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Protein

Cell division control protein 42 homolog

Gene

CDC42

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. Facilitates filopodia formation upon DOCK11-activation (By similarity). Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups.By similarity4 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi10 – 17GTP8
Nucleotide bindingi57 – 61GTPBy similarity5
Nucleotide bindingi115 – 118GTP4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processDifferentiation, Neurogenesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114604 GPVI-mediated activation cascade
R-HSA-182971 EGFR downregulation
R-HSA-194840 Rho GTPase cycle
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-375170 CDO in myogenesis
R-HSA-389359 CD28 dependent Vav1 pathway
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-418885 DCC mediated attractive signaling
R-HSA-428543 Inactivation of CDC42 and RAC1
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-5625970 RHO GTPases activate KTN1
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5627123 RHO GTPases activate PAKs
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P60953

SIGNOR Signaling Network Open Resource

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SIGNORi
P60953

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P60953 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cell division control protein 42 homolog
Alternative name(s):
G25K GTP-binding protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CDC42
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000070831.15

Human Gene Nomenclature Database

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HGNCi
HGNC:1736 CDC42

Online Mendelian Inheritance in Man (OMIM)

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MIMi
116952 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P60953

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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, Cytoplasm, Cytoskeleton, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Takenouchi-Kosaki syndrome (TKS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by macrothrombocytopenia, lymphedema, mental retardation, developmental delay, and distinctive facial features.
See also OMIM:616737
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07633764Y → C in TKS. 2 PublicationsCorresponds to variant dbSNP:rs864309721EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi12G → V: Constitutively active. Interacts with PARD6 proteins. Does not inhibit filopodia formation. No effect on NR3C2 transcriptional activity. 3 Publications1
Mutagenesisi17T → N: Constitutively inactive. Does not interact with PARD6 proteins. Inhibits filopodia formation. No effect on NR3C2 transcriptional activity. 3 Publications1
Mutagenesisi32Y → F: Abolishes AMPylation by Haemophilus IbpA. 1 Publication1
Mutagenesisi61Q → L: Constitutively active. Interacts with PARD6 proteins. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
998

MalaCards human disease database

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MalaCardsi
CDC42
MIMi616737 phenotype

Open Targets

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OpenTargetsi
ENSG00000070831

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
487796 Macrothrombocytopenia-lymphedema-developmental delay-facial dysmorphism-camptodactyly syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26266

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL6088

Drug and drug target database

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DrugBanki
DB02623 Aminophosphonic Acid-Guanylate Ester
DB04315 Guanosine-5'-Diphosphate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CDC42

Domain mapping of disease mutations (DMDM)

More...
DMDMi
322510015

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000304251 – 188Cell division control protein 42 homologAdd BLAST188
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000030426189 – 191Removed in mature form3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei32O-AMP-tyrosine; by Haemophilus IbpA; alternate2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi32O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate1 Publication1
Modified residuei35O-AMP-threonine; by Vibrio VopS1 Publication1
Modified residuei64Phosphotyrosine; by SRC1 Publication1
Modified residuei188Cysteine methyl esterCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi188S-geranylgeranyl cysteineCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

(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.3 Publications
Phosphorylated by SRC in an EGF-dependent manner, this stimulates the binding of the Rho-GDP dissociation inhibitor RhoGDI.1 Publication
(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.1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P60953

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P60953

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P60953

PeptideAtlas

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PeptideAtlasi
P60953

PRoteomics IDEntifications database

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PRIDEi
P60953

ProteomicsDB human proteome resource

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ProteomicsDBi
57238
57239 [P60953-1]

Consortium for Top Down Proteomics

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TopDownProteomicsi
P60953-2 [P60953-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P60953

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P60953

SwissPalm database of S-palmitoylation events

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SwissPalmi
P60953

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P60953

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000070831 Expressed in 231 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_CDC42

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P60953 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P60953 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004360
HPA069590

