Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Cell division control protein 42 homolog



Mus musculus (Mouse)
Reviewed-Annotation score: -Experimental evidence at protein leveli


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 (By similarity). Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons (PubMed:25851601). Facilitates filopodia formation upon DOCK11-activation (PubMed:22494997). Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups (By similarity).By similarity2 Publications

Enzyme regulationi

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.2 Publications


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 17GTPBy similarity8
Nucleotide bindingi57 – 61GTPBy similarity5
Nucleotide bindingi115 – 118GTPBy similarity4

GO - Molecular functioni

  • GTPase activity Source: MGI
  • GTP binding Source: MGI
  • GTP-dependent protein binding Source: UniProtKB
  • mitogen-activated protein kinase kinase kinase binding Source: MGI
  • protein kinase binding Source: BHF-UCL
  • Rho GDP-dissociation inhibitor binding Source: MGI

GO - Biological processi

  • actin filament branching Source: MGI
  • actin filament bundle assembly Source: MGI
  • actin filament organization Source: UniProtKB
  • adherens junction organization Source: MGI
  • canonical Wnt signaling pathway Source: MGI
  • cardiac conduction system development Source: MGI
  • Cdc42 protein signal transduction Source: MGI
  • cell-cell adhesion Source: MGI
  • cell junction assembly Source: UniProtKB
  • cellular protein localization Source: MGI
  • cellular response to interferon-gamma Source: MGI
  • dendritic cell migration Source: MGI
  • dendritic spine morphogenesis Source: UniProtKB
  • endocytosis Source: MGI
  • endosomal transport Source: UniProtKB
  • epidermis morphogenesis Source: MGI
  • epithelial cell-cell adhesion Source: MGI
  • epithelial-mesenchymal cell signaling Source: MGI
  • establishment of epithelial cell apical/basal polarity Source: UniProtKB
  • establishment of Golgi localization Source: MGI
  • establishment or maintenance of apical/basal cell polarity Source: MGI
  • establishment or maintenance of cell polarity Source: UniProtKB
  • filopodium assembly Source: MGI
  • Golgi organization Source: MGI
  • hair follicle morphogenesis Source: MGI
  • hair follicle placode formation Source: MGI
  • heart contraction Source: MGI
  • keratinization Source: MGI
  • keratinocyte development Source: MGI
  • modification of synaptic structure Source: MGI
  • multicellular organism growth Source: MGI
  • negative regulation of gene expression Source: MGI
  • neuron fate determination Source: MGI
  • nuclear migration Source: MGI
  • nucleus localization Source: MGI
  • organelle transport along microtubule Source: MGI
  • phagocytosis, engulfment Source: UniProtKB
  • positive regulation of catalytic activity Source: MGI
  • positive regulation of cytokinesis Source: UniProtKB
  • positive regulation of DNA replication Source: MGI
  • positive regulation of epithelial cell proliferation involved in lung morphogenesis Source: CACAO
  • positive regulation of filopodium assembly Source: UniProtKB
  • positive regulation of gene expression Source: MGI
  • positive regulation of hair follicle cell proliferation Source: MGI
  • positive regulation of intracellular protein transport Source: MGI
  • positive regulation of JNK cascade Source: MGI
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of neuron apoptotic process Source: MGI
  • positive regulation of peptidyl-serine phosphorylation Source: MGI
  • positive regulation of phosphatidylinositol 3-kinase activity Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • positive regulation of synapse structural plasticity Source: MGI
  • regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  • regulation of filopodium assembly Source: UniProtKB
  • regulation of mitotic nuclear division Source: MGI
  • regulation of protein catabolic process Source: MGI
  • regulation of protein heterodimerization activity Source: MGI
  • regulation of protein kinase activity Source: MGI
  • regulation of protein metabolic process Source: MGI
  • regulation of protein stability Source: MGI
  • Rho protein signal transduction Source: MGI
  • sprouting angiogenesis Source: MGI
  • submandibular salivary gland formation Source: Ensembl


Biological processDifferentiation, Neurogenesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-114604 GPVI-mediated activation cascade
R-MMU-182971 EGFR downregulation
R-MMU-194840 Rho GTPase cycle
R-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-375170 CDO in myogenesis
R-MMU-389359 CD28 dependent Vav1 pathway
R-MMU-3928662 EPHB-mediated forward signaling
R-MMU-416482 G alpha (12/13) signalling events
R-MMU-418885 DCC mediated attractive signaling
R-MMU-4420097 VEGFA-VEGFR2 Pathway
R-MMU-5625970 RHO GTPases activate KTN1
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5627123 RHO GTPases activate PAKs
R-MMU-5663213 RHO GTPases Activate WASPs and WAVEs
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-5687128 MAPK6/MAPK4 signaling
R-MMU-68877 Mitotic Prometaphase
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division control protein 42 homolog
Alternative name(s):
G25K GTP-binding protein
Gene namesi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:106211 Cdc42

