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Protein

Cell division control protein 42 homolog

Gene

CDC42

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.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

  • apolipoprotein A-I receptor binding Source: BHF-UCL
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein kinase binding Source: BHF-UCL
  • thioesterase binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: AgBase

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-182971. EGFR downregulation.
R-HSA-194840. Rho GTPase cycle.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-375170. CDO in myogenesis.
R-HSA-389359. CD28 dependent Vav1 pathway.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-418885. DCC mediated attractive signaling.
R-HSA-428543. Inactivation of Cdc42 and Rac.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP60953.
SIGNORiP60953.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1736. CDC42.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • cell-cell junction Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytosol Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • filopodium Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi membrane Source: BHF-UCL
  • leading edge membrane Source: Ensembl
  • membrane Source: UniProtKB
  • microtubule organizing center Source: UniProtKB-SubCell
  • midbody Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • myelin sheath Source: Ensembl
  • neuronal cell body Source: BHF-UCL
  • neuron projection Source: BHF-UCL
  • plasma membrane Source: UniProtKB
  • secretory granule Source: Ensembl
  • spindle midzone Source: UniProtKB
  • storage vacuole Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Takenouchi-Kosaki syndrome (TKS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by macrothrombocytopenia, lymphedema, mental retardation, developmental delay, and distinctive facial features.
See also OMIM:616737
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641Y → C in TKS. 2 Publications
VAR_076337

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

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi616737. phenotype.
PharmGKBiPA26266.

Chemistry

ChEMBLiCHEMBL6088.

Polymorphism and mutation databases

BioMutaiCDC42.
DMDMi322510015.

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 IbpA; alternate2 Publications
Glycosylationi32 – 321O-linked (GlcNAc); by Photorhabdus PAU_02230; alternate1 Publication
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

(Microbial infection) AMPylation at Tyr-32 and Thr-35 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo.3 Publications
Phosphorylated by SRC in an EGF-dependent manner, this stimulates the binding of the Rho-GDP dissociation inhibitor RhoGDI.1 Publication
(Microbial infection) Glycosylated at Tyr-32 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of CDC42 and leads to actin disassembly.1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

EPDiP60953.
MaxQBiP60953.
PaxDbiP60953.
PeptideAtlasiP60953.
PRIDEiP60953.
TopDownProteomicsiP60953-2. [P60953-2]

PTM databases

iPTMnetiP60953.
PhosphoSiteiP60953.
SwissPalmiP60953.

Miscellaneous databases

PMAP-CutDBP60953.

Expressioni

Gene expression databases

BgeeiENSG00000070831.
CleanExiHS_CDC42.
ExpressionAtlasiP60953. baseline and differential.
GenevisibleiP60953. HS.

Organism-specific databases

HPAiCAB004360.
CAB015931.

Interactioni

Subunit structurei

The GTP-bound form interacts with CCPG1 (By similarity). Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4, CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-dependent manner). Interacts with activated CSPG4 and with BAIAP2. Interacts with Zizimin1/DOCK9 and Zizimin2/DOCK11, which activate it by exchanging GDP for GTP. Interacts with NET1 and ARHGAP33/TCGAP. Part of a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ. Interacts with USP6. May interact with ARHGEF16; responsible for the activation of CDC42 by the viral protein HPV16 E6. Interacts with NEK6. Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with ITGB1BP1. Interacts with ARHGDIA; this interaction inactivates and stabilizes CDC42. Interacts with ARHGDIB; this maintains CDC42 in the inactive, GDP-bound form.By similarity16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-81752,EBI-81752
ABCA1O954772EBI-81752,EBI-784112
ARHGAP1Q079602EBI-81752,EBI-602762
BAIAP2Q9UQB82EBI-287394,EBI-525456
BAIAP2Q9UQB8-44EBI-81752,EBI-6174091
Bin1Q9VEX92EBI-81752,EBI-129424From a different organism.
CDC42BPAQ5VT255EBI-81752,EBI-689171
CDC42EP1Q005876EBI-81752,EBI-744130
CDC42EP2O146135EBI-81752,EBI-3438291
IQGAP1P469404EBI-81752,EBI-297509
ITSN1Q158112EBI-3625591,EBI-602041
LRRK2Q5S0073EBI-81752,EBI-5323863
MAP3K11Q165843EBI-81752,EBI-49961
MAPK8P459832EBI-81752,EBI-286483
MARK4Q96L342EBI-81752,EBI-302319
Mcf2lQ640963EBI-287394,EBI-602123From a different organism.
PAK1Q1315312EBI-81752,EBI-1307
PAK2Q131774EBI-81752,EBI-1045887
PAK3O759142EBI-287394,EBI-3389553
Pak3Q610363EBI-81752,EBI-457317From a different organism.
PAK4O960132EBI-81752,EBI-713738
PARD6AQ9NPB67EBI-81752,EBI-81876
PARD6BQ9BYG510EBI-81752,EBI-295391
Pard6bQ9JK836EBI-81752,EBI-81861From a different organism.
PARD6GQ9BYG45EBI-81752,EBI-295417
PRKCIP417435EBI-81752,EBI-286199
sopBA0A0H3NA162EBI-81752,EBI-10726187From a different organism.
sopBO309165EBI-81752,EBI-11167349From a different organism.
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.

