Contents 1 Function 2 Structure 3 Role in cancer 4 Interactions 5 References 6 External links


Function[edit] Human Cdc42 is a small GTPase of the Rho family, which regulates signaling pathways that control diverse cellular functions including cell morphology, cell migration, endocytosis and cell cycle progression.[3] Rho GTPases are central to dynamic actin cytoskeletal assembly and rearrangement that are the basis of cell-cell adhesion and migration. Activated Cdc42 activates by conformational changes[4] p21-activated kinases PAK1 and PAK2, which in turn initiate actin reorganization and regulate cell adhesion, migration, and invasion.[5]


Structure[edit] Cdc42 is a homodimer with A and B chains.[6] Its total length is 191 amino acids and its theoretical weight is 21.33 KDa.[6] Its sequence domains include a P-loop containing nucleoside triphosphate hydrolase and a small GTP-binding protein domain.[6] Cdc42 cycles between an active GTP-bound state and an inactive GDP-bound state. This process is regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase GTP hydrolysis activity, and GTDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase.[7]


Role in cancer[edit] Recently, Cdc42 has been shown to actively assist in cancer progression. Several studies have established the basis for this and hypothesized about the underlying mechanisms. Cdc42 is overexpressed in non-small cell lung cancer, colorectal adenocarcinoma, melanoma, breast cancer, and testicular cancer.[8] Elevated levels of the protein have been correlated with negative patient survival. Cdc42 has also been shown to be required for both G1-S phase progression and mitosis, and it also modulates the transcription factors SRF, STAT3, and NFkB.[8] It has been hypothesized that targeting Cdc42 in conjunction with chemotherapy may be an effective cancer treatment strategy. In one study studying the role of Cdc42 in cervical cancer, immunohistochemistry was used to detect Cdc42 expression in three types of tissues: normal cervical tissues, cervical intraepithelial neoplasia (CIN) I or below, CIN II or above, and cervical cancer tissues.[9] Cdc42 expression was gradually increased showing significant difference and was significantly higher in HeLa cells than in regular cells. The migration ability of HeLa cells transfected with Cdc42 was higher than that of non-transfected cells.[9] It was proposed that the overexpression of Cdc42 can promote filopodia formation in HeLa cells. Cdc42 overexpression significantly improved the ability of cervical cancer cells to migrate, possibly due to improved pseudopodia formation.[9] Another study found that Cdc42 drives the process of initiating a metastatic tumor in a new tissue by promoting the expression of β1 integrin, an adhesion receptor known to be involved in metastasis.[10] Levels of β1 integrin were reduced in Cdc42-deficient cells. β1 integrin is important for adhesion to the extracellular matrix, and could be important for the initial attachment to endothelial cells as well. Knocking down β1 integrin inhibited cancer cell migration, whereas overexpressing the integrin in Cdc42-deficient cells restored endothelial invasion.[10] Cdc42 promoted β1 integrin expression by activating a transcription factor called SRF. A continually active form of the transcription factor was also capable of restoring endothelial insertion to cancer cells lacking Cdc42. Normal cancer cells and Cdc42-deficient cancer cells have also been compared in vivo. When both types of cells were injected into mouse tail veins, control cells spread out more on the vessel endothelium within minutes, suggesting that Cdc42 assists in cell migration.[10] After six weeks, the control cells had generated more metastases than the Cdc42-deficient cells. Invading cancer cells send out protrusions that reach down between neighboring endothelial cells to contact the underlying basement membrane. The cancer cells then spread out on this extracellular matrix so that the endothelial cells retract, and allow the invaders to insert themselves between them.[10] In the absence of Cdc42, cancer cells failed to spread out on the basement membrane, and Cdc42-deficient cells showed reduced adhesion to extracellular matrix-coated coverslips.[10] Cdc42 therefore promotes the attachment of cancer cells to both endothelial cells and the underlying basement membrane during transendothelial migration. The small molecular inhibitor AZA197 has been used to inhibit Cdc42 in the treatment of KRAS mutant colorectal cancers.[11] There was evidence that Cdc42 inhibition by AZA197 treatment suppresses proliferative and pro-survival signaling pathways via PAK1-ERK signaling and reduces colon cancer cell migration and invasion.[11] In mice, systemic AZA197 treatment in vivo reduced primary tumor growth and prolonged survival.[11] Therapy targeting Rho GTPase Cdc42 signaling pathways may be effective for treatment of patients with advanced colon cancer overexpressing Cdc42, and particularly those with KRAS-mutant disease.


