UniProtKB - P60953 (CDC42_HUMAN)
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Protein
Cell division control protein 42 homolog
Gene
CDC42
Organism
Homo sapiens (Human)
Status
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).By similarity3 Publications
Enzyme 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.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Nucleotide bindingi | 10 – 17 | GTP | 8 | |
| Nucleotide bindingi | 57 – 61 | GTPBy similarity | 5 | |
| Nucleotide bindingi | 115 – 118 | GTP | 4 |
GO - Molecular functioni
- apolipoprotein A-I receptor binding Source: BHF-UCL
- GBD domain binding Source: CAFA
- GTPase activity Source: UniProtKB
- GTP binding Source: UniProtKB
- GTP-dependent protein binding Source: Ensembl
- identical protein binding Source: IntAct
- mitogen-activated protein kinase kinase kinase binding Source: Ensembl
- protein kinase binding Source: BHF-UCL
- Rho GDP-dissociation inhibitor binding Source: Ensembl
- thioesterase binding Source: UniProtKB
- ubiquitin protein ligase activity Source: AgBase
GO - Biological processi
- actin cytoskeleton organization Source: UniProtKB
- actin filament branching Source: Ensembl
- actin filament bundle assembly Source: Ensembl
- adherens junction organization Source: Ensembl
- blood coagulation Source: Reactome
- canonical Wnt signaling pathway Source: Ensembl
- cardiac conduction system development Source: Ensembl
- Cdc42 protein signal transduction Source: Ensembl
- cellular protein localization Source: Ensembl
- dendritic cell migration Source: Ensembl
- dendritic spine morphogenesis Source: UniProtKB
- ephrin receptor signaling pathway Source: Reactome
- epithelial cell-cell adhesion Source: Ensembl
- epithelial-mesenchymal cell signaling Source: Ensembl
- establishment of Golgi localization Source: BHF-UCL
- establishment or maintenance of apical/basal cell polarity Source: Ensembl
- establishment or maintenance of cell polarity Source: UniProtKB
- Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
- filopodium assembly Source: Ensembl
- Golgi organization Source: BHF-UCL
- hair follicle morphogenesis Source: Ensembl
- hair follicle placode formation Source: Ensembl
- heart contraction Source: Ensembl
- keratinization Source: Ensembl
- keratinocyte development Source: Ensembl
- macrophage differentiation Source: UniProtKB
- modification of synaptic structure Source: Ensembl
- multicellular organism growth Source: Ensembl
- negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
- negative regulation of gene expression Source: Ensembl
- negative regulation of protein complex assembly Source: UniProtKB
- neuron fate determination Source: Ensembl
- nuclear migration Source: Ensembl
- organelle transport along microtubule Source: BHF-UCL
- positive regulation of cell growth Source: AgBase
- positive regulation of cytokinesis Source: UniProtKB
- positive regulation of DNA replication Source: Ensembl
- positive regulation of epithelial cell proliferation involved in lung morphogenesis Source: Ensembl
- positive regulation of filopodium assembly Source: UniProtKB
- positive regulation of gene expression Source: Ensembl
- positive regulation of hair follicle cell proliferation Source: Ensembl
- positive regulation of intracellular protein transport Source: Ensembl
- positive regulation of JNK cascade Source: Ensembl
- positive regulation of lamellipodium assembly Source: CAFA
- positive regulation of muscle cell differentiation Source: Reactome
- positive regulation of neuron apoptotic process Source: Ensembl
- positive regulation of peptidyl-serine phosphorylation Source: Ensembl
- positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
- positive regulation of pseudopodium assembly Source: UniProtKB
- positive regulation of stress fiber assembly Source: CAFA
- positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
- positive regulation of synapse structural plasticity Source: Ensembl
- regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
- regulation of filopodium assembly Source: UniProtKB
- regulation of lamellipodium assembly Source: CAFA
- regulation of mitotic nuclear division Source: Ensembl
- regulation of protein catabolic process Source: Ensembl
- regulation of protein heterodimerization activity Source: Ensembl
- regulation of protein kinase activity Source: Ensembl
- regulation of protein stability Source: Ensembl
- regulation of small GTPase mediated signal transduction Source: Reactome
- regulation of stress fiber assembly Source: CAFA
- sprouting angiogenesis Source: Ensembl
- submandibular salivary gland formation Source: Ensembl
- substantia nigra development Source: UniProtKB
- T cell costimulation Source: Reactome
- vascular endothelial growth factor receptor signaling pathway Source: Reactome
- viral RNA genome replication Source: ParkinsonsUK-UCL
- Wnt signaling pathway, planar cell polarity pathway Source: ParkinsonsUK-UCL
Keywordsi
| Biological process | Differentiation, Neurogenesis |
| Ligand | GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
| 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-416482. G alpha (12/13) signalling events. R-HSA-416572. Sema4D induced cell migration and growth-cone collapse. R-HSA-418885. DCC mediated attractive signaling. R-HSA-428543. Inactivation of Cdc42 and Rac. 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-983231. Factors involved in megakaryocyte development and platelet production. |
| SignaLinki | P60953. |
| SIGNORi | P60953. |
Names & Taxonomyi
| Protein namesi | Recommended name: Cell division control protein 42 homologAlternative name(s): G25K GTP-binding protein |
| Gene namesi | Name:CDC42 |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi |
|
Organism-specific databases
| HGNCi | HGNC:1736. CDC42. |
Subcellular locationi
- Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated
- Cytoplasm › cytoskeleton › microtubule organizing center › centrosome
- Cytoplasm › cytoskeleton › spindle
- Midbody
Note: Localizes to spindle during prometaphase cells. 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. Its localization is regulated by the activities of guanine nucleotide exchange factor ECT2 and GTPase activating protein RACGAP1. Colocalizes with NEK6 in the centrosome.