GO - Molecular functioni

  • apolipoprotein A-I receptor binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • protein kinase binding Source: BHF-UCL
  • thioesterase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107433. 203 interactions.
DIPiDIP-31097N.
IntActiP60953. 176 interactions.
MINTiMINT-94609.
STRINGi9606.ENSP00000314458.

Chemistry

BindingDBiP60953.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4YC7X-ray2.50A1-179[»]
4YDHX-ray3.80B/D1-179[»]
5FI1X-ray3.20B1-191[»]
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

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP60953.
KOiK04393.
OMAiVITIDQG.
OrthoDBiEOG091G0KCM.
PhylomeDBiP60953.
TreeFamiTF101109.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 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: P60953-2) [UniParc]FASTAAdd to basket
Also known as: Placental

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP
60 70 80 90 100
YTLGLFDTAG QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE
110 120 130 140 150
ITHHCPKTPF LLVGTQIDLR DDPSTIEKLA KNKQKPITPE TAEKLARDLK
160 170 180 190
AVKYVECSAL TQKGLKNVFD EAILAALEPP EPKKSRRCVL L
Length:191
Mass (Da):21,259
Last modified:February 8, 2011 - v2
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641Y → C in TKS. 2 Publications
VAR_076337

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:
EMBLi
GenBanki
DDBJi
Links Updated
M35543 mRNA. Translation: AAA52494.1.
M57298 mRNA. Translation: AAA52592.1.
AL121734 mRNA. Translation: CAB57325.1.
AL121735 mRNA. Translation: CAB57326.1.
AF498962 mRNA. Translation: AAM21109.1.
AF498963 mRNA. Translation: AAM21110.1.
AY673602 Genomic DNA. Translation: AAT70721.1.
AL031281 Genomic DNA. Translation: CAB52602.1.
AL031281 Genomic DNA. Translation: CAD92551.1.
BC002711 mRNA. Translation: AAH02711.1.
BC003682 mRNA. Translation: AAH03682.1.
BC018266 mRNA. Translation: AAH18266.1.
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.4. human.

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:
EMBLi
GenBanki
DDBJi
Links Updated
M35543 mRNA. Translation: AAA52494.1.
M57298 mRNA. Translation: AAA52592.1.
AL121734 mRNA. Translation: CAB57325.1.
AL121735 mRNA. Translation: CAB57326.1.
AF498962 mRNA. Translation: AAM21109.1.
AF498963 mRNA. Translation: AAM21110.1.
AY673602 Genomic DNA. Translation: AAT70721.1.
AL031281 Genomic DNA. Translation: CAB52602.1.
AL031281 Genomic DNA. Translation: CAD92551.1.
BC002711 mRNA. Translation: AAH02711.1.
BC003682 mRNA. Translation: AAH03682.1.
BC018266 mRNA. Translation: AAH18266.1.
CCDSiCCDS221.1.
CCDS222.1. [P60953-1]
PIRiA36382.
A39265.
RefSeqiNP_001034891.1. NM_001039802.1. [P60953-2]
NP_001782.1. NM_001791.3. [P60953-2]
NP_426359.1. NM_044472.2. [P60953-1]
UniGeneiHs.467637.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4YC7X-ray2.50A1-179[»]
4YDHX-ray3.80B/D1-179[»]
5FI1X-ray3.20B1-191[»]
ProteinModelPortaliP60953.
SMRiP60953. Positions 1-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107433. 203 interactions.
DIPiDIP-31097N.
IntActiP60953. 176 interactions.
MINTiMINT-94609.
STRINGi9606.ENSP00000314458.

Chemistry

BindingDBiP60953.
ChEMBLiCHEMBL6088.

PTM databases

iPTMnetiP60953.
PhosphoSiteiP60953.
SwissPalmiP60953.

Polymorphism and mutation databases

BioMutaiCDC42.
DMDMi322510015.

Proteomic databases

EPDiP60953.
MaxQBiP60953.
PaxDbiP60953.
PeptideAtlasiP60953.
PRIDEiP60953.
TopDownProteomicsiP60953-2. [P60953-2]

Protocols and materials databases

DNASUi998.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi998.
GeneCardsiCDC42.
HGNCiHGNC:1736. CDC42.
HPAiCAB004360.
CAB015931.
MIMi116952. gene.
616737. phenotype.
neXtProtiNX_P60953.
PharmGKBiPA26266.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP60953.
KOiK04393.
OMAiVITIDQG.
OrthoDBiEOG091G0KCM.
PhylomeDBiP60953.
TreeFamiTF101109.

Enzyme and pathway databases

ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-182971. EGFR downregulation.
R-HSA-194840. Rho GTPase cycle.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-375170. CDO in myogenesis.
R-HSA-389359. CD28 dependent Vav1 pathway.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-418885. DCC mediated attractive signaling.
R-HSA-428543. Inactivation of Cdc42 and Rac.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP60953.
SIGNORiP60953.

Miscellaneous databases

ChiTaRSiCDC42. human.
EvolutionaryTraceiP60953.
GeneWikiiCDC42.
GenomeRNAii998.
PMAP-CutDBP60953.
PROiP60953.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000070831.
CleanExiHS_CDC42.
ExpressionAtlasiP60953. baseline and differential.
GenevisibleiP60953. HS.

Family and domain databases

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

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: September 7, 2016
This is version 166 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.