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RAC2 (ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2))

Identity

Other namesEN-7
GX
Gx
HSPC022
p21-Rac2
HGNC (Hugo) RAC2
LocusID (NCBI) 5880
Location 22q13.1
Location_base_pair Starts at 37621301 and ends at 37640339 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

Description The Rac2 gene sequence contains 7 exons (Courjal et al., 1997) and is expressed specifically in hematopoietic cells. Human Rac2 gene locus is silenced in non-hematopoietic cells by a mechanism that involves DNA methylation (Ladd et al., 2004). Cells that lack Rac2 expression exhibit increased cytosine methylation in the sequences flanking the gene, whereas cells that express Rac2 exhibit increased cytosine methylation within the body of the Rac2 gene.
Transcription The human Rac2 gene promoter lacks TATA and CCAAT boxes, utilizes multiple transcription initiation sites, and contains several putative Sp1 binding sites, which is common in promoters that lack TATA boxes (Ladd et al., 2004).
The transcript length is of 1471 nt translated to a 192 residues protein.

Protein

Description Rac2 protein belongs to the GTP-binding proteins of the Rho family and cycles between an active GTP-bound form and an inactive GDP-bound form. This regulatory cycle is exerted by three distinct families of proteins: guanine exchange factors (GEFs), GTPase-activating proteins (GAPs), and guanine nucleotide dissociation inhibitors (GDIs). Several GEFs have been shown to activate Rac2 selectively, Vav1 (Ming et al., 2007), Tiam1 (Haeusler et al., 2003), P-Rex1 (Welch et al., 2002), Swap70 (Sivalenka and Jessberger, 2004) and Dock2 (Nishihara et al., 2002). Two GAPs that act on Rac2 are Abr and Bcr (Chuang et al., 1995), as well as others found in leukocytes.
Rac2 function depends on association of the GTPase with membranes and subcellular localization, properties influenced by C-terminal lipid modifications, specifically is modified by the C20 GG isoprenoid.
Upon GTP loading, a conformational change takes place that allows Rac2 protein to interact with several downstream effectors that ultimately process the information and propagate the signal within the cell, causing changes in the actin cytoskeleton, release of inflammatory modulators and innate immunity. The signaling of active Rac2 is mediated by its interaction with effector proteins such as p67phox and cytochrome b-558 (Diebold and Bokoch, 2001), PLCbeta2 (Piechulek et al., 2005), nitric oxide synthase 2 (NOS2) (Kuncewicz et al., 2001) and Pak1 (Carstanjen et al., 2005).
Expression Expression is restricted to hematopoietic cells and exhibits the highest expression in myeloid cells. Rac2 expression is regulated during the differentiation of hematopoietic and myeloid cells. There is some data suggesting that Rac2 might be expressed in tumors.
Localisation Once activated Rac2 is mainly localized in endomembranes.
Function As suggested by its restricted expression, Rac2 has a specialized role in many hematopoietic and immunological processes. Rac2 deficient mice show defects in stem cells, mast cells as well as B and T cells.
Role in hematopoietic stem-cell progenitor engraftment
The contribution of the GTPase Rac2 to the normal functioning of hematopoietic stem-cell progenitors (HSC/Ps) was addressed based on the phenotype of Rac2-/- mice (Gu et al., 2003). HSC/Ps from these mice showed normal short-term engraftment, but decreased adhesion, suggesting a key role for Rac2 in integrin-mediated stem-cell adhesion. In addition, Rac2-/- HSC/Ps formed colonies with both impaired growth and migration, and showed an increased rate of apoptosis.
In response to stromal derived factor 1, Rac2-/- cells failed in cortical F-actin assembly, and presented reduced cell spreading and actin-based membrane protrusion.
Role in neutrophils function
Several reports point out Rac2 is the predominant Rac GTPase functioning in neutrophils. These observations came from studies in neutrophils from Rac2-/- mice and a patient with a dominant-negative Rac2 mutation in which these cells showed decreased motility, adhesion, major defects in cortical F-actin assembly, and accordingly, chemotaxis and reduced phagocytosis and superoxide production by NAPH oxidase (Williams et al., 2000; Roberts et al., 1999; Li et al., 2002; Gu et al., 2003). Rac2 is required for oxidase activity through its direct interaction with p67-phox and cytochrome b 558.
Role in B-cell development
Rac2-/- mice exhibit multiple defects in B-cell development, with reduced numbers of peripheral blood B-cells and IgM-secreting plasma cells, a severe reduction in the number of marginal zone and peritoneal B1 cells (Croker et al., 2002). Rac2 participates in the positive selection through the B-cell receptor (BCR), since is activated by BCR cross-linking (Grill and Schrader, 2002).
Role in T-cell differentiation
Rac2 activity is required for interferon-gamma (IFNgamma) production both in vitro and in vivo during normal T-cell activation and Th1-cell differentiation, through simultaneous activation of both the NFkappaB and p38 pathways (Li et al., 2000).
Role in Mast cell survival
The absence of Rac2 results in defects growth, survival, chemotaxis, adhesion, and degranulation in mast cell (Yang et al., 2000). Rac2 is critical in regulating the growth factor-induced survival through activation of Akt and a change in expression levels of the Bcl-2 family members BAD and Bcl-XL (Yang et al., 2000).
Homology Rac2 share significant sequence identity (~88%) with the other two members of the subfamily Rac: Rac1 and Rac3. The three proteins diverge primarily in the C-terminal 15 residues. Regarding to the biochemical properties, Rac2 shows a slower nucleotide association and is more efficiently activated by the Rac-GEF Tiam1 than Rac1 and Rac3.

