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P60953

- CDC42_HUMAN

UniProt

P60953 - CDC42_HUMAN

Protein

Cell division control protein 42 homolog

Gene

CDC42

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (08 Feb 2011)
      Previous versions | rss
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    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.3 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 178GTP
    Nucleotide bindingi57 – 615GTPBy similarity
    Nucleotide bindingi115 – 1184GTP

    GO - Molecular functioni

    1. apolipoprotein A-I receptor binding Source: BHF-UCL
    2. GTPase activity Source: UniProtKB
    3. GTP binding Source: MGI
    4. identical protein binding Source: IntAct
    5. protein binding Source: IntAct
    6. protein kinase binding Source: BHF-UCL
    7. thioesterase binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. actin filament branching Source: Ensembl
    3. actin filament bundle assembly Source: Ensembl
    4. adherens junction organization Source: Ensembl
    5. axon guidance Source: Reactome
    6. blood coagulation Source: Reactome
    7. canonical Wnt signaling pathway Source: Ensembl
    8. cardiac conduction system development Source: Ensembl
    9. cellular protein localization Source: Ensembl
    10. epidermal growth factor receptor signaling pathway Source: Reactome
    11. epithelial cell-cell adhesion Source: Ensembl
    12. epithelial-mesenchymal cell signaling Source: Ensembl
    13. establishment of Golgi localization Source: BHF-UCL
    14. establishment or maintenance of apical/basal cell polarity Source: Ensembl
    15. establishment or maintenance of cell polarity Source: UniProtKB
    16. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    17. filopodium assembly Source: Ensembl
    18. Golgi organization Source: BHF-UCL
    19. GTP catabolic process Source: GOC
    20. hair follicle morphogenesis Source: Ensembl
    21. hair follicle placode formation Source: Ensembl
    22. heart contraction Source: Ensembl
    23. innate immune response Source: Reactome
    24. keratinization Source: Ensembl
    25. keratinocyte development Source: Ensembl
    26. macrophage differentiation Source: UniProtKB
    27. multicellular organism growth Source: Ensembl
    28. muscle cell differentiation Source: Reactome
    29. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    30. negative regulation of gene expression Source: Ensembl
    31. negative regulation of protein complex assembly Source: UniProtKB
    32. neuron fate determination Source: Ensembl
    33. nuclear migration Source: Ensembl
    34. organelle transport along microtubule Source: BHF-UCL
    35. positive regulation of cytokinesis Source: UniProtKB
    36. positive regulation of DNA replication Source: Ensembl
    37. positive regulation of gene expression Source: Ensembl
    38. positive regulation of hair follicle cell proliferation Source: Ensembl
    39. positive regulation of intracellular protein transport Source: Ensembl
    40. positive regulation of JNK cascade Source: Ensembl
    41. positive regulation of metalloenzyme activity Source: Ensembl
    42. positive regulation of muscle cell differentiation Source: Reactome
    43. positive regulation of neuron apoptotic process Source: Ensembl
    44. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
    45. positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
    46. positive regulation of pseudopodium assembly Source: UniProtKB
    47. positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
    48. positive regulation of synapse structural plasticity Source: Ensembl
    49. regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
    50. regulation of filopodium assembly Source: UniProtKB
    51. regulation of mitosis Source: Ensembl
    52. regulation of protein catabolic process Source: Ensembl
    53. regulation of protein heterodimerization activity Source: Ensembl
    54. regulation of protein kinase activity Source: Ensembl
    55. regulation of protein stability Source: Ensembl
    56. regulation of small GTPase mediated signal transduction Source: Reactome
    57. small GTPase mediated signal transduction Source: Reactome
    58. sprouting angiogenesis Source: Ensembl
    59. submandibular salivary gland formation Source: Ensembl
    60. substantia nigra development Source: UniProt
    61. T cell costimulation Source: Reactome

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_12484. EGFR downregulation.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19238. CD28 dependent Vav1 pathway.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    REACT_19342. Inactivation of Cdc42 and Rac.
    REACT_21402. CDO in myogenesis.
    REACT_22351. DCC mediated attractive signaling.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    SignaLinkiP60953.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division control protein 42 homolog
    Alternative name(s):
    G25K GTP-binding protein
    Gene namesi
    Name:CDC42
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1736. CDC42.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. 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

