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P60766 (CDC42_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

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

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. The GTP-bound form interacts with CCPG1. Interacts with USP6 By similarity. Interacts with NEK6 By similarity. Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with ITGB1BP1 By similarity. Interacts with ARHGDIA; this interaction inactivates and stabilizes CDC42 By similarity. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Midbody By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. 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 By similarity.

Post-translational modification

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

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_processGTP catabolic process

Inferred from direct assay PubMed 10699171PubMed 15249579. Source: GOC

Golgi organization

Inferred from electronic annotation. Source: Ensembl

Rho protein signal transduction

Traceable author statement Ref.8. Source: MGI

actin filament branching

Inferred from electronic annotation. Source: Ensembl

actin filament bundle assembly

Inferred from mutant phenotype PubMed 16510873. Source: MGI

adherens junction organization

Inferred from mutant phenotype PubMed 16892058. Source: MGI

canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 16510873. Source: MGI

cardiac conduction system development

Inferred from genetic interaction PubMed 21690310. Source: MGI

cellular protein localization

Inferred from mutant phenotype PubMed 16621792. Source: MGI

dendritic cell migration

Inferred from genetic interaction PubMed 22461490. Source: MGI

endosomal transport

Traceable author statement PubMed 10954424. Source: UniProtKB

epidermis morphogenesis

Inferred from mutant phenotype PubMed 16510873. Source: MGI

epithelial cell-cell adhesion

Inferred from mutant phenotype PubMed 16510873. Source: MGI

epithelial-mesenchymal cell signaling

Inferred from mutant phenotype PubMed 16510873. Source: MGI

establishment of Golgi localization

Inferred from electronic annotation. Source: Ensembl

establishment or maintenance of apical/basal cell polarity

Inferred from mutant phenotype PubMed 16892058. Source: MGI

establishment or maintenance of cell polarity

Traceable author statement PubMed 10954424. Source: UniProtKB

filopodium assembly

Inferred from direct assay PubMed 10699171. Source: MGI

hair follicle morphogenesis

Inferred from mutant phenotype PubMed 16510873. Source: MGI

hair follicle placode formation

Inferred from mutant phenotype PubMed 16510873. Source: MGI

heart contraction

Inferred from genetic interaction PubMed 21690310. Source: MGI

keratinization

Inferred from mutant phenotype PubMed 16510873. Source: MGI

keratinocyte development

Inferred from mutant phenotype PubMed 16510873. Source: MGI

multicellular organism growth

Inferred from mutant phenotype PubMed 16510873. Source: MGI

negative regulation of gene expression

Inferred from mutant phenotype PubMed 16510873. Source: MGI

negative regulation of protein complex assembly

Inferred from electronic annotation. Source: Ensembl

neuron fate determination

Inferred from mutant phenotype PubMed 16892058. Source: MGI

nuclear migration

Inferred from mutant phenotype PubMed 15882626PubMed 16892058. Source: MGI

nucleus localization

Inferred from mutant phenotype PubMed 16892058. Source: MGI

organelle transport along microtubule

Inferred from electronic annotation. Source: Ensembl

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 MAPK cascade

Inferred from direct assay PubMed 19244314. Source: MGI

positive regulation of cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype PubMed 16510873. Source: MGI

positive regulation of hair follicle cell proliferation

Inferred from mutant phenotype PubMed 16510873. Source: MGI

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 neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 16510873. Source: MGI

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from mutant phenotype PubMed 15728722. Source: MGI

positive regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 16510873. Source: MGI

positive regulation of pseudopodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of substrate adhesion-dependent cell spreading

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synapse structural plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of attachment of spindle microtubules to kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of filopodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitosis

Inferred from mutant phenotype PubMed 16892058. Source: MGI

regulation of protein catabolic process

Inferred from mutant phenotype PubMed 16510873. Source: MGI

regulation of protein heterodimerization activity

Inferred from direct assay PubMed 19244314. Source: MGI

regulation of protein kinase activity

Inferred from mutant phenotype PubMed 16510873. Source: MGI

regulation of protein metabolic process

Inferred from mutant phenotype PubMed 16510873. Source: MGI

regulation of protein stability

Inferred from mutant phenotype PubMed 16510873. Source: MGI

single organismal cell-cell adhesion

Traceable author statement PubMed 10954424. Source: UniProtKB

sprouting angiogenesis

Inferred from electronic annotation. Source: Ensembl

submandibular salivary gland formation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: Ensembl

apical part of cell

Inferred from direct assay PubMed 16892058. Source: MGI

cell periphery

Inferred from direct assay PubMed 19796622. Source: MGI

cell projection

Inferred from direct assay PubMed 15728722. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 23793062. Source: MGI

cytoplasm

Inferred from direct assay PubMed 15775979PubMed 19796622. Source: MGI

cytosol

Traceable author statement. Source: Reactome

filopodium

Inferred from electronic annotation. Source: Ensembl

leading edge membrane

Inferred from direct assay PubMed 22461490. Source: MGI

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic spindle

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

secretory granule

Inferred from electronic annotation. Source: Ensembl

spindle midzone

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from direct assay PubMed 16510873. Source: MGI

GTP-dependent protein binding

Inferred from physical interaction PubMed 10954424. Source: UniProtKB

GTPase activity

Inferred from direct assay PubMed 10699171PubMed 15249579. Source: MGI

protein binding

Inferred from physical interaction PubMed 10954424. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 21048939. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PAK1Q131533EBI-81763,EBI-1307From a different organism.
Vamp2P630442EBI-81763,EBI-521920

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P60766-2)

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: P60766-1)

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_0000030427
Propeptide189 – 1913Removed in mature form By similarity
PRO_0000030428

Regions

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

Amino acid modifications

Modified residue641Phosphotyrosine; by SRC By similarity
Modified residue1881Cysteine methyl ester By similarity
Lipidation1881S-geranylgeranyl cysteine By similarity

Natural variations

Alternative sequence1631K → R in isoform 1.
VSP_040585
Alternative sequence182 – 19110PKKSRRCVLL → TQPKRKCCIF in isoform 1.
VSP_040586

Experimental info

Mutagenesis171T → N: Constitutively inactivated. Abolishes interaction with PARD6 and DOCK11. Ref.9 Ref.13
Mutagenesis611Q → L: Constitutively activated. Enhances interaction with DOCK11. Ref.13
Sequence conflict261N → D in BAC34669. Ref.4
Sequence conflict661R → G in AAH64792. Ref.6
Sequence conflict851V → I in BAE39489. Ref.4
Sequence conflict1161Q → K in BAE40049. Ref.4
Sequence conflict1711E → G in AAH64792. Ref.6