GO - Cellular componenti
- apical part of cell Source: Ensembl
- cell-cell junction Source: Ensembl
- cytoplasm Source: UniProtKB
- cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
- cytosol Source: Reactome
- dendritic spine Source: SynGO
- endoplasmic reticulum membrane Source: Reactome
- extracellular exosome Source: UniProtKB
- filopodium Source: UniProtKB
- focal adhesion Source: UniProtKB
- Golgi membrane Source: BHF-UCL
- Golgi transport complex Source: CAFA
- leading edge membrane Source: Ensembl
- membrane Source: UniProtKB
- microtubule organizing center Source: UniProtKB-SubCell
- midbody Source: UniProtKB
- mitotic spindle Source: UniProtKB
- myelin sheath Source: Ensembl
- neuronal cell body Source: BHF-UCL
- neuron projection Source: BHF-UCL
- plasma membrane Source: UniProtKB
- secretory granule Source: Ensembl
- spindle midzone Source: UniProtKB
- storage vacuole Source: Ensembl
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Cytoskeleton, MembranePathology & Biotechi
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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_076337 | 64 | Y → C in TKS. 2 PublicationsCorresponds to variant dbSNP:rs864309721Ensembl. | 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 12 | G → V: Constitutively active. Interacts with PARD6 proteins. Does not inhibit filopodia formation. No effect on NR3C2 transcriptional activity. 3 Publications | 1 | |
| Mutagenesisi | 17 | T → N: Constitutively inactive. Does not interact with PARD6 proteins. Inhibits filopodia formation. No effect on NR3C2 transcriptional activity. 3 Publications | 1 | |
| Mutagenesisi | 32 | Y → F: Abolishes AMPylation by Haemophilus IbpA. 1 Publication | 1 | |
| Mutagenesisi | 61 | Q → L: Constitutively active. Interacts with PARD6 proteins. 1 Publication | 1 |
Keywords - Diseasei
Disease mutation, Mental retardationOrganism-specific databases
| DisGeNETi | 998. |
| MalaCardsi | CDC42. |
| MIMi | 616737. phenotype. |
| OpenTargetsi | ENSG00000070831. |
| PharmGKBi | PA26266. |
Chemistry databases
| ChEMBLi | CHEMBL6088. |
| DrugBanki | DB02623. Aminophosphonic Acid-Guanylate Ester. DB04315. Guanosine-5'-Diphosphate. |
Polymorphism and mutation databases
| BioMutai | CDC42. |
| DMDMi | 322510015. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000030425 | 1 – 188 | Cell division control protein 42 homologAdd BLAST | 188 | |
| PropeptideiPRO_0000030426 | 189 – 191 | Removed in mature form | 3 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 32 | O-AMP-tyrosine; by Haemophilus IbpA; alternate2 Publications | 1 | |
| Glycosylationi | 32 | O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate1 Publication | 1 | |
| Modified residuei | 35 | O-AMP-threonine; by Vibrio VopS1 Publication | 1 | |
| Modified residuei | 64 | Phosphotyrosine; by SRC1 Publication | 1 | |
| Modified residuei | 188 | Cysteine methyl esterCombined sources1 Publication | 1 | |
| Lipidationi | 188 | S-geranylgeranyl cysteineCombined sources1 Publication | 1 |
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, PrenylationProteomic databases
| EPDi | P60953. |
| PaxDbi | P60953. |
| PeptideAtlasi | P60953. |
| PRIDEi | P60953. |
| TopDownProteomicsi | P60953-2. [P60953-2] |
PTM databases
| iPTMneti | P60953. |
| PhosphoSitePlusi | P60953. |
| SwissPalmi | P60953. |
Miscellaneous databases
| PMAP-CutDBi | P60953. |
Expressioni
Gene expression databases
| Bgeei | ENSG00000070831. |
| CleanExi | HS_CDC42. |
| ExpressionAtlasi | P60953. baseline and differential. |
| Genevisiblei | P60953. HS. |
Organism-specific databases
| HPAi | CAB004360. |
Interactioni
Subunit structurei
