Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P60766

- CDC42_MOUSE

UniProt

P60766 - CDC42_MOUSE

Protein

Cell division control protein 42 homolog

Gene

Cdc42

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (08 Feb 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    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 – 178GTPBy similarity
    Nucleotide bindingi57 – 615GTPBy similarity
    Nucleotide bindingi115 – 1184GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: MGI
    2. GTP binding Source: MGI
    3. GTP-dependent protein binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase binding Source: BHF-UCL

    GO - Biological processi

    1. actin filament branching Source: Ensembl
    2. actin filament bundle assembly Source: MGI
    3. adherens junction organization Source: MGI
    4. canonical Wnt signaling pathway Source: MGI
    5. cardiac conduction system development Source: MGI
    6. cellular protein localization Source: MGI
    7. dendritic cell migration Source: MGI
    8. endosomal transport Source: UniProtKB
    9. epidermis morphogenesis Source: MGI
    10. epithelial cell-cell adhesion Source: MGI
    11. epithelial-mesenchymal cell signaling Source: MGI
    12. establishment of Golgi localization Source: Ensembl
    13. establishment or maintenance of apical/basal cell polarity Source: MGI
    14. establishment or maintenance of cell polarity Source: UniProtKB
    15. filopodium assembly Source: MGI
    16. Golgi organization Source: Ensembl
    17. GTP catabolic process Source: GOC
    18. hair follicle morphogenesis Source: MGI
    19. hair follicle placode formation Source: MGI
    20. heart contraction Source: MGI
    21. keratinization Source: MGI
    22. keratinocyte development Source: MGI
    23. multicellular organism growth Source: MGI
    24. negative regulation of gene expression Source: MGI
    25. negative regulation of protein complex assembly Source: Ensembl
    26. neuron fate determination Source: MGI
    27. nuclear migration Source: MGI
    28. nucleus localization Source: MGI
    29. organelle transport along microtubule Source: Ensembl
    30. positive regulation of cytokinesis Source: UniProtKB
    31. positive regulation of DNA replication Source: Ensembl
    32. positive regulation of gene expression Source: MGI
    33. positive regulation of hair follicle cell proliferation Source: MGI
    34. positive regulation of intracellular protein transport Source: Ensembl
    35. positive regulation of JNK cascade Source: Ensembl
    36. positive regulation of MAPK cascade Source: MGI
    37. positive regulation of metalloenzyme activity Source: Ensembl
    38. positive regulation of neuron apoptotic process Source: Ensembl
    39. positive regulation of peptidyl-serine phosphorylation Source: MGI
    40. positive regulation of phosphatidylinositol 3-kinase activity Source: MGI
    41. positive regulation of protein phosphorylation Source: MGI
    42. positive regulation of pseudopodium assembly Source: Ensembl
    43. positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
    44. positive regulation of synapse structural plasticity Source: Ensembl
    45. regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
    46. regulation of filopodium assembly Source: UniProtKB
    47. regulation of mitosis Source: MGI
    48. regulation of protein catabolic process Source: MGI
    49. regulation of protein heterodimerization activity Source: MGI
    50. regulation of protein kinase activity Source: MGI
    51. regulation of protein metabolic process Source: MGI
    52. regulation of protein stability Source: MGI
    53. Rho protein signal transduction Source: MGI
    54. single organismal cell-cell adhesion Source: UniProtKB
    55. sprouting angiogenesis Source: Ensembl
    56. submandibular salivary gland formation Source: Ensembl

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_203917. EGFR downregulation.
    REACT_210090. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell division control protein 42 homolog
    Alternative name(s):
    G25K GTP-binding protein
    Gene namesi
    Name:Cdc42
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:106211. Cdc42.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Midbody By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
    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 By similarity.By similarity