Mutations

Note POLYMORPHISMS
Two single nucleotide polymorphisms (SNP) have been observed in gliomas (Idbaih et al., 2008). The SNPs rs2239774 in exon 2 (codon 27, GCC to GCG, Ala to Ala) and rs3179967 in exon 6 (codon 159, GCT to GCC, Ala to Ala) were observed in 15/78 and 7/78 cases, respectively. No association between these two SNPs with phenotype, tumor grade, patient age, and patient gender was seen.
Germinal A point mutation has been identified in one allele of the Rac2 gene resulting in the substitution of Asp57 by an Asn (Rac2D57N) in a patient with a primary immunodeficiency syndrome (Ambruso et al., 2000; Williams et al., 2000). Rac2D57N binds GDP but not GTP and inhibits oxidase activation and superoxide production in vitro.
Somatic So far only two studies have searched for the presence of somatic mutations, both of them analyzed human brain tumors. Hwang et al. found 26% of cases had Rac2 gene mutation, two cases with decreased Rac2 expression and four cases with normal Rac2 expression. One case showed the mutation site nearby the GTP-binding site, which may affect Rac2 GTPase activity, but the site of Rac2 mutation seems not to concentrate in the effector region. However, Idbaih et al. did not find missense mutations in a series of 78 gliomas.

Implicated in

Entity Immunodeficiency
Disease Lack of Rac2 activity causes immunodeficiency (Ambruso et al., 2000; Williams et al., 2000). A single patient was identified with a primary immunodeficiency syndrome resulting from a heterozygous mutation in the Rac2 gene. In the first 5 months after birth, the patient presented several bacterial infections, poor wound healing, and absence of pus in the wounds, indicative of a phagocyte defect. The neutrophils had decreased chemotactic motility, polarization, and secretion of azurophilic granules. Rac2 levels were reduced, suggesting a defect in this GTPase. Western blot analysis of lysates from patient neutrophils demonstrated decreased levels of Rac2 protein. Molecular analysis identified a point mutation in one allele of the Rac2 gene resulting in the substitution of Asp57 by an Asn (Rac2D57N). Rac2D57N inhibits oxidase activation and superoxide production in vitro. These data represent the description of an inhibitory mutation in a member of the Rho family of GTPases associated with a human immunodeficiency syndrome.
  