    1. apical part of cell Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. filopodium Source: UniProtKB
    7. Golgi membrane Source: BHF-UCL
    8. membrane Source: UniProtKB
    9. microtubule organizing center Source: UniProtKB-SubCell
    10. midbody Source: UniProtKB
    11. mitotic spindle Source: UniProtKB
    12. neuronal cell body Source: BHF-UCL
    13. neuron projection Source: BHF-UCL
    14. plasma membrane Source: UniProtKB
    15. secretory granule Source: Ensembl
    16. spindle midzone Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121G → V: Constitutively active. Interacts with PARD6 proteins. Does not inhibit filopodia formation. No effect on NR3C2 transcriptional activity. 3 Publications
    Mutagenesisi17 – 171T → N: Constitutively inactive. Does not interact with PARD6 proteins. Inhibits filopodia formation. No effect on NR3C2 transcriptional activity. 3 Publications
    Mutagenesisi32 – 321Y → F: Abolishes AMPylation by Haemophilus IbpA. 1 Publication
    Mutagenesisi61 – 611Q → L: Constitutively active. Interacts with PARD6 proteins. 1 Publication

    Organism-specific databases

    PharmGKBiPA26266.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 188188Cell division control protein 42 homologPRO_0000030425Add
    BLAST
    Propeptidei189 – 1913Removed in mature formPRO_0000030426

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321O-AMP-tyrosine; by Haemophilus IbpA2 Publications
    Modified residuei35 – 351O-AMP-threonine; by Vibrio VopS1 Publication
    Modified residuei64 – 641Phosphotyrosine; by SRC1 Publication
    Modified residuei188 – 1881Cysteine methyl esterBy similarity
    Lipidationi188 – 1881S-geranylgeranyl cysteineBy similarity

    Post-translational modificationi

    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

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP60953.
    PaxDbiP60953.
    PRIDEiP60953.

    PTM databases

    PhosphoSiteiP60953.

    Miscellaneous databases

    PMAP-CutDBP60953.

    Expressioni

    Gene expression databases

    ArrayExpressiP60953.
    BgeeiP60953.
    CleanExiHS_CDC42.
    GenevestigatoriP60953.

    Organism-specific databases

    HPAiCAB004360.

    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.By similarity15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-81752,EBI-81752
    ABCA1O954772EBI-81752,EBI-784112
    ARHGAP1Q079602EBI-287394,EBI-602762
    BAIAP2Q9UQB82EBI-287394,EBI-525456
    BAIAP2Q9UQB8-44EBI-81752,EBI-6174091
    Bin1Q9VEX92EBI-81752,EBI-129424From a different organism.
    CDC42BPAQ5VT255EBI-81752,EBI-689171
    CDC42EP1Q005873EBI-81752,EBI-744130
    IQGAP1P469402EBI-81752,EBI-297509
    ITSN1Q158112EBI-3625591,EBI-602041
    LRRK2Q5S0073EBI-81752,EBI-5323863
    MAP3K11Q165843EBI-81752,EBI-49961
    MARK4Q96L342EBI-81752,EBI-302319
    Mcf2lQ640963EBI-287394,EBI-602123From a different organism.
    PAK1Q131537EBI-81752,EBI-1307
    PAK3O759142EBI-287394,EBI-3389553
    Pak3Q610363EBI-81752,EBI-457317From a different organism.
    PAK4O960132EBI-81752,EBI-713738
    PARD6AQ9NPB67EBI-81752,EBI-81876
    PARD6BQ9BYG57EBI-81752,EBI-295391
    Pard6bQ9JK836EBI-81752,EBI-81861From a different organism.
    PARD6GQ9BYG45EBI-81752,EBI-295417
    PRKCIP417435EBI-81752,EBI-286199
    sopEO526232EBI-81752,EBI-602254From a different organism.
    TNK2Q079122EBI-287394,EBI-603457
    WASP4276810EBI-81752,EBI-346375
    WASLO004013EBI-81752,EBI-957615
    WaslO088162EBI-81752,EBI-6142604From a different organism.

    Protein-protein interaction databases

    BioGridi107433. 141 interactions.
    DIPiDIP-31097N.
    IntActiP60953. 120 interactions.
    MINTiMINT-94609.
    STRINGi9606.ENSP00000314458.

    Structurei

    Secondary structure

    1
    191
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 1110
    Turni12 – 143
    Helixi16 – 2510
    Helixi29 – 313
    Beta strandi36 – 4611
    Beta strandi49 – 5810
    Helixi62 – 643
    Turni65 – 673
    Helixi68 – 714
    Beta strandi72 – 743
    Beta strandi76 – 838
    Helixi87 – 959
    Helixi97 – 1048
    Beta strandi105 – 1073
    Beta strandi110 – 1156
    Helixi117 – 1215
    Helixi123 – 1308
    Turni131 – 1333
    Helixi139 – 14810
    Beta strandi154 – 1563
    Turni159 – 1613
    Turni162 – 1643
    Helixi165 – 17612
    Beta strandi179 – 1813
    Turni184 – 1863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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-ray2.40A1-181[»]
    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[»]
    ProteinModelPortaliP60953.
    SMRiP60953. Positions 1-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60953.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi32 – 409Effector regionSequence Analysis