    GO - Cellular componenti

    1. apical part of cell Source: MGI
    2. cell-cell junction Source: MGI
    3. cell periphery Source: MGI
    4. cell projection Source: MGI
    5. cytoplasm Source: MGI
    6. cytosol Source: Reactome
    7. filopodium Source: Ensembl
    8. Golgi membrane Source: Ensembl
    9. leading edge membrane Source: MGI
    10. membrane Source: UniProtKB
    11. microtubule organizing center Source: UniProtKB-SubCell
    12. midbody Source: UniProtKB
    13. mitotic spindle Source: UniProtKB
    14. neuronal cell body Source: Ensembl
    15. neuron projection Source: Ensembl
    16. secretory granule Source: Ensembl
    17. spindle midzone Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171T → N: Constitutively inactivated. Abolishes interaction with PARD6 and DOCK11. 2 Publications
    Mutagenesisi61 – 611Q → L: Constitutively activated. Enhances interaction with DOCK11. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 188188Cell division control protein 42 homologPRO_0000030427Add
    BLAST
    Propeptidei189 – 1913Removed in mature formBy similarityPRO_0000030428

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei64 – 641Phosphotyrosine; by SRCBy similarity
    Modified residuei188 – 1881Cysteine methyl esterBy similarity
    Lipidationi188 – 1881S-geranylgeranyl cysteineBy similarity

    Post-translational modificationi

    Phosphorylated by SRC in an EGF-dependent manner, this stimulates the binding of the Rho-GDP dissociation inhibitor RhoGDI.By similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP60766.
    PaxDbiP60766.
    PRIDEiP60766.

    PTM databases

    PhosphoSiteiP60766.

    Expressioni

    Gene expression databases

    ArrayExpressiP60766.
    BgeeiP60766.
    CleanExiMM_CDC42.
    GenevestigatoriP60766.

    Interactioni

    Subunit structurei

    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. The GTP-bound form interacts with CCPG1. Interacts with USP6 By similarity. Interacts with NEK6 By similarity. Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with ITGB1BP1 By similarity. Interacts with ARHGDIA; this interaction inactivates and stabilizes CDC42 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PAK1Q131533EBI-81763,EBI-1307From a different organism.
    Vamp2P630442EBI-81763,EBI-521920

    Protein-protein interaction databases

    BioGridi198627. 16 interactions.
    DIPiDIP-32554N.
    IntActiP60766. 15 interactions.
    MINTiMINT-1602743.

    Structurei

    Secondary structure

    1
    191
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi16 – 2510
    Beta strandi36 – 4611
    Beta strandi49 – 5810
    Helixi62 – 643
    Turni65 – 673
    Helixi68 – 714
    Beta strandi76 – 838
    Helixi87 – 959
    Helixi97 – 1048
    Beta strandi110 – 1156
    Helixi117 – 1193
    Helixi123 – 1319
    Helixi139 – 14810
    Beta strandi154 – 1563
    Turni159 – 1613
    Helixi165 – 17713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EG5X-ray2.70A/C1-178[»]
    ProteinModelPortaliP60766.
    SMRiP60766. Positions 1-191.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60766.

    Family & Domainsi

    Motif

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1100.
    GeneTreeiENSGT00720000108634.
    HOVERGENiHBG009351.
    KOiK04393.
    OMAiVITIDQG.
    OrthoDBiEOG764747.
    PhylomeDBiP60766.
    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: P60766-2) [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: P60766-1) [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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261N → D in BAC34669. (PubMed:16141072)Curated
    Sequence conflicti66 – 661R → G in AAH64792. (PubMed:15489334)Curated
    Sequence conflicti85 – 851V → I in BAE39489. (PubMed:16141072)Curated
    Sequence conflicti116 – 1161Q → K in BAE40049. (PubMed:16141072)Curated
    Sequence conflicti171 – 1711E → G in AAH64792. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei163 – 1631K → R in isoform 1. CuratedVSP_040585
    Alternative sequencei182 – 19110PKKSRRCVLL → TQPKRKCCIF in isoform 1. CuratedVSP_040586

