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Protein Page:
Cdc42 (mouse)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Cdc42 a small GTPase of the Rho-subfamily, which regulates signaling pathways that control diverse cellular functions including cell morphology, migration, endocytosis and cell cycle progression. Causes the formation of thin, actin-rich surface projections called filopodia. The oncoprotein Dbl specifically catalyzes the dissociation of GDP from this protein. Regulate actin polymerization through its direct binding to Neural Wiskott-Aldrich syndrome protein (N-WASP), which subsequently activates Arp2/3 complex. Interacts with DOCK9 which activates it by exchanging GDP for GTP. Interacts with PARD6A, PARD6B and PARD6G in a GTP-dependent manner. Part of a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ. Interacts with CDC42EP4.Alternative splicing of this gene results in at least two transcript variants. Note: This description may include information from UniProtKB.
Protein type: G protein; G protein, monomeric (Rho); Motility/polarity/chemotaxis
Cellular Component: neuron projection; secretory granule; Golgi membrane; cell projection; cytoskeleton; membrane; cell soma; apical part of cell; cytoplasm; plasma membrane; spindle midzone; midbody; intracellular; filopodium
Molecular Function: GTPase activity; identical protein binding; protein binding; GTP binding; GTP-dependent protein binding; thioesterase binding; nucleotide binding; mitogen-activated protein kinase kinase kinase binding; apolipoprotein A-I receptor binding; protein kinase binding
Biological Process: regulation of protein heterodimerization activity; filopodium formation; regulation of protein metabolic process; establishment and/or maintenance of cell polarity; positive regulation of JNK cascade; regulation of protein stability; regulation of filopodium formation; Wnt receptor signaling pathway through beta-catenin; endosome transport; Rho protein signal transduction; cell-cell adhesion; positive regulation of MAPKKK cascade; establishment of Golgi localization; GTP catabolic process; small GTPase mediated signal transduction; positive regulation of neuron apoptosis; epidermis morphogenesis; keratinization; regulation of mitosis; cell differentiation; Golgi organization and biogenesis; neuron fate determination; nervous system development; actin filament bundle formation; regulation of attachment of spindle microtubules to kinetochore; hair follicle morphogenesis; multicellular organism growth; positive regulation of phosphoinositide 3-kinase activity; actin filament organization; establishment and/or maintenance of apical/basal cell polarity; positive regulation of metalloenzyme activity; nucleus localization; positive regulation of peptidyl-serine phosphorylation; positive regulation of synapse structural plasticity; positive regulation of pseudopodium formation; heart contraction; regulation of protein catabolic process; positive regulation of protein amino acid phosphorylation; sprouting angiogenesis; actin cytoskeleton organization and biogenesis; regulation of protein kinase activity; negative regulation of protein complex assembly; nuclear migration; positive regulation of DNA replication
Reference #:  P60766 (UniProtKB)
Alt. Names/Synonyms: AI747189; AU018915; Cdc42; Cell division control protein 42 homolog; cell division cycle 42 homolog (S. cerevisiae); G25K GTP-binding protein; OTTMUSP00000010388
Gene Symbols: Cdc42
Molecular weight: 21,259 Da
Basal Isoelectric point: 6.16  Predict pI for various phosphorylation states
CST Pathways:  Adherens Junction Dynamics  |  B Cell Receptor Signaling  |  ErbB/HER Signaling  |  Regulation of Actin Dynamics  |  Regulation of Microtubule Dynamics  |  SAPK/JNK Signaling Cascades  |  T Cell Receptor Signaling  |  TGF-ß Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Cdc42

Protein Structure Not Found.