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4, CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-dependent manner) (PubMed:10490598, PubMed:10816584, PubMed:10954424, PubMed:11260256). Interacts with activated CSPG4 and with BAIAP2 (PubMed:10587647, PubMed:11130076). Interacts with activated CSPG4 and with BAIAP2 (By similarity). Interacts with DOCK11/Zizimin2; the interaction activates CDC42 by exchanging GDP for GTP (By similarity). Interacts with DOCK9; the interaction activates CDC42 by exchanging GDP for GTP (PubMed:12172552, PubMed:19745154). Interacts with DOCK8 (via DHR-2 domain); the interaction activates CDC42 by exchanging GDP for GTP (PubMed:12172552). Interacts with IQGAP1 (By similarity). Interacts with NET1 and ARHGAP33/TCGAP (By similarity). Part of a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ (PubMed:11260256). The GTP-bound form interacts with CCPG1 (By similarity). Interacts with USP6 (PubMed:12612085). Interacts with NEK6 (PubMed:20873783). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (PubMed:17038317). Interacts with ITGB1BP1 (PubMed:11807099). Interacts with ARHGDIA; this interaction inactivates and stabilizes CDC42 (PubMed:23434736). Interacts with ARHGDIB; this maintains CDC42 in the inactive, GDP-bound form (PubMed:7512369). Interacts (in GTP-bound form) with FNBP1L and ABI1, but only in the presence of FNBP1L (PubMed:19798448). May interact with ARHGEF16; responsible for the activation of CDC42 by the viral protein HPV16 E6 (PubMed:21139582).By similarity17 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107433, 215 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P60953

Database of interacting proteins

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DIPi
DIP-31097N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P60953

Protein interaction database and analysis system

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IntActi
P60953, 220 interactors

Molecular INTeraction database

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MINTi
P60953

STRING: functional protein association networks

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STRINGi
9606.ENSP00000314458

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P60953

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A4RX-ray2.50A/B1-191[»]
1AJENMR-A1-187[»]
1AM4X-ray2.70D/E/F2-177[»]
1AN0X-ray2.80A/B1-190[»]
1CEENMR-A1-179[»]
1CF4NMR-A1-184[»]
1DOAX-ray2.60A1-188[»]
1E0ANMR-A1-184[»]
1EESNMR-A1-178[»]
1GRNX-ray2.10A1-191[»]
1GZSX-ray2.30A/C1-178[»]
1KI1X-ray2.30A/C1-188[»]
1KZ7X-ray2.40B/D1-188[»]
1KZGX-ray2.60B/D1-188[»]
1NF3X-ray2.10A/B2-191[»]
2ASENMR-A1-178[»]
2DFKX-ray2.15B/D1-191[»]
2KB0NMR-A1-178[»]
2NGRX-ray1.90A1-191[»]
2ODBX-ray2.40A1-191[»]
2QRZX-ray2.40A/B1-189[»]
2WM9X-ray2.20B1-188[»]
2WMNX-ray2.39B1-188[»]
2WMOX-ray2.20B1-188[»]
3GCGX-ray2.30A2-178[»]
3QBVX-ray2.65A/C1-178[»]
3VHLX-ray2.08B1-188[»]
4DIDX-ray2.35A1-183[»]
4ITRX-ray2.30C/D1-191[»]
4JS0X-ray1.90A1-178[»]
4YC7X-ray2.50A1-179[»]
4YDHX-ray3.80B/D1-179[»]
5CJPX-ray2.60A/B/C/D1-177[»]
5FI1X-ray3.20B1-191[»]
5HZKX-ray3.30A/C1-181[»]
5UPKX-ray2.40C1-177[»]
5UPLX-ray3.00B1-177[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P60953

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P60953

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P60953

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi32 – 40Effector regionSequence analysis9

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0393 Eukaryota
COG1100 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153675

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233974

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG009351

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P60953

KEGG Orthology (KO)

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KOi
K04393

Identification of Orthologs from Complete Genome Data

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OMAi
MQNMKCV

Database of Orthologous Groups

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OrthoDBi
1091615at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P60953

TreeFam database of animal gene trees

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TreeFami
TF101109

Family and domain databases

Conserved Domains Database

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CDDi
cd01874 Cdc42, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR037874 Cdc42
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR003578 Small_GTPase_Rho

