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Ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)
Protein RAC2 PDB 1ds6.png
PDB rendering based on 1ds6.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols RAC2 ; EN-7; Gx; HSPC022; p21-Rac2
External IDs OMIM602049 MGI97846 HomoloGene55699 ChEMBL: 5581 GeneCards: RAC2 Gene
RNA expression pattern
PBB GE RAC2 213603 s at tn.png
More reference expression data
Species Human Mouse
Entrez 5880 19354
Ensembl ENSG00000128340 ENSMUSG00000033220
UniProt P15153 Q05144
RefSeq (mRNA) NM_002872 NM_009008
RefSeq (protein) NP_002863 NP_033034
Location (UCSC) Chr 22:
37.62 – 37.64 Mb
Chr 15:
78.56 – 78.57 Mb
PubMed search [1] [2]

Rac2 (Ras-related C3 botulinum toxin substrate 2) is a small (~21 kDa) signaling G protein (to be specific, a GTPase), and is a member of the Rac subfamily of the family Rho family of GTPases.[1] It is encoded by the gene RAC2.[2]

Members of Rho family of GTPases appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases.[2]


Rac2 has been shown to interact with ARHGDIA[3][4] and Nitric oxide synthase 2A.[5]

See also[edit]


  1. ^ Ridley A (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol. 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823. 
  2. ^ a b "Entrez Gene: RAC2 ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)". 
  3. ^ Gorvel J, Chang T, Boretto J, Azuma T, Chavrier P (January 1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. 422 (2): 269–73. doi:10.1016/S0014-5793(98)00020-9. PMID 9490022. 
  4. ^ Fauré J, Dagher M (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie 83 (5): 409–14. doi:10.1016/S0300-9084(01)01263-9. PMID 11368848. 
  5. ^ Kuncewicz T, Balakrishnan P, Snuggs M, Kone B (August 2001). "Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages". Am. J. Physiol. Renal Physiol. 281 (2): F326–36. PMID 11457725. 

Further reading[edit]

  • Mizuno T, Kaibuchi K, Ando S, Musha T, Hiraoka K, Takaishi K et al. (1992). "Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins". J. Biol. Chem. 267 (15): 10215–8. PMID 1316893. 
  • Reibel L, Dorseuil O, Stancou R, Bertoglio J, Gacon G (1991). "A hemopoietic specific gene encoding a small GTP binding protein is overexpressed during T cell activation". Biochem. Biophys. Res. Commun. 175 (2): 451–8. doi:10.1016/0006-291X(91)91585-Z. PMID 1902092. 
  • Kinsella B, Erdman R, Maltese W (1991). "Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA". J. Biol. Chem. 266 (15): 9786–94. PMID 1903399. 
  • Didsbury J, Weber R, Bokoch G, Evans T, Snyderman R (1989). "rac, a novel ras-related family of proteins that are botulinum toxin substrates". J. Biol. Chem. 264 (28): 16378–82. PMID 2674130. 
  • Kwong C, Malech H, Rotrosen D, Leto T (1993). "Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins". Biochemistry 32 (21): 5711–7. doi:10.1021/bi00072a029. PMID 8504089. 
  • Courjal F, Chuchana P, Theillet C, Fort P (1997). "Structure and chromosomal assignment to 22q12 and 17qter of the ras-related Rac2 and Rac3 human genes". Genomics 44 (2): 242–6. doi:10.1006/geno.1997.4871. PMID 9299243. 
  • Gorvel J, Chang T, Boretto J, Azuma T, Chavrier P (1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. 422 (2): 269–73. doi:10.1016/S0014-5793(98)00020-9. PMID 9490022. 
  • Dai Q, Choy E, Chiu V, Romano J, Slivka S, Steitz S et al. (1998). "Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum". J. Biol. Chem. 273 (24): 15030–4. doi:10.1074/jbc.273.24.15030. PMID 9614111. 
  • Ahmed S, Prigmore E, Govind S, Veryard C, Kozma R, Wientjes F et al. (1998). "Cryptic Rac-binding and p21(Cdc42Hs/Rac)-activated kinase phosphorylation sites of NADPH oxidase component p67(phox)". J. Biol. Chem. 273 (25): 15693–701. doi:10.1074/jbc.273.25.15693. PMID 9624165. 
  • Faris S, Rinckel L, Huang J, Hong Y, Kleinberg M (1998). "Phagocyte NADPH oxidase p67-phox possesses a novel carboxylterminal binding site for the GTPases Rac2 and Cdc42". Biochem. Biophys. Res. Commun. 247 (2): 271–6. doi:10.1006/bbrc.1998.8775. PMID 9642115. 
  • Zhang B, Zheng Y (1998). "Negative regulation of Rho family GTPases Cdc42 and Rac2 by homodimer formation". J. Biol. Chem. 273 (40): 25728–33. doi:10.1074/jbc.273.40.25728. PMID 9748241. 
  • Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T et al. (1999). "Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins". Biochim. Biophys. Acta 1452 (2): 179–87. doi:10.1016/S0167-4889(99)00133-0. PMID 10559471. 
  • Dunham I, Shimizu N, Roe B, Chissoe S, Hunt A, Collins J et al. (1999). "The DNA sequence of human chromosome 22". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208. 
  • Scheffzek K, Stephan I, Jensen O, Illenberger D, Gierschik P (2000). "The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI". Nat. Struct. Biol. 7 (2): 122–6. doi:10.1038/72392. PMID 10655614. 
  • Ambruso D, Knall C, Abell A, Panepinto J, Kurkchubasche A, Thurman G et al. (2000). "Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4654–9. doi:10.1073/pnas.080074897. PMC 18288. PMID 10758162. 
  • Williams D, Tao W, Yang F, Kim C, Gu Y, Mansfield P et al. (2000). "Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency". Blood 96 (5): 1646–54. PMID 10961859. 
  • Tamura M, Kai T, Tsunawaki S, Lambeth J, Kameda K (2000). "Direct interaction of actin with p47(phox) of neutrophil NADPH oxidase". Biochem. Biophys. Res. Commun. 276 (3): 1186–90. doi:10.1006/bbrc.2000.3598. PMID 11027608. 
  • Zhang Q, Ye M, Wu X, Ren S, Zhao M, Zhao C et al. (2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152. 
  • Lapouge K, Smith S, Walker P, Gamblin S, Smerdon S, Rittinger K (2000). "Structure of the TPR domain of p67phox in complex with Rac.GTP". Mol. Cell 6 (4): 899–907. doi:10.1016/S1097-2765(05)00091-2. PMID 11090627. 
  • Tarricone C, Xiao B, Justin N, Walker P, Rittinger K, Gamblin S et al. (2001). "The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways". Nature 411 (6834): 215–9. doi:10.1038/35075620. PMID 11346801. 

External links[edit]