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12G → V: No effect on filopodia formation. 1 Publication1
Mutagenesisi17T → N: Constitutively inactivated. Abolishes interaction with PARD6 and DOCK11. Inhibits filopodia formation. 3 Publications1
Mutagenesisi61Q → L: Constitutively activated. Enhances interaction with DOCK11. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000304271 – 188Cell division control protein 42 homologAdd BLAST188
PropeptideiPRO_0000030428189 – 191Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei64Phosphotyrosine; by SRCBy similarity1
Modified residuei188Cysteine methyl esterBy similarity1
Lipidationi188S-geranylgeranyl cysteineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases


PTM databases



Gene expression databases

GenevisibleiP60766 MM


Subunit structurei

Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4, CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-dependent manner) (PubMed:10490598, PubMed:10934474). Interacts with activated CSPG4 and with BAIAP2 (By similarity). Interacts with DOCK11/Zizimin2; the interaction activates CDC42 by exchanging GDP for GTP (PubMed:15710388, PubMed:16968698). Interacts with DOCK9; the interaction activates CDC42 by exchanging GDP for GTP (By similarity). Interacts with DOCK8 (via DHR-2 domain); the interaction activates CDC42 by exchanging GDP for GTP (PubMed:22461490). Interacts with IQGAP1 (PubMed:16968698). Interacts with NET1 and ARHGAP33/TCGAP (PubMed:9535835, PubMed:12773384). Part of a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ (PubMed:10934474). The GTP-bound form interacts with CCPG1 (PubMed:17000758). 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 (By similarity). Interacts with ITGB1BP1 (By similarity). Interacts with ARHGDIA; this interaction inactivates and stabilizes CDC42. Interacts with ARHGDIB; this maintains CDC42 in the inactive, GDP-bound form (By similarity). Interacts in (GTP-bound form) with FNBP1L and ABI1, but only in the presence of FNBP1L (By similarity).By similarity8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • GTP-dependent protein binding Source: UniProtKB
  • mitogen-activated protein kinase kinase kinase binding Source: MGI
  • protein kinase binding Source: BHF-UCL
  • Rho GDP-dissociation inhibitor binding Source: MGI

Protein-protein interaction databases

BioGridi198627, 18 interactors
IntActiP60766, 18 interactors


Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi16 – 25Combined sources10
Beta strandi36 – 46Combined sources11
Beta strandi49 – 58Combined sources10
Helixi62 – 64Combined sources3
Turni65 – 67Combined sources3
Helixi68 – 71Combined sources4
Beta strandi76 – 83Combined sources8
Helixi87 – 95Combined sources9
Helixi97 – 104Combined sources8
Beta strandi110 – 115Combined sources6
Helixi117 – 121Combined sources5
Helixi123 – 131Combined sources9
Helixi139 – 148Combined sources10
Beta strandi154 – 156Combined sources3
Turni159 – 161Combined sources3
Helixi165 – 177Combined sources13
Beta strandi178 – 181Combined sources4
Helixi183 – 186Combined sources4

3D structure databases


Miscellaneous databases


Family & Domainsi


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi32 – 40Effector regionSequence analysis9

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0393 Eukaryota

Family and domain databases

CDDicd01874 Cdc42, 1 hit
InterProiView protein in InterPro
IPR037874 Cdc42
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR003578 Small_GTPase_Rho
PfamiView protein in Pfam
PF00071 Ras, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51420 RHO, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P60766-2) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
60 70 80 90 100
110 120 130 140 150
160 170 180 190
Mass (Da):21,259
Last modified:February 8, 2011 - v2
Isoform 1 (identifier: P60766-1) [UniParc] [UniParc]FASTAAdd to basket
Also known as: Brain

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

Show »
Mass (Da):21,311

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26N → D in BAC34669 (PubMed:16141072).Curated1
Sequence conflicti66R → G in AAH64792 (PubMed:15489334).Curated1
Sequence conflicti85V → I in BAE39489 (PubMed:16141072).Curated1
Sequence conflicti116Q → K in BAE40049 (PubMed:16141072).Curated1
Sequence conflicti171E → G in AAH64792 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_040585163K → R in isoform 1. Curated1
Alternative sequenceiVSP_040586182 – 191PKKSRRCVLL → TQPKRKCCIF in isoform 1. Curated10

Sequence databases

Select the link destinations:
Links Updated
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
CCDS57305.1 [P60766-1]
RefSeqiNP_001230698.1, NM_001243769.1 [P60766-1]
NP_033991.1, NM_009861.3 [P60766-2]

Genome annotation databases

EnsembliENSMUST00000030417; ENSMUSP00000030417; ENSMUSG00000006699 [P60766-1]
ENSMUST00000051477; ENSMUSP00000054634; ENSMUSG00000006699 [P60766-2]
UCSCiuc008viw.3 mouse
uc008viy.2 mouse [P60766-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiCDC42_MOUSE
AccessioniPrimary (citable) accession number: P60766
Secondary accession number(s): A2A9U6
, P21181, P25763, Q3THZ7, Q3TJK6, Q545V0, Q6P201, Q8BQ51
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 8, 2011
Last modified: July 18, 2018
This is version 164 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program


Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome


  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health