Cdc42
entrez
12540
canonical
uniprot
P60766
canonical
ensembl
ENSMUSG00000006699
resolver
ensp
ENSMUSP00000030417
resolver
ensp
ENSMUSP00000054634
resolver
ensp
ENSMUSP00000217244
resolver
ensp
ENSMUSP00000217248
resolver
ensp
ENSMUSP00000217255
resolver
ensp
ENSMUSP00000217258
resolver
ensp
ENSMUSP00000217261
resolver
ensp
ENSMUSP00000217263
resolver
ensp
ENSMUSP00000217268
resolver
ensp
ENSMUSP00000361660
resolver
genesymbol
Cdc42
resolver
uniprot
A2A9U6
resolver
uniprot
P21181
resolver
uniprot
P25763
resolver
uniprot
Q3THZ7
resolver
uniprot
Q3TJK6
resolver
uniprot
Q545V0
resolver
uniprot
Q6P201
resolver
uniprot
Q8BQ51
resolver
uniprot_entry
CDC42_MOUSE
resolver
uniprot_sec
A2A9U6
resolver
uniprot_sec
P21181
resolver
uniprot_sec
P25763
resolver
uniprot_sec
Q3THZ7
resolver
uniprot_sec
Q3TJK6
resolver
uniprot_sec
Q545V0
resolver
uniprot_sec
Q6P201
resolver
uniprot_sec
Q8BQ51
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. Inhibited by GAPs such as ARHGAP44 (PubMed:24352656, PubMed:26969129). {ECO:0000269|PubMed:15710388, ECO:0000269|PubMed:22461490, ECO:0000269|PubMed:24352656, ECO:0000269|PubMed:26969129}.
uniprot
proteins
amino_acid_sequence
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL
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 (PubMed:24352656). In its 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. Regulates cell migration (By similarity). In neurons, plays a role in the extension and maintenance of the formation of filopodia, thin and actin-rich surface projections. Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons (PubMed:25851601). Facilitates filopodia formation upon DOCK11-activation (PubMed:22494997). 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 (By similarity). Upon activation by PLEKHG4B, involved in actin cytoskeletal remodeling during epithelial cell-cell junction formation (By similarity). Negatively regulates polymerization of SEPTIN12, as a result may be involved in spermatogenesis (By similarity). {ECO:0000250|UniProtKB:P60953, ECO:0000250|UniProtKB:Q8CFN2, ECO:0000269|PubMed:22494997, ECO:0000269|PubMed:24352656, ECO:0000269|PubMed:25851601}.
uniprot
proteins
mass_dalton
21259
uniprot
proteins
mutagenesis
MUTAGEN 12; /note="G->V: No effect on filopodia formation."; /evidence="ECO:0000269|PubMed:22494997"; MUTAGEN 17; /note="T->N: Constitutively inactivated. Abolishes interaction with PARD6 and DOCK11. Inhibits filopodia formation."; /evidence="ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:16968698, ECO:0000269|PubMed:22494997"; MUTAGEN 61; /note="Q->L: Constitutively activated. Enhances interaction with DOCK11."; /evidence="ECO:0000269|PubMed:16968698
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by SRC in an EGF-dependent manner, this stimulates the binding of the Rho-GDP dissociation inhibitor RhoGDI. {ECO:0000250}.; PTM: Sumoylated; sumoylation is enhanced by TINCR and promotes CDC42 activation. {ECO:0000250|UniProtKB:P60953}.
uniprot
proteins
protein_family
CDC42 subfamily
uniprot
proteins
protein_family
Rho family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10490598
uniprot
proteins
pubmed
10934474
uniprot
proteins
pubmed
12773384
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15710388
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16968698
uniprot
proteins
pubmed
17000758
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22461490
uniprot
proteins
pubmed
22494997
uniprot
proteins
pubmed
24352656
uniprot
proteins
pubmed
25851601
uniprot
proteins
pubmed
26969129
uniprot
proteins
pubmed
30185885
uniprot
proteins
pubmed
30189608
uniprot
proteins
pubmed
8464478
uniprot
proteins
pubmed
8954774
uniprot
proteins
pubmed
9224952
uniprot
proteins
pubmed
9535835
uniprot
proteins
sequence_length
191
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22461490, ECO:0000269|PubMed:30185885}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Midbody {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P60953}. Cytoplasm {ECO:0000269|PubMed:22461490}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:22461490}; Peripheral membrane protein {ECO:0000305|PubMed:22461490}; Cytoplasmic side {ECO:0000305|PubMed:22461490}. Cell projection, dendrite {ECO:0000269|PubMed:24352656}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:30189608}. Note=Localizes to spindle during prometaphase cells (By similarity). 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 (By similarity). 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). In its active GTP-bound form localizes to the leading edge membrane of migrating dendritic cells (PubMed:22461490). During sperm head formation in elongating spermatids, expressed at the acrosome, perinuclear mantle of the manchette structure and the sperm neck (PubMed:30189608). Expressed at the neck and mitochondrial materials in elongated spermatids (PubMed:30189608). Expressed at the midpiece in mature spermatozoa (PubMed:30189608). {ECO:0000250|UniProtKB:P60953, ECO:0000269|PubMed:22461490, ECO:0000269|PubMed:30189608}.
uniprot
proteins