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]"Oncogene ect2 is related to regulators of small GTP-binding proteins."
Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.
Nature 362:462-465(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Complete cDNAs for CDC42 from chicken cochlea and mouse liver."
Gong T.W., Shin J.J., Burmeister M., Lomax M.I.
Biochim. Biophys. Acta 1352:282-292(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Liver.
[3]"Genomic organization and chromosomal location of murine Cdc42."
Marks P.W., Kwiatkowski D.J.
Genomics 38:13-18(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: BALB/c, C57BL/6J, DBA/2 and NOD.
Tissue: Amnion, Bone marrow, Heart, Kidney, Liver, Mammary gland, Placenta, Spinal ganglion and Thymus.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]"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).
Strain: C57BL/6J.
Tissue: Embryonic germ cell.
[7]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 108-120, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[8]"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 CDC42EP4.
[9]"The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
Joberty G., Petersen C., Gao L., Macara I.G.
Nat. Cell Biol. 2:531-539(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT OF A COMPLEX CONTAINING PARD6B; PARD3 AND PRKCZ, MUTAGENESIS OF THR-17.
[10]"Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7."
Alberts A.S., Bouquin N., Johnston L.H., Treisman R.
J. Biol. Chem. 273:8616-8622(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NET1.
[11]"TCGAP, a multidomain Rho GTPase-activating protein involved in insulin-stimulated glucose transport."
Chiang S.-H., Hwang J., Legendre M., Zhang M., Kimura A., Saltiel A.R.
EMBO J. 22:2679-2691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP33/TCGAP.
[12]"Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange factor expressed predominantly in lymphocytes."
Nishikimi A., Meller N., Uekawa N., Isobe K., Schwartz M.A., Maruyama M.
FEBS Lett. 579:1039-1046(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOCK11.
[13]"Identification of a DOCK180-related guanine nucleotide exchange factor that is capable of mediating a positive feedback activation of Cdc42."
Lin Q., Yang W., Baird D., Feng Q., Cerione R.A.
J. Biol. Chem. 281:35253-35262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOCK11 AND IQGAP1, MUTAGENESIS OF THR-17 AND GLN-61.
[14]"Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCPG1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11318 mRNA. Translation: AAA37410.1.
U37720 mRNA. Translation: AAC00028.1.
L78075 Genomic DNA. Translation: AAB40051.1.
AK003098 mRNA. Translation: BAB22563.1.
AK051543 mRNA. Translation: BAC34669.1.
AK075567 mRNA. Translation: BAC35825.1.
AK144216 mRNA. Translation: BAE25778.1.
AK151087 mRNA. Translation: BAE30100.1.
AK151726 mRNA. Translation: BAE30644.1.
AK153564 mRNA. Translation: BAE32098.1.
AK154870 mRNA. Translation: BAE32891.1.
AK159470 mRNA. Translation: BAE35111.1.
AK166281 mRNA. Translation: BAE38678.1.
AK167195 mRNA. Translation: BAE39325.1.
AK167400 mRNA. Translation: BAE39489.1.
AK167609 mRNA. Translation: BAE39663.1.
AK168013 mRNA. Translation: BAE40000.1.
AK168076 mRNA. Translation: BAE40049.1.
AK168089 mRNA. Translation: BAE40062.1.
AK168276 mRNA. Translation: BAE40222.1.
AK168758 mRNA. Translation: BAE40595.1.
AK168820 mRNA. Translation: BAE40647.1.
AK169122 mRNA. Translation: BAE40902.1.
AK169232 mRNA. Translation: BAE41001.1.
AK169805 mRNA. Translation: BAE41379.1.
AL645468 Genomic DNA. Translation: CAM18513.1.
AL645468 Genomic DNA. Translation: CAM18514.1.
BC064792 mRNA. Translation: AAH64792.1.
CCDSCCDS18816.1.
CCDS57305.1. [P60766-1]
RefSeqNP_001230698.1. NM_001243769.1. [P60766-1]
NP_033991.1. NM_009861.3. [P60766-2]
UniGeneMm.1022.
Mm.447553.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EG5X-ray2.70A/C1-178[»]
ProteinModelPortalP60766.
SMRP60766. Positions 1-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198627. 16 interactions.
DIPDIP-32554N.
IntActP60766. 15 interactions.
MINTMINT-1602743.

Chemistry

BindingDBP60766.

PTM databases

PhosphoSiteP60766.

Proteomic databases

MaxQBP60766.
PaxDbP60766.
PRIDEP60766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030417; ENSMUSP00000030417; ENSMUSG00000006699. [P60766-1]
ENSMUST00000051477; ENSMUSP00000054634; ENSMUSG00000006699. [P60766-2]
GeneID12540.
KEGGmmu:12540.
UCSCuc008viw.3. mouse.
uc008viy.2. mouse. [P60766-1]

Organism-specific databases

CTD998.
MGIMGI:106211. Cdc42.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00720000108634.
HOVERGENHBG009351.
KOK04393.
OMAVITIDQG.
OrthoDBEOG764747.
PhylomeDBP60766.
TreeFamTF101109.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressP60766.
BgeeP60766.
CleanExMM_CDC42.
GenevestigatorP60766.

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. mouse.
EvolutionaryTraceP60766.
NextBio281582.
PROP60766.
SOURCESearch...

Entry information

Entry nameCDC42_MOUSE
AccessionPrimary (citable) accession number: P60766
Secondary accession number(s): A2A9U6 expand/collapse secondary AC list , P21181, P25763, Q3THZ7, Q3TJK6, Q545V0, Q6P201, Q8BQ51
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 8, 2011
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot