CDC42
entrez
998
canonical
uniprot
P60953
canonical
ensembl
ENSG00000070831
resolver
ensembl
ENSG00000289694
resolver
ensp
ENSP00000314458
resolver
ensp
ENSP00000341072
resolver
ensp
ENSP00000499457
resolver
genesymbol
CDC42
resolver
hgnc
HGNC:1736
resolver
uniprot
P21181
resolver
uniprot
P25763
resolver
uniprot
Q7L8R5
resolver
uniprot
Q9UDI2
resolver
uniprot_entry
CDC42_HUMAN
resolver
uniprot_sec
P21181
resolver
uniprot_sec
P25763
resolver
uniprot_sec
Q7L8R5
resolver
uniprot_sec
Q9UDI2
resolver
activity_regulation
ACTIVITY 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. {ECO:0000269|PubMed:12172552}.
uniprot
proteins
amino_acid_sequence
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL
uniprot
proteins
disease_involvement
DISEASE: Takenouchi-Kosaki syndrome (TKS) [MIM:616737]: An autosomal dominant syndrome characterized by macrothrombocytopenia, lymphedema, intellectual disability, developmental delay, and distinctive facial features. {ECO:0000269|PubMed:26386261, ECO:0000269|PubMed:26708094}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
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 (PubMed:15642749). Regulates cell migration (PubMed:17038317, PubMed:22843693). In neurons, plays a role in the extension and maintenance of the formation of filopodia, thin and actin-rich surface projections (PubMed:14978216). Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. In podocytes, facilitates filopodia and podosomes formation upon DOCK11-activation (PubMed:33523862). Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling (By similarity). Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups (PubMed:26465210). Upon activation by PLEKHG4B, involved in actin cytoskeletal remodeling during epithelial cell-cell junction formation (PubMed:33310911). Negatively regulates polymerization of SEPTIN12, as a result may be involved in spermatogenesis (PubMed:30189608). {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:Q8CFN2, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:22843693, ECO:0000269|PubMed:26465210, ECO:0000269|PubMed:30189608, ECO:0000269|PubMed:33310911, ECO:0000269|PubMed:33523862}.
uniprot
proteins
mass_dalton
21259
uniprot
proteins
mutagenesis
MUTAGEN 12; /note="G->V: Constitutively active. Interacts with PARD6 proteins. Does not inhibit filopodia formation. No effect on NR3C2 transcriptional activity."; /evidence="ECO:0000269|PubMed:10954424, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:19029984"; MUTAGEN 17; /note="T->N: Constitutively inactive. Does not interact with PARD6 proteins. Inhibits filopodia formation. No effect on NR3C2 transcriptional activity. Abolishes polymerization of SEPTIN12."; /evidence="ECO:0000269|PubMed:11260256, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:19029984, ECO:0000269|PubMed:30189608"; MUTAGEN 32; /note="Y->F: Abolishes AMPylation by Haemophilus IbpA."; /evidence="ECO:0000269|PubMed:19362538"; MUTAGEN 61; /note="Q->L: Constitutively active. Interacts with PARD6 proteins. Enhances polymerization of SEPTIN12."; /evidence="ECO:0000269|PubMed:11260256, ECO:0000269|PubMed:30189608
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) 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. {ECO:0000269|PubMed:19039103, ECO:0000269|PubMed:19362538, ECO:0000269|PubMed:20622875}.; PTM: Phosphorylated by SRC in an EGF-dependent manner, this stimulates the binding of the Rho-GDP dissociation inhibitor RhoGDI. {ECO:0000269|PubMed:14506284}.; PTM: (Microbial infection) Glycosylated at Tyr-32 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of CDC42 and leads to actin disassembly. {ECO:0000269|PubMed:24141704}.; PTM: (Microbial infection) Glucosylated at Thr-35 by C.difficile toxins TcdA and TcdB in the colonic epithelium (PubMed:24905543, PubMed:7775453, PubMed:7777059). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption and cell death, resulting in the loss of colonic epithelial barrier function (PubMed:7775453, PubMed:7777059). {ECO:0000269|PubMed:24905543, ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059}.; PTM: (Microbial infection) Glycosylated (O-GlcNAcylated) at Thr-35 by C.novyi toxin TcdA (PubMed:8810274). O-GlcNAcylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption (PubMed:8810274). {ECO:0000269|PubMed:8810274}.; PTM: Sumoylated; sumoylation is enhanced by TINCR and promotes CDC42 activation. {ECO:0000269|PubMed:36369429}.
uniprot
proteins
protein_family
CDC42 subfamily
uniprot
proteins
protein_family
Rho family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10211824
uniprot
proteins
pubmed
10490598
uniprot
proteins
pubmed
10587647
uniprot
proteins
pubmed
10676816
uniprot
proteins
pubmed
10816584
uniprot
proteins
pubmed
10954424
uniprot
proteins
pubmed
11130076
uniprot
proteins
pubmed
11260256
uniprot
proteins
pubmed
11807099
uniprot
proteins
pubmed
12172552
uniprot
proteins
pubmed
12612085
uniprot
proteins
pubmed
14506284
uniprot
proteins
pubmed
14978216
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15642749
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17038317
uniprot
proteins
pubmed
19029984
uniprot
proteins
pubmed
19039103
uniprot
proteins
pubmed
19362538
uniprot
proteins
pubmed
19745154
uniprot
proteins
pubmed
19798448
uniprot
proteins
pubmed
20622875
uniprot
proteins
pubmed
20873783
uniprot
proteins
pubmed
21139582
uniprot
proteins
pubmed
2122236
uniprot
proteins
pubmed
2124704
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21565175
uniprot
proteins
pubmed
22461490
uniprot
proteins
pubmed
22843693
uniprot
proteins
pubmed
23434736
uniprot
proteins
pubmed
23940119
uniprot
proteins
pubmed
24141704
uniprot
proteins
pubmed
24905543
uniprot
proteins
pubmed
2496687
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26386261
uniprot
proteins
pubmed
26465210
uniprot
proteins
pubmed
26708094
uniprot
proteins
pubmed
30189608
uniprot
proteins
pubmed
33310911
uniprot
proteins
pubmed
33523862
uniprot
proteins
pubmed
36369429
uniprot
proteins
pubmed
7512369
uniprot
proteins
pubmed
7775453
uniprot
proteins
pubmed
7777059
uniprot
proteins
pubmed
8504089
uniprot
proteins
pubmed
8810274
uniprot
proteins
pubmed
9220962
uniprot
proteins
pubmed
9262406
uniprot
proteins
pubmed
9760238
uniprot
proteins
sequence_length
191
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22843693}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15642749}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15642749}. Midbody {ECO:0000269|PubMed:15642749}. Cell projection, dendrite {ECO:0000250|UniProtKB:P60766}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P60766}. Note=Localizes to spindle during prometaphase cells. Moves to the central spindle as cells progressed through anaphase to telophase (PubMed:15642749). Localizes at the end of cytokinesis in the intercellular bridge formed between two daughter cells (PubMed:15642749). Its localization is regulated by the activities of guanine nucleotide exchange factor ECT2 and GTPase activating protein RACGAP1 (PubMed:15642749). Colocalizes with NEK6 in the centrosome (PubMed:20873783). In its active GTP-bound form localizes to the leading edge membrane of migrating dendritic cells (By similarity). During sperm head formation in elongating spermatids, expressed at the acrosome, perinuclear mantle of the manchette structure and the sperm neck (By similarity). Expressed at the neck and mitochondrial materials in elongated spermatids (By similarity). Expressed at the midpiece in mature spermatozoa (By similarity). {ECO:0000250|UniProtKB:P60766, ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:20873783}.
uniprot
proteins