The GTP-bound form interacts with CCPG1 (By similarity). Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4, CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-dependent manner). Interacts with activated CSPG4 and with BAIAP2. Interacts with Zizimin1/DOCK9 and Zizimin2/DOCK11, which activate it by exchanging GDP for GTP. Interacts with NET1 and ARHGAP33/TCGAP. Part of a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ. Interacts with USP6. May interact with ARHGEF16; responsible for the activation of CDC42 by the viral protein HPV16 E6. Interacts with NEK6. Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with ITGB1BP1. Interacts with ARHGDIA; this interaction inactivates and stabilizes CDC42. Interacts with ARHGDIB; this maintains CDC42 in the inactive, GDP-bound form. Interacts in (GTP-bound form) with FNBP1L and ABI1, but only in the presence of FNBP1L (PubMed:19798448).By similarity17 Publications
Binary interactionsi
GO - Molecular functioni
- apolipoprotein A-I receptor binding Source: BHF-UCL
- GBD domain binding Source: CAFA
- GTP-dependent protein binding Source: Ensembl
- identical protein binding Source: IntAct
- mitogen-activated protein kinase kinase kinase binding Source: Ensembl
- protein kinase binding Source: BHF-UCL
- Rho GDP-dissociation inhibitor binding Source: Ensembl
- thioesterase binding Source: UniProtKB
Protein-protein interaction databases
| BioGridi | 107433. 205 interactors. |
| DIPi | DIP-31097N. |
| IntActi | P60953. 181 interactors. |
| MINTi | MINT-94609. |
| STRINGi | 9606.ENSP00000314458. |
Chemistry databases
| BindingDBi | P60953. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Beta strandi | 2 – 11 | Combined sources | 10 | |
| Turni | 12 – 14 | Combined sources | 3 | |
| Helixi | 16 – 25 | Combined sources | 10 | |
| Helixi | 29 – 31 | Combined sources | 3 | |
| Beta strandi | 36 – 46 | Combined sources | 11 | |
| Beta strandi | 49 – 58 | Combined sources | 10 | |
| Helixi | 62 – 64 | Combined sources | 3 | |
| Turni | 65 – 67 | Combined sources | 3 | |
| Helixi | 68 – 71 | Combined sources | 4 | |
| Beta strandi | 72 – 74 | Combined sources | 3 | |
| Beta strandi | 76 – 83 | Combined sources | 8 | |
| Helixi | 87 – 95 | Combined sources | 9 | |
| Helixi | 97 – 104 | Combined sources | 8 | |
| Beta strandi | 105 – 107 | Combined sources | 3 | |
| Beta strandi | 110 – 115 | Combined sources | 6 | |
| Helixi | 117 – 121 | Combined sources | 5 | |
| Helixi | 123 – 130 | Combined sources | 8 | |
| Turni | 131 – 133 | Combined sources | 3 | |
| Helixi | 139 – 148 | Combined sources | 10 | |
| Beta strandi | 154 – 156 | Combined sources | 3 | |
| Turni | 159 – 161 | Combined sources | 3 | |
| Turni | 162 – 164 | Combined sources | 3 | |
| Helixi | 165 – 176 | Combined sources | 12 | |
| Beta strandi | 179 – 181 | Combined sources | 3 | |
| Turni | 184 – 186 | Combined sources | 3 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1A4R | X-ray | 2.50 | A/B | 1-191 | [»] | |
| 1AJE | NMR | - | A | 1-187 | [»] | |
| 1AM4 | X-ray | 2.70 | D/E/F | 2-177 | [»] | |
| 1AN0 | X-ray | 2.80 | A/B | 1-190 | [»] | |
| 1CEE | NMR | - | A | 1-179 | [»] | |
| 1CF4 | NMR | - | A | 1-184 | [»] | |
| 1DOA | X-ray | 2.60 | A | 1-188 | [»] | |
| 1E0A | NMR | - | A | 1-184 | [»] | |
| 1EES | NMR | - | A | 1-178 | [»] | |
| 1GRN | X-ray | 2.10 | A | 1-191 | [»] | |
| 1GZS | X-ray | 2.30 | A/C | 1-178 | [»] | |
| 1KI1 | X-ray | 2.30 | A/C | 1-188 | [»] | |
| 1KZ7 | X-ray | 2.40 | B/D | 1-188 | [»] | |
| 1KZG | X-ray | 2.60 | B/D | 1-188 | [»] | |
| 1NF3 | X-ray | 2.10 | A/B | 2-191 | [»] | |
| 2ASE | NMR | - | A | 1-178 | [»] | |
| 2DFK | X-ray | 2.15 | B/D | 1-191 | [»] | |