Pfam protein domain database

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Pfami
View protein in Pfam
PF00071 Ras, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51420 RHO, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 2 (identifier: P60953-2) [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
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP
60 70 80 90 100
YTLGLFDTAG QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE
110 120 130 140 150
ITHHCPKTPF LLVGTQIDLR DDPSTIEKLA KNKQKPITPE TAEKLARDLK
160 170 180 190
AVKYVECSAL TQKGLKNVFD EAILAALEPP EPKKSRRCVL L
Length:191
Mass (Da):21,259
Last modified:February 8, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i51A437E22A4D8FFF
GO
Isoform 1 (identifier: P60953-1) [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
     182-191: PKKSRRCVLL → TQPKRKCCIF

Show »
Length:191
Mass (Da):21,311
Checksum:i34B44F9225EC106B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5JYX0Q5JYX0_HUMAN
Cell division control protein 42 ho...
CDC42
136Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A3B3IRV0A0A3B3IRV0_HUMAN
Cell division control protein 42 ho...
CDC42
41Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07633764Y → C in TKS. 2 PublicationsCorresponds to variant dbSNP:rs864309721EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_040583163K → R in isoform 1. 3 Publications1
Alternative sequenceiVSP_040584182 – 191PKKSRRCVLL → TQPKRKCCIF in isoform 1. 3 Publications10

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M35543 mRNA Translation: AAA52494.1
M57298 mRNA Translation: AAA52592.1
AL121734 mRNA Translation: CAB57325.1
AL121735 mRNA Translation: CAB57326.1
AF498962 mRNA Translation: AAM21109.1
AF498963 mRNA Translation: AAM21110.1
AY673602 Genomic DNA Translation: AAT70721.1
AL031281 Genomic DNA No translation available.
BC002711 mRNA Translation: AAH02711.1
BC003682 mRNA Translation: AAH03682.1
BC018266 mRNA Translation: AAH18266.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS221.1
CCDS222.1 [P60953-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A36382
A39265

NCBI Reference Sequences

More...
RefSeqi
NP_001034891.1, NM_001039802.1 [P60953-2]
NP_001782.1, NM_001791.3 [P60953-2]
NP_426359.1, NM_044472.2 [P60953-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.467637

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000315554; ENSP00000314458; ENSG00000070831 [P60953-1]
ENST00000344548; ENSP00000341072; ENSG00000070831 [P60953-2]
ENST00000400259; ENSP00000383118; ENSG00000070831 [P60953-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
998

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:998

UCSC genome browser

More...
UCSCi
uc001bfp.4 human

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35543 mRNA Translation: AAA52494.1
M57298 mRNA Translation: AAA52592.1
AL121734 mRNA Translation: CAB57325.1
AL121735 mRNA Translation: CAB57326.1
AF498962 mRNA Translation: AAM21109.1
AF498963 mRNA Translation: AAM21110.1
AY673602 Genomic DNA Translation: AAT70721.1
AL031281 Genomic DNA No translation available.
BC002711 mRNA Translation: AAH02711.1
BC003682 mRNA Translation: AAH03682.1
BC018266 mRNA Translation: AAH18266.1
CCDSiCCDS221.1
CCDS222.1 [P60953-1]
PIRiA36382
A39265
RefSeqiNP_001034891.1, NM_001039802.1 [P60953-2]
NP_001782.1, NM_001791.3 [P60953-2]
NP_426359.1, NM_044472.2 [P60953-1]
UniGeneiHs.467637

