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Protein Page:
Cdc42 iso1 (human)
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 iso1 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: Motility/polarity/chemotaxis; G protein, monomeric (Rho); G protein
Cellular Component: Golgi membrane; neuron projection; cell soma; apical part of cell; cytoplasm; plasma membrane; microtubule organizing center; spindle midzone; midbody; cytosol; filopodium; secretory granule
Molecular Function: GTPase activity; identical protein binding; protein binding; GTP binding; GTP-dependent protein binding; thioesterase binding; mitogen-activated protein kinase kinase kinase binding; apolipoprotein A-I receptor binding; protein kinase binding
Biological Process: negative regulation of epidermal growth factor receptor signaling pathway; axon guidance; regulation of protein heterodimerization activity; macrophage differentiation; filopodium formation; establishment and/or maintenance of cell polarity; regulation of protein stability; positive regulation of JNK cascade; regulation of filopodium formation; Wnt receptor signaling pathway through beta-catenin; GTP catabolic process; establishment of Golgi localization; keratinization; small GTPase mediated signal transduction; regulation of mitosis; Golgi organization and biogenesis; neuron fate determination; epidermal growth factor receptor signaling pathway; 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; establishment and/or maintenance of apical/basal cell polarity; positive regulation of peptidyl-serine phosphorylation; muscle cell differentiation; regulation of small GTPase mediated signal transduction; positive regulation of pseudopodium formation; heart contraction; T cell costimulation; positive regulation of muscle cell differentiation; regulation of protein catabolic process; regulation of protein kinase activity; blood coagulation; actin cytoskeleton organization and biogenesis; negative regulation of protein complex assembly; nuclear migration; positive regulation of DNA replication
Reference #:  P60953-1 (UniProtKB)
Alt. Names/Synonyms: CDC42; CDC42Hs; Cell division control protein 42 homolog; cell division cycle 42 (GTP binding protein, 25kDa); dJ224A6.1.1 (cell division cycle 42 (GTP-binding protein, 25kD)); dJ224A6.1.2 (cell division cycle 42 (GTP-binding protein, 25kD)); G25K; G25K GTP-binding protein; growth-regulating protein; GTP-binding protein, 25kD; small GTP binding protein CDC42
Gene Symbols: CDC42
Molecular weight: 21,311 Da
Basal Isoelectric point: 5.76  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 iso1

Protein Structure Not Found.


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Sites Implicated In
cell growth, altered: Y64‑p
activation: Y64‑p
molecular association, regulation: Y64‑p

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.


       human

► Hide Isoforms
 
0 1 S30-p YTTNKFPsEyVPTVF
0 3 Y32-p TNKFPsEyVPTVFDN
1 0 Y32 TNKFPsEYVPTVFDN
0 2 T35 FPsEyVPTVFDNYAV
1 29 Y64-p DTAGQEDyDRLRPLS
0 1 K96 SFENVKEKWVPEITH
0 14 K107 EITHHCPKTPFLLVG
0 2 K128 DDPSTIEKLAKNKQK
0 21 K133 IEKLAKNKQKPITPE
0 1 K135 KLAKNKQKPITPEtA
0 5 K135 KLAKNKQKPITPEtA
0 2 T141-p QKPITPEtAEKLARD
0 1 K144 ITPEtAEKLARDLKA
0 7 K144 ITPEtAEKLARDLKA
0 2 K153-a ARDLKAVkYVECSAL
0 9 K153-u ARDLKAVkYVECSAL
0 1 Y154 RDLKAVkYVECSALT
0 17 K163-u ECSALTQkGLkNVFD
0 7 K166-u ALTQkGLkNVFDEAI
0 1 P182 AALEPPEPkkSRRCV
0 21 K183-u ALEPPEPkkSRRCVL
0 13 K184-u LEPPEPkkSRRCVLL
0 1 - 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_
  mouse

► Hide Isoforms
 
S30 YTTNKFPSEYVPTVF
Y32 TNKFPSEYVPTVFDN
Y32 TNKFPSEYVPTVFDN
T35 FPSEYVPTVFDNYAV
Y64 DTAGQEDYDRLRPLS
K96-u SFENVKEkWVPEITH
K107 EITHHCPKTPFLLVG
K128-u DDPSTIEkLAKNkQk
K133-u IEkLAKNkQkPITPE
K135 kLAKNkQKPITPEtA
K135-u kLAKNkQkPITPEtA
T141-p QkPITPEtAEkLARD
K144 ITPEtAEKLARDLKA
K144-u ITPEtAEkLARDLKA
K153 ARDLKAVKYVECSAL
K153-u ARDLKAVkYVECSAL
Y154 RDLKAVkYVECSALT
K163-u ECSALTQkGLKNVFD
K166 ALTQkGLKNVFDEAI
P182 AALEPPEPkkSRRCV
K183-u ALEPPEPkkSRRCVL
K184-u LEPPEPkkSRRCVLL
- 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_
  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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