix

68 – 71

4

Beta strand

72 – 74

3

Beta strand

76 – 83

8

Helix

87 – 95

9

Helix

97 – 104

8

Beta strand

105 – 107

3

Beta strand

110 – 115

6

Helix

117 – 121

5

Helix

123 – 130

8

Turn

131 – 133

3

Helix

139 – 148

10

Beta strand

154 – 156

3

Turn

159 – 161

3

Turn

162 – 164

3

Helix

165 – 176

12

Beta strand

179 – 181

3

Turn

184 – 186

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (Placental) [UniParc]. Last modified February 8, 2011. Version 2. Checksum: 51A437E22A4D8FFF	FASTA	191	21,259
	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
	Isoform 1 (Brain) [UniParc] [UniParc]. Checksum: 34B44F9225EC106B	FASTA	191	21,311
	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 TQRGLKNVFD EAILAALEPP 190 ETQPKRKCCI F

References

	« Hide 'large scale' referencesShow '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. , 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), 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]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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].
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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).
[33]	"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.
[34]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

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.

IPI

IPI00007189.
IPI00016786.

PIR

A36382.
A39265.

RefSeq

NP_001034891.1. NM_001039802.1.
NP_001782.1. NM_001791.3.
NP_426359.1. NM_044472.2.

UniGene

Hs.467637.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A4R	X-ray	2.50	A/B	1-191	[»]
1AJE	NMR	-	A	1-187	[»]
1AM4	X-ray	2.70	D/E/F	2-177	[»]
1AN0	X-ray	2.80	A/B	2-190	[»]
1CEE	NMR	-	A	1-179	[»]
1CF4	NMR	-	A	1-184	[»]
1DOA	X-ray	2.60	A	1-188	[»]
1E0A	NMR	-	A	1-184	[»]
1EES	NMR	-	A	1-178	[»]
1GRN	X-ray	2.10	A	1-191	[»]
1GZS	X-ray	2.30	A/C	1-178	[»]
1KI1	X-ray	2.30	A/C	1-187	[»]
1KZ7	X-ray	2.40	B/D	1-187	[»]
1KZG	X-ray	2.60	B/D	1-187	[»]
1NF3	X-ray	2.10	A/B	2-191	[»]
2ASE	NMR	-	A	1-178	[»]
2DFK	X-ray	2.15	B/D	1-191	[»]
2KB0	NMR	-	A	1-178	[»]
2NGR	X-ray	1.90	A	1-191	[»]
2ODB	X-ray	2.40	A	1-191	[»]
2QRZ	X-ray	2.40	A/B	1-189	[»]
2WM9	X-ray	2.20	B	1-188	[»]
2WMN	X-ray	2.39	B	1-188	[»]
2WMO	X-ray	2.20	B	1-188	[»]
3GCG	X-ray	2.30	A	2-178	[»]
3QBV	X-ray	2.65	A/C	1-178	[»]
3VHL	X-ray	2.08	B	1-187	[»]
4DID	X-ray	2.35	A	1-183	[»]
4ITR	X-ray	2.30	C/D	1-191	[»]

ProteinModelPortal

P60953.

SMR

P60953. Positions 1-191.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31097N.

IntAct

P60953. 103 interactions.

MINT

MINT-94609.

STRING

9606.ENSP00000314458.

PTM databases

PhosphoSite

P60953.

Polymorphism databases

DMDM

46397381.

Proteomic databases

PaxDb

P60953.

PRIDE

P60953.

Protocols and materials databases

DNASU

998.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000315554; ENSP00000314458; ENSG00000070831.
ENST00000344548; ENSP00000341072; ENSG00000070831.
ENST00000400259; ENSP00000383118; ENSG00000070831.

GeneID

998.

KEGG

hsa:998.

UCSC

uc001bfp.3. human.
uc001bfq.3. human.

Organism-specific databases

CTD

998.

GeneCards

GC01P022379.

HGNC

HGNC:1736. CDC42.

HPA

CAB004360.

MIM

116952. gene.

neXtProt

NX_P60953.

PharmGKB

PA26266.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233974.

HOVERGEN

HBG009351.

KO

K04393.

OMA

ITMEQGE.

Enzyme and pathway databases

Pathway_Interaction_DB

endothelinpathway. Endothelins.
ephbfwdpathway. EPHB forward signaling.
lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
wnt_calcium_pathway. Noncanonical Wnt signaling pathway.
avb3_opn_pathway. Osteopontin-mediated events.
s1p_s1p4_pathway. S1P4 pathway.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
tcrpathway. TCR signaling in naive CD4+ T cells.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
REACT_96538. Developmental Biology.

Gene expression databases

ArrayExpress

P60953.

Bgee

P60953.

CleanEx

HS_CDC42.

Genevestigator

P60953.

GermOnline

ENSG00000070831. Homo sapiens.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00174. RHO. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51420. RHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P60953.

ChEMBL

CHEMBL6088.

ChiTaRS

CDC42. human.

EvolutionaryTrace

P60953.

GenomeRNAi

998.

NextBio

4192.

PMAP-CutDB

P60953.

SOURCE

Search...

Entry information

Entry name

CDC42_HUMAN

Accession

Primary (citable) accession number: P60953
Secondary accession number(s): P21181 , P25763, Q7L8R5, Q9UDI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	February 8, 2011
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.