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11318 mRNA. Translation: AAA37410.1.
    U37720 mRNA. Translation: AAC00028.1.
    L78075 Genomic DNA. Translation: AAB40051.1.
    AK003098 mRNA. Translation: BAB22563.1.
    AK051543 mRNA. Translation: BAC34669.1.
    AK075567 mRNA. Translation: BAC35825.1.
    AK144216 mRNA. Translation: BAE25778.1.
    AK151087 mRNA. Translation: BAE30100.1.
    AK151726 mRNA. Translation: BAE30644.1.
    AK153564 mRNA. Translation: BAE32098.1.
    AK154870 mRNA. Translation: BAE32891.1.
    AK159470 mRNA. Translation: BAE35111.1.
    AK166281 mRNA. Translation: BAE38678.1.
    AK167195 mRNA. Translation: BAE39325.1.
    AK167400 mRNA. Translation: BAE39489.1.
    AK167609 mRNA. Translation: BAE39663.1.
    AK168013 mRNA. Translation: BAE40000.1.
    AK168076 mRNA. Translation: BAE40049.1.
    AK168089 mRNA. Translation: BAE40062.1.
    AK168276 mRNA. Translation: BAE40222.1.
    AK168758 mRNA. Translation: BAE40595.1.
    AK168820 mRNA. Translation: BAE40647.1.
    AK169122 mRNA. Translation: BAE40902.1.
    AK169232 mRNA. Translation: BAE41001.1.
    AK169805 mRNA. Translation: BAE41379.1.
    AL645468 Genomic DNA. Translation: CAM18513.1.
    AL645468 Genomic DNA. Translation: CAM18514.1.
    BC064792 mRNA. Translation: AAH64792.1.
    CCDSiCCDS18816.1.
    CCDS57305.1. [P60766-1]
    RefSeqiNP_001230698.1. NM_001243769.1. [P60766-1]
    NP_033991.1. NM_009861.3. [P60766-2]
    UniGeneiMm.1022.
    Mm.447553.

    Genome annotation databases

    EnsembliENSMUST00000030417; ENSMUSP00000030417; ENSMUSG00000006699. [P60766-1]
    ENSMUST00000051477; ENSMUSP00000054634; ENSMUSG00000006699. [P60766-2]
    GeneIDi12540.
    KEGGimmu:12540.
    UCSCiuc008viw.3. mouse.
    uc008viy.2. mouse. [P60766-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11318 mRNA. Translation: AAA37410.1 .
    U37720 mRNA. Translation: AAC00028.1 .
    L78075 Genomic DNA. Translation: AAB40051.1 .
    AK003098 mRNA. Translation: BAB22563.1 .
    AK051543 mRNA. Translation: BAC34669.1 .
    AK075567 mRNA. Translation: BAC35825.1 .
    AK144216 mRNA. Translation: BAE25778.1 .
    AK151087 mRNA. Translation: BAE30100.1 .
    AK151726 mRNA. Translation: BAE30644.1 .
    AK153564 mRNA. Translation: BAE32098.1 .
    AK154870 mRNA. Translation: BAE32891.1 .
    AK159470 mRNA. Translation: BAE35111.1 .
    AK166281 mRNA. Translation: BAE38678.1 .
    AK167195 mRNA. Translation: BAE39325.1 .
    AK167400 mRNA. Translation: BAE39489.1 .
    AK167609 mRNA. Translation: BAE39663.1 .
    AK168013 mRNA. Translation: BAE40000.1 .
    AK168076 mRNA. Translation: BAE40049.1 .
    AK168089 mRNA. Translation: BAE40062.1 .
    AK168276 mRNA. Translation: BAE40222.1 .
    AK168758 mRNA. Translation: BAE40595.1 .
    AK168820 mRNA. Translation: BAE40647.1 .
    AK169122 mRNA. Translation: BAE40902.1 .
    AK169232 mRNA. Translation: BAE41001.1 .
    AK169805 mRNA. Translation: BAE41379.1 .
    AL645468 Genomic DNA. Translation: CAM18513.1 .
    AL645468 Genomic DNA. Translation: CAM18514.1 .
    BC064792 mRNA. Translation: AAH64792.1 .
    CCDSi CCDS18816.1.
    CCDS57305.1. [P60766-1 ]
    RefSeqi NP_001230698.1. NM_001243769.1. [P60766-1 ]
    NP_033991.1. NM_009861.3. [P60766-2 ]
    UniGenei Mm.1022.
    Mm.447553.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EG5 X-ray 2.70 A/C 1-178 [» ]
    ProteinModelPortali P60766.
    SMRi P60766. Positions 1-191.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198627. 16 interactions.
    DIPi DIP-32554N.
    IntActi P60766. 15 interactions.
    MINTi MINT-1602743.

