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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. Causes the formation of thin, actin-rich surface projections called filopodia.
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. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
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.
Sequence similarities	Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from direct assay. Source: UniProtKB establishment or maintenance of cell polarity Ref.17 Traceable author statement. Source: UniProtKB macrophage differentiation Ref.17 Traceable author statement. Source: UniProtKB negative regulation of protein complex assembly Inferred from physical interaction. Source: UniProtKB positive regulation of pseudopodium assembly Inferred from direct assay. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from Experiment. Source: Reactome filopodium Inferred from direct assay. Source: UniProtKB plasma membrane Ref.17 Inferred from direct assay. Source: UniProtKB
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement. Source: UniProtKB thioesterase binding Ref.19 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARHGAP1	Q07960	2	EBI-81752,EBI-602762
ARHGDIA	P19803	1	EBI-81752,EBI-603777	From a different organism.
ARHGDIA	P52565	1	EBI-81752,EBI-712693
Bin1	Q9VEX9	1	EBI-81752,EBI-129424	From a different organism.
CDC42BPA	Q5VT25	3	EBI-81752,EBI-689171
Cdc42bpb	Q7TT49	1	EBI-81752,EBI-692673	From a different organism.
CDC42BPG	Q6DT37	1	EBI-81752,EBI-689124
IQGAP1	P46940	2	EBI-81752,EBI-297509
ITSN1	Q15811	2	EBI-81752,EBI-602041
MARK4	Q96L34	1	EBI-81752,EBI-302319
Mcf2l	Q64096	2	EBI-81752,EBI-602123	From a different organism.
NCF2	P19878	1	EBI-81752,EBI-489611
PAK1	Q13153	2	EBI-81752,EBI-1307
Pak1	O88643	1	EBI-81752,EBI-457240	From a different organism.
Pak1	P35465	2	EBI-81752,EBI-444379	From a different organism.
Pak3	Q61036	1	EBI-81752,EBI-457317	From a different organism.
PAK4	O96013	1	EBI-81752,EBI-713738
PARD6A	Q9NPB6	4	EBI-81752,EBI-81876
PARD6B	Q9BYG5	2	EBI-81752,EBI-295391
Pard6b	Q9JK83	4	EBI-81752,EBI-81861	From a different organism.
PARD6G	Q9BYG4	2	EBI-81752,EBI-295417
PRKCI	P41743	1	EBI-81752,EBI-286199
sopE	O52623	2	EBI-81752,EBI-602254	From a different organism.
TNK2	Q07912	1	EBI-81752,EBI-603457
TNK2	Q17R13	1	EBI-81752,EBI-457220	From a different organism.
WAS	P42768	6	EBI-81752,EBI-346375

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P60953-1)

Also known as: Brain;

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 2 (identifier: P60953-2)

Also known as: Placental;

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

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 By similarity

Nucleotide binding

57 – 61

5

GTP By similarity

Nucleotide binding

115 – 118

4

GTP By similarity

Motif

32 – 40

9

Effector region Potential

Amino acid modifications

Modified residue

32

1

O-AMP-tyrosine; by Haemophilus vopS

Modified residue

35

1

O-AMP-threonine; by Vibrio ibpA

Modified residue

135

1

N6-acetyllysine Ref.22

Modified residue

144

1

N6-acetyllysine Ref.22

Modified residue

188

1

Cysteine methyl ester

Lipidation

188

1

S-geranylgeranyl cysteine Ref.11

Natural variations

Alternative sequence

163

1

R → K in isoform 2.

VSP_007490

Alternative sequence

182 – 191

10

TQPKRKCCIF → PKKSRRCVLL in isoform 2.

VSP_007491

Experimental info

Mutagenesis

12

1

G → V: Constitutively active. Interacts with PARD6 proteins. Ref.15

Mutagenesis

17

1

T → N: Constitutively inactive. Does not interact with PARD6 proteins. Ref.17

Mutagenesis

32

1

Y → F: Abolishes AMPylation by Haemophilus vopS. Ref.20

Mutagenesis

61

1

Q → L: Constitutively active. Interacts with PARD6 proteins. Ref.17

Secondary structure

1

.

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191

Helix Strand Turn

Details...

Beta strand

2 – 11

10

Helix

16 – 25

10

Beta strand

36 – 46

11

Beta strand

49 – 57

9

Helix

62 – 64

3

Turn

65 – 67

3

Helix

68 – 71

4

Beta strand

76 – 83

8

Helix

87 – 95

9

Helix

97 – 104

8

Beta strand

110 – 115

6

Helix

117 – 121

5

Helix

123 – 131

9

Helix

139 – 149

11

Beta strand

154 – 156

3

Turn

159 – 161

3

Helix

165 – 176

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Brain) [UniParc]. Last modified April 13, 2004. Version 1. 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
	Isoform 2 (Placental) [UniParc] [UniParc]. 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