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    KOiK04393.
    OMAiTPDQGER.
    PhylomeDBiP60953.
    TreeFamiTF101109.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00174. RHO. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51420. RHO. 1 hit.
    [Graphical view]

    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. Align

    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

    MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP    50
    YTLGLFDTAG QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE 100
    ITHHCPKTPF LLVGTQIDLR DDPSTIEKLA KNKQKPITPE TAEKLARDLK 150
    AVKYVECSAL TQKGLKNVFD EAILAALEPP EPKKSRRCVL L 191
    Length:191
    Mass (Da):21,259
    Last modified:February 8, 2011 - v2
    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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei163 – 1631K → R in isoform 1. 3 PublicationsVSP_040583
    Alternative sequencei182 – 19110PKKSRRCVLL → TQPKRKCCIF in isoform 1. 3 PublicationsVSP_040584

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    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.

    Genome annotation databases

    EnsembliENST00000315554; ENSP00000314458; ENSG00000070831. [P60953-1]
    ENST00000344548; ENSP00000341072; ENSG00000070831. [P60953-2]
    ENST00000400259; ENSP00000383118; ENSG00000070831. [P60953-2]
    GeneIDi998.
    KEGGihsa:998.
    UCSCiuc001bfp.3. human. [P60953-1]
    uc001bfq.3. human.

    Polymorphism databases

    DMDMi322510015.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P60953.
    SMRi P60953. Positions 1-191.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107433. 141 interactions.
    DIPi DIP-31097N.
    IntActi P60953. 120 interactions.
    MINTi MINT-94609.
    STRINGi 9606.ENSP00000314458.

    Chemistry

    BindingDBi P60953.
    ChEMBLi CHEMBL6088.

    PTM databases

    PhosphoSitei P60953.

    Polymorphism databases

    DMDMi 322510015.

    Proteomic databases

    MaxQBi P60953.
    PaxDbi P60953.
    PRIDEi P60953.

    Protocols and materials databases

    DNASUi 998.
    Structural Biology Knowledgebase Search...

    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.3. human. [P60953-1 ]
    uc001bfq.3. human.

    Organism-specific databases

    CTDi 998.
    GeneCardsi GC01P022379.
    HGNCi HGNC:1736. CDC42.
    HPAi CAB004360.
    MIMi 116952. gene.
    neXtProti NX_P60953.
    PharmGKBi PA26266.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    KOi K04393.
    OMAi TPDQGER.
    PhylomeDBi P60953.
    TreeFami TF101109.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_12484. EGFR downregulation.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19238. CD28 dependent Vav1 pathway.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    REACT_19342. Inactivation of Cdc42 and Rac.
    REACT_21402. CDO in myogenesis.
    REACT_22351. DCC mediated attractive signaling.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    SignaLinki P60953.