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A4RX-ray2.50A/B1-191[»]
1AJENMR-A1-187[»]
1AM4X-ray2.70D/E/F2-177[»]
1AN0X-ray2.80A/B1-190[»]
1CEENMR-A1-179[»]
1CF4NMR-A1-184[»]
1DOAX-ray2.60A1-188[»]
1E0ANMR-A1-184[»]
1EESNMR-A1-178[»]
1GRNX-ray2.10A1-191[»]
1GZSX-ray2.30A/C1-178[»]
1KI1X-ray2.30A/C1-188[»]
1KZ7X-ray2.40B/D1-188[»]
1KZGX-ray2.60B/D1-188[»]
1NF3X-ray2.10A/B2-191[»]
2ASENMR-A1-178[»]
2DFKX-ray2.15B/D1-191[»]
2KB0NMR-A1-178[»]
2NGRX-ray1.90A1-191[»]
2ODBX-ray2.40A1-191[»]
2QRZX-ray2.40A/B1-189[»]
2WM9X-ray2.20B1-188[»]
2WMNX-ray2.39B1-188[»]
2WMOX-ray2.20B1-188[»]
3GCGX-ray2.30A2-178[»]
3QBVX-ray2.65A/C1-178[»]
3VHLX-ray2.08B1-188[»]
4DIDX-ray2.35A1-183[»]
4ITRX-ray2.30C/D1-191[»]
4JS0X-ray1.90A1-178[»]
4YC7X-ray2.50A1-179[»]
4YDHX-ray3.80B/D1-179[»]
5CJPX-ray2.60A/B/C/D1-177[»]
5FI1X-ray3.20B1-191[»]
5HZKX-ray3.30A/C1-181[»]
5UPKX-ray2.40C1-177[»]
5UPLX-ray3.00B1-177[»]
ProteinModelPortaliP60953
SMRiP60953
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107433, 215 interactors
CORUMiP60953
DIPiDIP-31097N
ELMiP60953
IntActiP60953, 220 interactors
MINTiP60953
STRINGi9606.ENSP00000314458

Chemistry databases

BindingDBiP60953
ChEMBLiCHEMBL6088
DrugBankiDB02623 Aminophosphonic Acid-Guanylate Ester
DB04315 Guanosine-5'-Diphosphate

Protein family/group databases

MoonDBiP60953 Predicted

PTM databases

iPTMnetiP60953
PhosphoSitePlusiP60953
SwissPalmiP60953

Polymorphism and mutation databases

BioMutaiCDC42
DMDMi322510015

Proteomic databases

EPDiP60953
jPOSTiP60953
PaxDbiP60953
PeptideAtlasiP60953
PRIDEiP60953
ProteomicsDBi57238
57239 [P60953-1]
TopDownProteomicsiP60953-2 [P60953-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
998
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315554; ENSP00000314458; ENSG00000070831 [P60953-1]
ENST00000344548; ENSP00000341072; ENSG00000070831 [P60953-2]
ENST00000400259; ENSP00000383118; ENSG00000070831 [P60953-2]
GeneIDi998
KEGGihsa:998
UCSCiuc001bfp.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
998
DisGeNETi998
EuPathDBiHostDB:ENSG00000070831.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CDC42
HGNCiHGNC:1736 CDC42
HPAiCAB004360
HPA069590
MalaCardsiCDC42
MIMi116952 gene
616737 phenotype
neXtProtiNX_P60953
OpenTargetsiENSG00000070831
Orphaneti487796 Macrothrombocytopenia-lymphedema-developmental delay-facial dysmorphism-camptodactyly syndrome
PharmGKBiPA26266

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0393 Eukaryota
COG1100 LUCA
GeneTreeiENSGT00940000153675
HOGENOMiHOG000233974
HOVERGENiHBG009351
InParanoidiP60953
KOiK04393
OMAiMQNMKCV
OrthoDBi1091615at2759
PhylomeDBiP60953
TreeFamiTF101109

Enzyme and pathway databases

ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-182971 EGFR downregulation
R-HSA-194840 Rho GTPase cycle
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-375170 CDO in myogenesis
R-HSA-389359 CD28 dependent Vav1 pathway
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-418885 DCC mediated attractive signaling
R-HSA-428543 Inactivation of CDC42 and RAC1
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-5625970 RHO GTPases activate KTN1
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5627123 RHO GTPases activate PAKs
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SignaLinkiP60953
SIGNORiP60953

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CDC42 human
EvolutionaryTraceiP60953

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
CDC42

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
998
PMAP-CutDBiP60953

Protein Ontology

More...
PROi
PR:P60953

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000070831 Expressed in 231 organ(s), highest expression level in testis
CleanExiHS_CDC42
ExpressionAtlasiP60953 baseline and differential
GenevisibleiP60953 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDC42_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P60953
Secondary accession number(s): P21181
, P25763, Q7L8R5, Q9UDI2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 8, 2011
Last modified: January 16, 2019
This is version 192 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
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