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: 2122236] [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: 2124704] [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: 16710414] [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: 15489334] [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 6-27; 108-120; 154-163 AND 167-185 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE (ISOFORM 2), 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: 8504089] [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: 2496687] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[11]	"Membrane-binding domain of the small G protein G25K contains an S-(all-trans-geranylgeranyl)cysteine methyl ester at its carboxyl terminus." Yamane H.K., Farnsworth C.C., Xie H.Y., Evans T., Howald W.N., Gelb M.H., Glomset J.A., Clarke S., Fung B.K.-K. Proc. Natl. Acad. Sci. U.S.A. 88:286-290(1991) [PubMed: 1898776] [Abstract] Cited for: ISOPRENYLATION AT CYS-188. Tissue: Brain.
[12]	"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: 10490598] [Abstract] Cited for: INTERACTION WITH CDC42EP1; CDC42EP2; CDC42EP3 AND CDC42EP5. Tissue: Embryo.
[13]	"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: 10587647] [Abstract] Cited for: INTERACTION WITH CSPG4.
[14]	"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: 10816584] [Abstract] Cited for: INTERACTION WITH CDC42SE1 AND CDC42SE2.
[15]	"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: 10954424] [Abstract] Cited for: INTERACTION WITH PARD6A, MUTAGENESIS OF GLY-12.
[16]	"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: 11130076] [Abstract] Cited for: INTERACTION WITH BAIAP2.
[17]	"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: 11260256] [Abstract] Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G, SUBUNIT OF A COMPLEX CONTAINING PRKCI AND PARD6B, MUTAGENESIS OF THR-17 AND GLN-61.
[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: 12172552] [Abstract] Cited for: INTERACTION WITH DOCK9, ACTIVATION BY DOCK9.
[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: 12612085] [Abstract] Cited for: INTERACTION WITH USP6.
[20]	"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: 19362538] [Abstract] Cited for: AMPYLATION AT TYR-32, MUTAGENESIS OF TYR-32.
[21]	"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: 19039103] [Abstract] Cited for: AMPYLATION AT THR-35.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135 AND LYS-144, MASS SPECTROMETRY.
[23]	"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: 9220962] [Abstract] Cited for: STRUCTURE BY NMR.
[24]	"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: 9760238] [Abstract] Cited for: STRUCTURE BY NMR.
[25]	"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: 9262406] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH RHOGAP.
[26]	"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: 10211824] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF VAL-12 MUTANT.
[27]	"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).
+	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.
NP_001782.1.
NP_426359.1.

UniGene

Hs.467637.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A4R	X-ray	2.50	A/B	1-181	[»]
1AJE	NMR	-	A	1-181	[»]
1AM4	X-ray	2.70	D/E/F	2-177	[»]
1AN0	X-ray	2.80	A/B	2-181	[»]
1CEE	NMR	-	A	1-179	[»]
1CF4	NMR	-	A	1-181	[»]
1DOA	X-ray	2.60	A	1-181	[»]
1E0A	NMR	-	A	1-181	[»]
1EES	NMR	-	A	1-178	[»]
1GRN	X-ray	2.10	A	1-181	[»]
1GZS	X-ray	2.30	A/C	1-178	[»]
1KI1	X-ray	2.30	A/C	1-181	[»]
1KZ7	X-ray	2.40	B/D	1-181	[»]
1KZG	X-ray	2.60	B/D	1-181	[»]
1NF3	X-ray	2.10	A/B	2-181	[»]
2ASE	NMR	-	A	1-178	[»]
2DFK	X-ray	2.15	B/D	1-181	[»]
2KB0	NMR	-	A	1-178	[»]
2NGR	X-ray	1.90	A	1-181	[»]
2ODB	X-ray	2.40	A	1-181	[»]
2QRZ	X-ray	2.40	A/B	1-181	[»]
2WM9	X-ray	2.20	B	1-181	[»]
2WMN	X-ray	2.39	B	1-181	[»]
2WMO	X-ray	2.20	B	1-181	[»]
3GCG	X-ray	2.30	A	2-178	[»]

ProteinModelPortal

P60953.

SMR

P60953. Positions 1-191.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-128N.
DIP-6082N.

IntAct

P60953. 117 interactions.

MINT

MINT-94609.

STRING

P60953.

PTM databases

PhosphoSite

P60953.

Proteomic databases

PRIDE

P60953.

Genome annotation databases

Ensembl

ENST00000315554; ENSP00000314458; ENSG00000070831; Homo sapiens. [Genome view]

GeneID

998.

KEGG

hsa:998.

UCSC

uc001bfp.1. human.
uc001bfq.1. human.

Organism-specific databases

CTD

998.

GeneCards

GC01P022379.

HGNC

HGNC:1736. CDC42.

HPA

CAB004360.

MIM

116952. gene.

PharmGKB

PA142672159.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15747.

HOVERGEN

HBG009351.

OMA

EITHHCQ.

PhylomeDB

P60953.

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_11044. Signaling by Rho GTPases.
REACT_14797. Signaling by GPCR.
REACT_18266. Axon guidance.
REACT_21303. Myogenesis.
REACT_6900. Signaling in Immune system.
REACT_9417. Signaling by EGFR.

Gene expression databases

ArrayExpress

P60953.

Bgee

P60953.

CleanEx

HS_CDC42.

Genevestigator

P60953.

GermOnline

ENSG00000070831. Homo sapiens.

Family and domain databases

InterPro

IPR003578. GTPase_Rho.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP-bd.
[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 Resources

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:	April 13, 2004
Last modified:	August 10, 2010
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.