| 2KB0 | NMR | - | A | 1-178 | [»] | |
| 2NGR | X-ray | 1.90 | A | 1-191 | [»] | |
| 2ODB | X-ray | 2.40 | A | 1-181 | [»] | |
| 2QRZ | X-ray | 2.40 | A/B | 1-189 | [»] | |
| 2WM9 | X-ray | 2.20 | B | 1-188 | [»] | |
| 2WMN | X-ray | 2.39 | B | 1-188 | [»] | |
| 2WMO | X-ray | 2.20 | B | 1-188 | [»] | |
| 3GCG | X-ray | 2.30 | A | 2-178 | [»] | |
| 3QBV | X-ray | 2.65 | A/C | 1-178 | [»] | |
| 3VHL | X-ray | 2.08 | B | 1-188 | [»] | |
| 4DID | X-ray | 2.35 | A | 1-183 | [»] | |
| 4ITR | X-ray | 2.30 | C/D | 1-191 | [»] | |
| 4JS0 | X-ray | 1.90 | A | 1-178 | [»] | |
| 4YC7 | X-ray | 2.50 | A | 1-179 | [»] | |
| 4YDH | X-ray | 3.80 | B/D | 1-179 | [»] | |
| 5CJP | X-ray | 2.60 | A/B/C/D | 1-177 | [»] | |
| 5FI1 | X-ray | 3.20 | B | 1-191 | [»] | |
| 5HZK | X-ray | 3.30 | A/C | 1-181 | [»] | |
| ProteinModelPortali | P60953. | |||||
| SMRi | P60953. | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | P60953. |
Family & Domainsi
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Motifi | 32 – 40 | Effector regionSequence analysis | 9 |
Sequence similaritiesi
Phylogenomic databases
| eggNOGi | KOG0393. Eukaryota. COG1100. LUCA. |
| GeneTreei | ENSGT00760000118978. |
| HOGENOMi | HOG000233974. |
| HOVERGENi | HBG009351. |
| InParanoidi | P60953. |
| KOi | K04393. |
| OMAi | MQTLKCV. |
| OrthoDBi | EOG091G0KCM. |
| PhylomeDBi | P60953. |
| TreeFami | TF101109. |
Family and domain databases
| InterProi | View protein in InterPro IPR027417. P-loop_NTPase. IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003578. Small_GTPase_Rho. |
| Pfami | View protein in Pfam PF00071. Ras. 1 hit. |
| SUPFAMi | SSF52540. SSF52540. 1 hit. |
| TIGRFAMsi | TIGR00231. small_GTP. 1 hit. |
| PROSITEi | View protein in PROSITE PS51420. RHO. 1 hit. |
Sequences (2)i
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket
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.
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
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_076337 | 64 | Y → C in TKS. 2 PublicationsCorresponds to variant dbSNP:rs864309721Ensembl. | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Alternative sequenceiVSP_040583 | 163 | K → R in isoform 1. 3 Publications | 1 | |
| Alternative sequenceiVSP_040584 | 182 – 191 | PKKSRRCVLL → TQPKRKCCIF in isoform 1. 3 Publications | 10 |
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. Translation: CAB52602.1. AL031281 Genomic DNA. Translation: CAD92551.1. BC002711 mRNA. Translation: AAH02711.1. BC003682 mRNA. Translation: AAH03682.1. BC018266 mRNA. Translation: AAH18266.1. |
| CCDSi | CCDS221.1. CCDS222.1. [P60953-1] |
| PIRi | A36382. A39265. |
| 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] |
| UniGenei | Hs.467637. |
Genome annotation databases
| Ensembli | ENST00000315554; ENSP00000314458; ENSG00000070831. [P60953-1] ENST00000344548; ENSP00000341072; ENSG00000070831. [P60953-2] ENST00000400259; ENSP00000383118; ENSG00000070831. [P60953-2] |
| GeneIDi | 998. |
| KEGGi | hsa:998. |
| UCSCi | uc001bfp.4. human. |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:| 100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry. |
| 90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
| 50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |
Entry informationi
| Entry namei | CDC42_HUMAN | |
| Accessioni | P60953Primary (citable) accession number: P60953 Secondary accession number(s): P21181 Q9UDI2 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 13, 2004 |
| Last sequence update: | February 8, 2011 | |
| Last modified: | June 7, 2017 | |
| This is version 175 of the entry and version 2 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