    Chemistry

    BindingDBi P60766.

    PTM databases

    PhosphoSitei P60766.

    Proteomic databases

    MaxQBi P60766.
    PaxDbi P60766.
    PRIDEi P60766.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030417 ; ENSMUSP00000030417 ; ENSMUSG00000006699 . [P60766-1 ]
    ENSMUST00000051477 ; ENSMUSP00000054634 ; ENSMUSG00000006699 . [P60766-2 ]
    GeneIDi 12540.
    KEGGi mmu:12540.
    UCSCi uc008viw.3. mouse.
    uc008viy.2. mouse. [P60766-1 ]

    Organism-specific databases

    CTDi 998.
    MGIi MGI:106211. Cdc42.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00720000108634.
    HOVERGENi HBG009351.
    KOi K04393.
    OMAi VITIDQG.
    OrthoDBi EOG764747.
    PhylomeDBi P60766.
    TreeFami TF101109.

    Enzyme and pathway databases

    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_203917. EGFR downregulation.
    REACT_210090. Rho GTPase cycle.

    Miscellaneous databases

    ChiTaRSi CDC42. mouse.
    EvolutionaryTracei P60766.
    NextBioi 281582.
    PROi P60766.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P60766.
    Bgeei P60766.
    CleanExi MM_CDC42.
    Genevestigatori P60766.

    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. "Oncogene ect2 is related to regulators of small GTP-binding proteins."
      Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.
      Nature 362:462-465(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Complete cDNAs for CDC42 from chicken cochlea and mouse liver."
      Gong T.W., Shin J.J., Burmeister M., Lomax M.I.
      Biochim. Biophys. Acta 1352:282-292(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Liver.
    3. "Genomic organization and chromosomal location of murine Cdc42."
      Marks P.W., Kwiatkowski D.J.
      Genomics 38:13-18(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: BALB/c, C57BL/6J, DBA/2 and NOD.
      Tissue: Amnion, Bone marrow, Heart, Kidney, Liver, Mammary gland, Placenta, Spinal ganglion and Thymus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "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).
      Strain: C57BL/6J.
      Tissue: Embryonic germ cell.
    7. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 108-120, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    8. "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 CDC42EP4.
    9. "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
      Joberty G., Petersen C., Gao L., Macara I.G.
      Nat. Cell Biol. 2:531-539(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT OF A COMPLEX CONTAINING PARD6B; PARD3 AND PRKCZ, MUTAGENESIS OF THR-17.
    10. "Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7."
      Alberts A.S., Bouquin N., Johnston L.H., Treisman R.
      J. Biol. Chem. 273:8616-8622(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NET1.
    11. "TCGAP, a multidomain Rho GTPase-activating protein involved in insulin-stimulated glucose transport."
      Chiang S.-H., Hwang J., Legendre M., Zhang M., Kimura A., Saltiel A.R.
      EMBO J. 22:2679-2691(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGAP33/TCGAP.
    12. "Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange factor expressed predominantly in lymphocytes."
      Nishikimi A., Meller N., Uekawa N., Isobe K., Schwartz M.A., Maruyama M.
      FEBS Lett. 579:1039-1046(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOCK11.
    13. "Identification of a DOCK180-related guanine nucleotide exchange factor that is capable of mediating a positive feedback activation of Cdc42."
      Lin Q., Yang W., Baird D., Feng Q., Cerione R.A.
      J. Biol. Chem. 281:35253-35262(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOCK11 AND IQGAP1, MUTAGENESIS OF THR-17 AND GLN-61.
    14. "Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
      Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
      Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CCPG1.

    Entry informationi

    Entry nameiCDC42_MOUSE
    AccessioniPrimary (citable) accession number: P60766
    Secondary accession number(s): A2A9U6
    , P21181, P25763, Q3THZ7, Q3TJK6, Q545V0, Q6P201, Q8BQ51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3