    Miscellaneous databases

    ChiTaRSi CDC42. human.
    EvolutionaryTracei P60953.
    GeneWikii CDC42.
    GenomeRNAii 998.
    NextBioi 4192.
    PMAP-CutDB P60953.
    PROi P60953.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P60953.
    Bgeei P60953.
    CleanExi HS_CDC42.
    Genevestigatori P60953.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00174. RHO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51420. RHO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42."
      Munemitsu S., Innis M.A., Clark R., McCormick F., Ullrich A., Polakis P.
      Mol. Cell. Biol. 10:5977-5982(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42."
      Shinjo K., Koland J.G., Hart M.J., Narasimhan V., Johnson D.I., Evans T., Cerione R.A.
      Proc. Natl. Acad. Sci. U.S.A. 87:9853-9857(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Placenta.
    3. Rhodes S., Huckle E.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    4. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain and Placenta.
    5. NIEHS SNPs program
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Cervix, Placenta and Uterus.
    8. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 67-83 (ISOFORM 2), PARTIAL PROTEIN SEQUENCE (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    9. "Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins."
      Kwong C.H., Malech H.L., Rotrosen D., Leto T.L.
      Biochemistry 32:5711-5717(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 97-107; 134-144 AND 167-183 (ISOFORM 2).
      Tissue: Neutrophil.
    10. "Characterization of G25K, a GTP-binding protein containing a novel putative nucleotide binding domain."
      Polakis P.G., Snyderman R., Evans T.
      Biochem. Biophys. Res. Commun. 160:25-32(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    11. "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins."
      Joberty G., Perlungher R.R., Macara I.G.
      Mol. Cell. Biol. 19:6585-6597(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC42EP1; CDC42EP2; CDC42EP3 AND CDC42EP5.
      Tissue: Embryo.
    12. "Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas."
      Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L., Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.
      Nat. Cell Biol. 1:507-513(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSPG4.
    13. Cited for: INTERACTION WITH CDC42SE1 AND CDC42SE2.
    14. "The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1."
      Johansson A.-S., Driessens M., Aspenstroem P.
      J. Cell Sci. 113:3267-3275(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARD6A, MUTAGENESIS OF GLY-12.
    15. "IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling."
      Miki H., Yamaguchi H., Suetsugu S., Takenawa T.
      Nature 408:732-735(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BAIAP2.
    16. "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C."
      Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.
      Genes Cells 6:107-119(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G, SUBUNIT OF A COMPLEX CONTAINING PRKCI AND PARD6B, MUTAGENESIS OF THR-17 AND GLN-61.
    17. "The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading."
      Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L., Eva A., Tarone G.
      J. Cell Biol. 156:377-387(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB1BP1.
    18. "Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins."
      Meller N., Irani-Tehrani M., Kiosses W.B., Del Pozo M.A., Schwartz M.A.
      Nat. Cell Biol. 4:639-647(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOCK9, ACTIVATION BY DOCK9.
    19. "Epidermal growth factor-dependent regulation of Cdc42 is mediated by the Src tyrosine kinase."
      Tu S., Wu W.J., Wang J., Cerione R.A.
      J. Biol. Chem. 278:49293-49300(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-64 BY SRC.
    20. "The TRE17 oncogene encodes a component of a novel effector pathway for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling."
      Masuda-Robens J.M., Kutney S.N., Qi H., Chou M.M.
      Mol. Cell. Biol. 23:2151-2161(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP6.
    21. "Regulation of dendritic branching and filopodia formation in hippocampal neurons by specific acylated protein motifs."
      Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.
      Mol. Biol. Cell 15:2205-2217(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-12 AND THR-17.
    22. "Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis."
      Oceguera-Yanez F., Kimura K., Yasuda S., Higashida C., Kitamura T., Hiraoka Y., Haraguchi T., Narumiya S.
      J. Cell Biol. 168:221-232(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    23. "Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas."
      Modzelewska K., Newman L.P., Desai R., Keely P.J.
      J. Biol. Chem. 281:37527-37535(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH BCAR1; TNK2 AND CRK.
    24. "Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease."
      Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H., Miyoshi J., Takai Y., Fujita T.
      Nat. Med. 14:1370-1376(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-12 AND THR-17.
    25. Cited for: AMPYLATION AT TYR-32, MUTAGENESIS OF TYR-32.
    26. "AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling."
      Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.
      Science 323:269-272(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: AMPYLATION AT THR-35.
    27. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
      Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
      J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which activates Cdc42."
      Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L., Hampson I.N.
      Br. J. Cancer 104:324-331(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGEF16.
    30. Cited for: INTERACTION WITH ARHGDIA.
    31. "Definition of the switch surface in the solution structure of Cdc42Hs."
      Feltham J.L., Dotsch V., Raza S., Manor D., Cerione R.A., Sutcliffe M.J., Wagner G., Oswald R.E.
      Biochemistry 36:8755-8766(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    32. "Identification of the binding surface on Cdc42Hs for p21-activated kinase."
      Guo W., Sutcliffe M.J., Cerione R.A., Oswald R.E.
      Biochemistry 37:14030-14037(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    33. "Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP."
      Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D., Laue E., Gamblin S.J., Smerdon S.J.
      Nature 388:693-697(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH RHOGAP.
    34. "Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: two different nucleotide states in one crystal."
      Rudolph M.G., Wittinghofer A., Vetter I.R.
      Protein Sci. 8:778-787(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF VAL-12 MUTANT.
    35. "The structure determination of CDC42Hs and GDP complex."
      Kongsaeree P., Cerione R.A., Clardy J.C.
      Submitted (JUN-1997) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    36. "Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor."
      Yang J., Zhang Z., Roe S.M., Marshall C.J., Barford D.
      Science 325:1398-1402(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-188 IN COMPLEX WITH DOCK9.
    37. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-181 IN COMPLEX WITH H.SOMNUS IBPA AND GDP, AMPYLATION AT TYR-32.

    Entry informationi

    Entry nameiCDC42_HUMAN
    AccessioniPrimary (citable) accession number: P60953
    Secondary accession number(s): P21181
    , P25763, Q7L8R5, Q9UDI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 145 of the entry and version 2 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3