Interactions[edit] CDC42 has been shown to interact with: ARHGAP1,[12][13][14][15] ARHGDIA,[16][17] BAIAP2,[18][19][20] BNIP2,[14][21][22] BNIPL,[23] CDC42EP2,[24][25] CDC42EP3,[24][26] ERRFI1,[27] GDI1,[28] IQGAP1,[15][29][30][31][32] IQGAP2,[33] ITSN1,[34][35] MAP3K10,[12] MAP3K11,[12][36] PAK1,[15][37] PAK2,[15][38][39] PAK4.[16][39][40] PAK7,[40][41] PARD6A,[42][43][44] PARD6B,[42][43][45] Phospholipase D1,[46] RICS[47][48][49] TRIP10,[50][51] WASL,[52][53] Wiskott-Aldrich syndrome protein,[51][54][55][56]


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External links[edit] Wikimedia Commons has media related to CDC42. cdc42 GTP-Binding Protein at the US National Library of Medicine Medical Subject Headings (MeSH) CDC42 Info with links in the Cell Migration Gateway Human CDC42 genome location and CDC42 gene details page in the UCSC Genome Browser. v t e PDB gallery 1a4r: G12V MUTANT OF HUMAN PLACENTAL CDC42 GTPASE IN THE GDP FORM  1aje: CDC42 FROM HUMAN, NMR, 20 STRUCTURES  1am4: COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)  1an0: CDC42HS-GDP COMPLEX  1cee: SOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE BINDING DOMAIN OF WASP  1cf4: CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX  1doa: STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI  1e0a: CDC42 COMPLEXED WITH THE GTPASE BINDING DOMAIN OF P21 ACTIVATED KINASE  1ees: SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES  1grn: CRYSTAL STRUCTURE OF THE CDC42/CDC42GAP/ALF3 COMPLEX.  1gzs: CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GEF DOMAIN OF THE SALMONELLA TYPHIMURIUM SOPE TOXIN AND HUMAN CDC42  1ki1: Guanine Nucleotide Exchange Region of Intersectin in Complex with Cdc42  1kz7: Crystal Structure of the DH/PH Fragment of Murine Dbs in Complex with the Placental Isoform of Human Cdc42  1kzg: DbsCdc42(Y889F)  1nf3: Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6  2ase: NMR structure of the F28L mutant of Cdc42Hs  2dfk: Crystal structure of the CDC42-Collybistin II complex  2ngr: TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS BY CDC42: COMPARISONS OF THE HIGH RESOLUTION STRUCTURES FOR CDC42 BOUND TO THE ACTIVE AND CATALYTICALLY COMPROMISED FORMS OF THE CDC42-GAP.  2odb: The crystal structure of human cdc42 in complex with the CRIB domain of human p21-activated kinase 6 (PAK6)  v t e Hydrolases: acid anhydride hydrolases (EC 3.6) 3.6.1 Pyrophosphatase Inorganic Thiamine Apyrase Thiamine-triphosphatase 3.6.2 Adenylylsulfatase Phosphoadenylylsulfatase 3.6.3-4: ATPase 3.6.3 Cu++ (3.6.3.4) Menkes/ATP7A Wilson/ATP7B Ca+ (3.6.3.8) SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2 Na+/K+ (3.6.3.9) ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4 H+/K+ (3.6.3.10) ATP4A Other P-type ATPase ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3 3.6.4 Dynein Kinesin Myosin Katanin 3.6.5: GTPase 3.6.5.1: Heterotrimeric G protein Gαs Gαi GNAI1 GNAI2 GNAI3 Gαq/11 GNAQ GNA11 Gα12/13 GNA12 GNA13 Transducin GNAT1 GNAT2 Gustducin GNAT3 3.6.5.2: Small