Scansite  |  Pfam  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

► Hide Isoforms
 
0 1 S30 YTTNKFPSEYVPTVF
0 3 Y32 TNKFPSEYVPTVFDN
1 0 Y32 TNKFPSEYVPTVFDN
0 2 T35 FPSEYVPTVFDNYAV
1 29 Y64 DTAGQEDYDRLRPLS
0 1 K96-u SFENVKEkWVPEITH
0 14 K107 EITHHCPKTPFLLVG
0 2 K128-u DDPSTIEkLAKNkQk
0 21 K133-u IEkLAKNkQkPITPE
0 1 K135 kLAKNkQKPITPEtA
0 5 K135-u kLAKNkQkPITPEtA
0 2 T141-p QkPITPEtAEkLARD
0 1 K144 ITPEtAEKLARDLKA
0 7 K144-u ITPEtAEkLARDLKA
0 2 K153 ARDLKAVKYVECSAL
0 9 K153-u ARDLKAVkYVECSAL
0 1 Y154 RDLKAVkYVECSALT
0 17 K163-u ECSALTQkGLKNVFD
0 7 K166 ALTQkGLKNVFDEAI
0 1 P182 AALEPPEPkkSRRCV
0 21 K183-u ALEPPEPkkSRRCVL
0 13 K184-u LEPPEPkkSRRCVLL
0 1 - under review  
  Cdc42 iso1  
S30 YTTNKFPSEYVPTVF
Y32 TNKFPSEYVPTVFDN
Y32 TNKFPSEYVPTVFDN
T35 FPSEYVPTVFDNYAV
Y64 DTAGQEDYDRLRPLS
K96 SFENVKEKWVPEITH
K107-u EITHHCPkTPFLLVG
K128 DDPSTIEKLAKNkQK
K133-u IEKLAKNkQKPITPE
K135 KLAKNkQKPITPETA
K135 KLAKNkQKPITPETA
T141 QKPITPETAEkLARD
K144 ITPETAEKLARDLKA
K144-u ITPETAEkLARDLKA
K153 ARDLKAVKYVECSAL
K153-u ARDLKAVkYVECSAL
Y154 RDLKAVkYVECSALT
R163 ECSALTQRGLKNVFD
K166 ALTQRGLKNVFDEAI
T182 AALEPPETQPkRKCC
Q183 ALEPPETQPkRKCCI
P184 LEPPETQPkRKCCIF
K185-u EPPETQPkRKCCIF_
  human

► Hide Isoforms
 
S30-p YTTNKFPsEyVPTVF
Y32-p TNKFPsEyVPTVFDN
Y32 TNKFPsEYVPTVFDN
T35 FPsEyVPTVFDNYAV
Y64-p DTAGQEDyDRLRPLS
K96 SFENVKEKWVPEITH
K107 EITHHCPKTPFLLVG
K128 DDPSTIEKLAKNKQK
K133 IEKLAKNKQKPITPE
K135 KLAKNKQKPITPEtA
K135 KLAKNKQKPITPEtA
T141-p QKPITPEtAEKLARD
K144 ITPEtAEKLARDLKA
K144 ITPEtAEKLARDLKA
K153-a ARDLKAVkYVECSAL
K153-u ARDLKAVkYVECSAL
Y154 RDLKAVkYVECSALT
K163-u ECSALTQkGLkNVFD
K166-u ALTQkGLkNVFDEAI
P182 AALEPPEPkkSRRCV
K183-u ALEPPEPkkSRRCVL
K184-u LEPPEPkkSRRCVLL
- under review  
  Cdc42 iso1  
S30 YTTNKFPSEyVPtVF
Y32-p TNKFPSEyVPtVFDN
Y32-ad TNKFPSEyVPtVFDN
T35-p FPSEyVPtVFDNYAV
Y64-p DTAGQEDyDRLRPLS
K96 SFENVKEKWVPEITH
K107-u EITHHCPkTPFLLVG
K128-u DDPSTIEkLAKNkQk
K133-u IEkLAKNkQkPITPE
K135-a kLAKNkQkPITPETA
K135-u kLAKNkQkPITPETA
T141 QkPITPETAEkLARD
K144-a ITPETAEkLARDLKA
K144-u ITPETAEkLARDLKA
K153 ARDLKAVKyVECSAL
K153-u ARDLKAVkyVECSAL
Y154-p RDLKAVkyVECSALT
R163 ECSALTQRGLKNVFD
K166 ALTQRGLKNVFDEAI
T182-p AALEPPEtQPKRKCC
Q183 ALEPPEtQPKRKCCI
P184 LEPPEtQPKRKCCIF
K185 EPPEtQPKRKCCIF_
  rat

 
S30 YTTNKFPSEYVPTVF
Y32 TNKFPSEYVPTVFDN
Y32 TNKFPSEYVPTVFDN
T35 FPSEYVPTVFDNYAV
Y64 DTAGQEDYDRLRPLS
K96 SFENVKEKWVPEITH
K107 EITHHCPKTPFLLVG
K128 DDPSTIEKLAKNkQk
K133-u IEKLAKNkQkPITPE
K135 KLAKNkQKPITPETA
K135-u KLAKNkQkPITPETA
T141 QkPITPETAEkLARD
K144 ITPETAEKLARDLKA
K144-u ITPETAEkLARDLKA
K153 ARDLKAVKYVECSAL
K153 ARDLKAVKYVECSAL
Y154 RDLKAVKYVECSALT
K163 ECSALTQKGLKNVFD
K166 ALTQKGLKNVFDEAI
P182 AALEPPEPKKSRRCV
K183 ALEPPEPKKSRRCVL
K184 LEPPEPKKSRRCVLL
- under review  
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