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Protein

Cell division control protein 42 homolog

Gene

Cdc42

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 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. endocytosis Source: MGI
  9. endosomal transport Source: UniProtKB
  10. epidermis morphogenesis Source: MGI
  11. epithelial cell-cell adhesion Source: MGI
  12. epithelial-mesenchymal cell signaling Source: MGI
  13. establishment of Golgi localization Source: Ensembl
  14. establishment or maintenance of apical/basal cell polarity Source: MGI
  15. establishment or maintenance of cell polarity Source: UniProtKB
  16. filopodium assembly Source: MGI
  17. Golgi organization Source: Ensembl
  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. metabolic process Source: GOC
  24. multicellular organism growth Source: MGI
  25. negative regulation of gene expression Source: MGI
  26. negative regulation of protein complex assembly Source: Ensembl
  27. neuron fate determination Source: MGI
  28. nuclear migration Source: MGI
  29. nucleus localization Source: MGI
  30. organelle transport along microtubule Source: Ensembl
  31. positive regulation of cytokinesis Source: UniProtKB
  32. positive regulation of DNA replication Source: Ensembl
  33. positive regulation of epithelial cell proliferation involved in lung morphogenesis Source: CACAO
  34. positive regulation of gene expression Source: MGI
  35. positive regulation of hair follicle cell proliferation Source: MGI
  36. positive regulation of intracellular protein transport Source: Ensembl
  37. positive regulation of JNK cascade Source: Ensembl
  38. positive regulation of MAPK cascade Source: MGI
  39. positive regulation of metalloenzyme activity Source: Ensembl
  40. positive regulation of neuron apoptotic process Source: Ensembl
  41. positive regulation of peptidyl-serine phosphorylation Source: MGI
  42. positive regulation of phosphatidylinositol 3-kinase activity Source: MGI
  43. positive regulation of protein phosphorylation Source: MGI
  44. positive regulation of pseudopodium assembly Source: Ensembl
  45. positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  46. positive regulation of synapse structural plasticity Source: Ensembl
  47. regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  48. regulation of filopodium assembly Source: UniProtKB
  49. regulation of mitotic nuclear division Source: MGI
  50. regulation of protein catabolic process Source: MGI
  51. regulation of protein heterodimerization activity Source: MGI
  52. regulation of protein kinase activity Source: MGI
  53. regulation of protein metabolic process Source: MGI
  54. regulation of protein stability Source: MGI
  55. Rho protein signal transduction Source: MGI
  56. single organismal cell-cell adhesion Source: UniProtKB
  57. sprouting angiogenesis Source: Ensembl
  58. submandibular salivary gland formation Source: Ensembl
  59. substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_295531. DCC mediated attractive signaling.
REACT_297947. Rho GTPase cycle.
REACT_300885. Inactivation of Cdc42 and Rac.
REACT_304595. CDO in myogenesis.
REACT_313804. EPHB-mediated forward signaling.
REACT_314817. CD28 dependent Vav1 pathway.
REACT_315885. VEGFA-VEGFR2 Pathway.
REACT_344463. Regulation of actin dynamics for phagocytic cup formation.
REACT_350802. EGFR downregulation.

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 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:106211. Cdc42.

Subcellular locationi

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

  4. 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. cytoplasmic ribonucleoprotein granule Source: Ensembl
  7. cytosol Source: Reactome
  8. extracellular vesicular exosome Source: Ensembl
  9. filopodium Source: Ensembl
  10. focal adhesion Source: Ensembl
  11. Golgi membrane Source: Ensembl
  12. leading edge membrane Source: MGI
  13. membrane Source: UniProtKB
  14. microtubule organizing center Source: UniProtKB-SubCell
  15. midbody Source: UniProtKB
  16. mitotic spindle Source: UniProtKB
  17. myelin sheath Source: UniProtKB
  18. neuronal cell body Source: Ensembl
  19. neuron projection Source: Ensembl
  20. plasma membrane Source: MGI
  21. secretory granule Source: Ensembl
  22. spindle midzone Source: UniProtKB
Complete GO annotation...

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

BgeeiP60766.
CleanExiMM_CDC42.
ExpressionAtlasiP60766. baseline and differential.
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 – 96Combined sources
Helixi16 – 2510Combined sources
Beta strandi36 – 4611Combined sources
Beta strandi49 – 5810Combined sources
Helixi62 – 643Combined sources
Turni65 – 673Combined sources
Helixi68 – 714Combined sources
Beta strandi76 – 838Combined sources
Helixi87 – 959Combined sources
Helixi97 – 1048Combined sources
Beta strandi110 – 1156Combined sources
Helixi117 – 1193Combined sources
Helixi123 – 1319Combined sources
Helixi139 – 14810Combined sources
Beta strandi154 – 1563Combined sources
Turni159 – 1613Combined sources
Helixi165 – 17713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118978.
HOVERGENiHBG009351.
InParanoidiP60766.
KOiK04393.
OMAiKSDGERM.
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. AlignAdd to basket

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

        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
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiP60766.

PTM databases

PhosphoSiteiP60766.

Proteomic databases

MaxQBiP60766.
PaxDbiP60766.
PRIDEiP60766.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi998.
MGIiMGI:106211. Cdc42.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118978.
HOVERGENiHBG009351.
InParanoidiP60766.
KOiK04393.
OMAiKSDGERM.
OrthoDBiEOG764747.
PhylomeDBiP60766.
TreeFamiTF101109.

Enzyme and pathway databases

ReactomeiREACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_295531. DCC mediated attractive signaling.
REACT_297947. Rho GTPase cycle.
REACT_300885. Inactivation of Cdc42 and Rac.
REACT_304595. CDO in myogenesis.
REACT_313804. EPHB-mediated forward signaling.
REACT_314817. CD28 dependent Vav1 pathway.
REACT_315885. VEGFA-VEGFR2 Pathway.
REACT_344463. Regulation of actin dynamics for phagocytic cup formation.
REACT_350802. EGFR downregulation.

Miscellaneous databases

EvolutionaryTraceiP60766.
NextBioi281582.
PROiP60766.
SOURCEiSearch...

Gene expression databases

BgeeiP60766.
CleanExiMM_CDC42.
ExpressionAtlasiP60766. baseline and differential.
GenevestigatoriP60766.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 132 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

Similar 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 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.