GTPase > Ras superfamily Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK 3.6.5.3: Protein-synthesizing GTPase Prokaryotic IF-2 EF-Tu EF-G Eukaryotic 3.6.5.5-6: Polymerization motors Dynamin Tubulin v t e Cell cycle proteins Cyclin A (A1, A2) B (B1, B2, B3) D (D1, D2, D3) E (E1, E2) CDK 1 2 3 4 5 6 7 8 9 10 CDK-activating kinase CDK inhibitor INK4a/ARF (p14arf/p16, p15, p18, p19) cip/kip (p21, p27, p57) P53 p63 p73 family p53 p63 p73 Other Cdc2 Cdc25 Cdc42 Cellular apoptosis susceptibility protein E2F Maturation promoting factor Wee Cullin (CUL7) Phases and checkpoints Interphase G1 phase S phase G2 phase M phase Mitosis (Preprophase Prophase Prometaphase Metaphase Anaphase Telophase) Cytokinesis Cell cycle checkpoints Restriction point Spindle checkpoint Postreplication checkpoint Other cellular phases Apoptosis G0 phase Meiosis v t e Hydrolases: acid anhydride hydrolases (EC 3.6) 3.6.1 Pyrophosphatase Inorganic Thiamine Apyrase Thiamine-triphosphatase 3.6.2 Adenylylsulfatase Phosphoadenylylsulfatase 3.6.3-4: ATPase 3.6.3 Cu++ (3.6.3.4) Menkes/ATP7A Wilson/ATP7B Ca+ (3.6.3.8) SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2 Na+/K+ (3.6.3.9) ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4 H+/K+ (3.6.3.10) ATP4A Other P-type ATPase ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3 3.6.4 Dynein Kinesin Myosin Katanin 3.6.5: GTPase 3.6.5.1: Heterotrimeric G protein Gαs Gαi GNAI1 GNAI2 GNAI3 Gαq/11 GNAQ GNA11 Gα12/13 GNA12 GNA13 Transducin GNAT1 GNAT2 Gustducin GNAT3 3.6.5.2: Small GTPase > Ras superfamily Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK 3.6.5.3: Protein-synthesizing GTPase Prokaryotic IF-2 EF-Tu EF-G Eukaryotic 3.6.5.5-6: Polymerization motors Dynamin Tubulin Retrieved from "https://en.wikipedia.org/w/index.php?title=CDC42&oldid=785612509" Categories: Genes on human chromosome 1Hidden categories: Commons category without a link on Wikidata


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CDC42 - Photos and All Basic Informations

CDC42 More Links

ProteinCell CycleSaccharomyces CerevisiaeCell DivisionProtein Data BankGene NomenclatureMendelian Inheritance In ManHomoloGeneGeneCardsChromosome 1 (human)ChromosomeChromosome 1 (human)Chromosome 1 (human)Genomic Location For CDC42Genomic Location For CDC42Locus (genetics)Base PairBase PairGene ExpressionGene OntologyEntrezEnsemblUniProtPubMedWikidataGTPaseRho Family Of GTPasesMorphology (biology)Cell MigrationPAK1PAK2HomodimerImmunohistochemistryCervical Intraepithelial NeoplasiaHeLaFilopodiaPseudopodiaMetastasisIntegrinExtracellular MatrixEndotheliumProtein-protein InteractionARHGAP1ARHGDIABAIAP2BNIP2BNIPLCDC42EP2CDC42EP3ERRFI1GDI1IQGAP1IQGAP2ITSN1MAP3K10MAP3K11PAK1PAK2PAK4PAK7PARD6APARD6BPhospholipase D1RICS (gene)TRIP10WASL (gene)Wiskott-Aldrich Syndrome ProteinEnsembl Genome Database ProjectDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierMedical Subject HeadingsUCSC Genome BrowserTemplate:PDB GalleryTemplate Talk:PDB Gallery1a4r: G12V MUTANT OF HUMAN PLACENTAL CDC42 GTPASE IN THE GDP FORM1aje: CDC42 FROM HUMAN, NMR, 20 STRUCTURES1am4: COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)1an0: CDC42HS-GDP COMPLEX1cee: SOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE BINDING DOMAIN OF WASP1cf4: CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX1doa: STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI1e0a: CDC42 COMPLEXED WITH THE GTPASE BINDING DOMAIN OF P21 ACTIVATED KINASE1ees: SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES1grn: CRYSTAL STRUCTURE OF THE CDC42/CDC42GAP/ALF3 COMPLEX.1gzs: CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GEF DOMAIN OF THE SALMONELLA TYPHIMURIUM SOPE TOXIN AND HUMAN CDC421ki1: Guanine Nucleotide Exchange Region Of Intersectin In Complex With Cdc421kz7: Crystal Structure Of The DH/PH Fragment Of Murine Dbs In Complex With The Placental Isoform Of Human Cdc421kzg: DbsCdc42(Y889F)1nf3: Structure Of Cdc42 In A Complex With The GTPase-binding Domain Of The Cell Polarity Protein, Par62ase: NMR Structure Of The F28L Mutant Of Cdc42Hs2dfk: Crystal Structure Of The CDC42-Collybistin II Complex2ngr: TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS BY CDC42: COMPARISONS OF THE HIGH RESOLUTION STRUCTURES FOR CDC42 BOUND TO THE ACTIVE AND CATALYTICALLY COMPROMISED FORMS OF THE CDC42-GAP.2odb: The Crystal Structure Of Human Cdc42 In Complex With The CRIB Domain Of Human P21-activated Kinase 6 (PAK6)Template:Acid Anhydride HydrolasesTemplate Talk:Acid Anhydride HydrolasesHydrolaseAcid Anhydride HydrolasesEnzyme Commission NumberList Of EC Numbers (EC 3)PyrophosphataseInorganic PyrophosphataseThiamine PyrophosphataseApyraseThiamine-triphosphataseList Of EC Numbers (EC 3)AdenylylsulfatasePhosphoadenylylsulfataseList Of EC Numbers (EC 3)List Of EC Numbers (EC 3)ATPaseATP7AWilson Disease ProteinCalcium ATPaseSERCAATP2A1ATP2A2ATP2A3Plasma Membrane Ca2+ ATPaseATP2B1ATP2B2ATP2B3ATP2B4Secretory Pathway Ca²⁺ ATPaseATP2C1Na+/K+-ATPaseATPase, Na+/K+ Transporting, Alpha 1ATP1A2ATP1A3ATP1A4ATP1B1ATP1B3Hydrogen Potassium ATPaseP-type ATPaseATP8B1ATP10AATP11BATP12AATP13A2ATP13A3DyneinKinesinMyosinKataninList Of EC Numbers (EC 3)GTPaseHeterotrimeric G ProteinGs Alpha SubunitGi Alpha SubunitGNAI1GNAI2GNAI3Gq Alpha SubunitGNAQGNA11G12/G13 Alpha SubunitsGNA12GNA13TransducinGNAT1GNAT2GustducinGNAT3Small GTPaseRas SuperfamilyRho Family Of GTPasesTC10 ProteinTCL (GTPase)Wrch1Chp (GTPase)Rac (GTPase)RAC1RAC2Rac3RhoGRHOBTB1RHOBTB2RhoHRho Family Of GTPasesRHOARHOBRhoCRnd (GTPase)Rnd1Rnd2Rnd3Rif (GTPase)RhoDRas SubfamilyHRASKRASNeuroblastoma RAS Viral Oncogene HomologRab (G-protein)RAB23RAB27ADP Ribosylation FactorARF6SAR1BARL13BARL6Ran (gene)RHEBRap GTP-binding ProteinRRADProtein-synthesizing GTPaseProkaryotic Elongation FactorsProkaryotic Initiation Factor-2EF-TuEF-GEukaryotic Elongation FactorsMolecular MotorDynaminTubulinTemplate:Cell Cycle ProteinsTemplate Talk:Cell Cycle ProteinsCell CycleProteinCyclinCyclin ACyclin A1Cyclin A2Cyclin BCyclin B1Cyclin B2Cyclin DCyclin D1Cyclin D2Cyclin D3Cyclin ECyclin E1Cyclin E2Cyclin-dependent KinaseCyclin-dependent Kinase 1Cyclin-dependent Kinase 2Cyclin-dependent Kinase 3Cyclin-dependent Kinase 4Cyclin-dependent Kinase 5Cyclin-dependent Kinase 6Cyclin-dependent Kinase 7Cyclin-dependent Kinase 8Cyclin-dependent Kinase 9Cyclin-dependent Kinase 10CDK-activating KinaseCyclin-dependent Kinase Inhibitor ProteinCell CycleP14arfP16CDKN2BCDKN2CCDKN2DCell CycleP21CDKN1BCyclin-dependent Kinase Inhibitor 1CP53 P63 P73 FamilyP53TP63P73Cdk1Cdc25Cellular Apoptosis Susceptibility ProteinE2FMaturation Promoting FactorWee1CullinCUL7InterphaseG1 PhaseS PhaseG2 PhaseCell DivisionMitosisPreprophaseProphasePrometaphaseMetaphaseAnaphaseTelophaseCytokinesisCell Cycle CheckpointRestriction PointSpindle CheckpointPostreplication CheckpointApoptosisG0 PhaseMeiosisTemplate:Acid Anhydride HydrolasesTemplate Talk:Acid Anhydride HydrolasesHydrolaseAcid Anhydride HydrolasesEnzyme Commission NumberList Of EC Numbers (EC 3)PyrophosphataseInorganic PyrophosphataseThiamine PyrophosphataseApyraseThiamine-triphosphataseList Of EC Numbers (EC 3)AdenylylsulfatasePhosphoadenylylsulfataseList Of EC Numbers (EC 3)List Of EC Numbers (EC 3)ATPaseATP7AWilson Disease ProteinCalcium ATPaseSERCAATP2A1ATP2A2ATP2A3Plasma Membrane Ca2+ ATPaseATP2B1ATP2B2ATP2B3ATP2B4Secretory Pathway Ca²⁺ ATPaseATP2C1Na+/K+-ATPaseATPase, Na+/K+ Transporting, Alpha 1ATP1A2ATP1A3ATP1A4ATP1B1ATP1B3Hydrogen Potassium ATPaseP-type ATPaseATP8B1ATP10AATP11BATP12AATP13A2ATP13A3DyneinKinesinMyosinKataninList Of EC Numbers (EC 3)GTPaseHeterotrimeric G ProteinGs Alpha SubunitGi Alpha SubunitGNAI1GNAI2GNAI3Gq Alpha SubunitGNAQGNA11G12/G13 Alpha SubunitsGNA12GNA13TransducinGNAT1GNAT2GustducinGNAT3Small GTPaseRas SuperfamilyRho Family Of GTPasesTC10 ProteinTCL (GTPase)Wrch1Chp (GTPase)Rac (GTPase)RAC1RAC2Rac3RhoGRHOBTB1RHOBTB2RhoHRho Family Of GTPasesRHOARHOBRhoCRnd (GTPase)Rnd1Rnd2Rnd3Rif (GTPase)RhoDRas SubfamilyHRASKRASNeuroblastoma RAS Viral Oncogene HomologRab (G-protein)RAB23RAB27ADP Ribosylation FactorARF6SAR1BARL13BARL6Ran (gene)RHEBRap GTP-binding ProteinRRADProtein-synthesizing GTPaseProkaryotic Elongation FactorsProkaryotic Initiation Factor-2EF-TuEF-GEukaryotic Elongation FactorsMolecular MotorDynaminTubulinHelp:CategoryCategory:Genes On Human Chromosome 1Category:Commons Category Without A Link On WikidataDiscussion About Edits From This IP Address [n]A List Of Edits Made From This IP Address [y]View The Content Page [c]Discussion About The Content Page [t]Edit This Page [e]Visit The Main Page [z]Guides To Browsing WikipediaFeatured Content – The Best Of WikipediaFind Background Information On Current EventsLoad A Random Article [x]Guidance On How To Use And Edit WikipediaFind Out About WikipediaAbout The Project, What You Can Do, Where To Find ThingsA List Of Recent Changes In The Wiki [r]List Of All English Wikipedia Pages Containing Links To This Page [j]Recent Changes In Pages Linked From This Page [k]Upload Files [u]A List Of All Special Pages 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