Entity Brain tumors
Oncogenesis Expression of Rac2 was examined by RT-PCR and Northern blotting in human brain tumors: 10 astrocytomas, 8 meningiomas, and 8 pituitary adenomas (Hwang et al., 2005). The overexpression of Rac2 was evident in 1/10 astrocytomas and 1/8 meningiomas. No overexpression was found in pituitary adenomas. The decreased expression of Rac2 was found in 15 of 26 brain tumors (8/10 astrocytomas, 2/8 meningiomas and 5/8 pituitary adenomas).
  
Entity Head and neck squamous cell cancer
Oncogenesis Western blot analysis showed increased expression of Rac2 in a malignant squamous cell cancer cell line and a premalignant dysplastic cell line compared to the normal human epidermal keratinocytes (Abraham et al., 2001). This observation was confirmed with an immunohistochemical study of 15 moderately to poorly differentiated head and neck squamous cell cancer specimens, where a specific increased expression of Rac2 in areas of squamous cell cancer compared to the normal tissue was observed. Rac2 shows nuclear staining in normal human epidermal keratinocytes increasing sequentially in premalignant and malignant cell lines. In addition, there is specific cytoplasmic staining of the malignant cancer cell line which is absent in the normal and premalignant cell lines. This differential cytoplasmic staining may be able to distinguish invasive squamous cell carcinoma from dysplastic lesions and benign normal mucosa. Consequently it has been proposed that this GTPase could have an important role in the diagnosis and staging of this tumor type.
  
Entity Acute myeloid leukemia (AML)
Oncogenesis Activating mutations of KIT, which encodes the receptor for the cytokine stem cell factor, have been described in acute myeloid leukemia. Genetic disruption of Rac2 or pharmacologic evidence through treatment with Rac inhibitor NC23766, implicate Rac2 in regulating KIT-induced transformation in acute myeloid leukaemia (Munugalavadla et al., 2007). These results suggest Rac2 as a potential novel therapeutic target for the treatment of KIT-bearing acute myeloid leukemia.
  
Entity Chronic myelogenous leukemia (CML)
Oncogenesis Gene targeting of Rac1 and Rac2 significantly delays or abrogates development of chronic myelogenous leukemia (CML), a clonal myeloproliferative disease (MPD) initiated by expression of the p210-BCR- ABL fusion protein (Thomas et al., 2007). These genetic data were further substantiated experimentally by use of NSC23766, small molecule antagonist of Rac activation, to validate biochemically and functionally Rac as a molecular target in both a relevant animal model and in primary human CML cells in vitro and in a xenograft model in vivo. These findings indicate that Rac GTPases are critical for p210-BCR-ABL-mediated transformation and, therefore, suggest that the Rac GTPases may prove to be useful therapeutically by targeting alternative signaling pathways, which may be responsible for resistance and relapse in CML.
  

External links

Nomenclature
HGNC (Hugo)RAC2   9802
Cards
AtlasRAC2ID42021ch22q13
Entrez_Gene (NCBI)RAC2  5880  ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)
GeneCards (Weizmann)RAC2
Ensembl (Hinxton)ENSG00000128340 [Gene_View]  chr22:37621301-37640339 [Contig_View]  RAC2 [Vega]
AceView (NCBI)RAC2
Genatlas (Paris)RAC2
WikiGenes5880
SOURCE (Princeton)NM_002872
Genomic and cartography
GoldenPath (UCSC)RAC2  -  22q13.1   chr22:37621301-37640339 -  22q13.1   [Description]    (hg19-Feb_2009)
EnsemblRAC2 - 22q13.1 [CytoView]
Mapping of homologs : NCBIRAC2 [Mapview]
OMIM602049   608203   
Gene and transcription
Genbank (Entrez)AF077208 AF498965 AK096924 BC001485 BC018735
RefSeq transcript (Entrez)NM_002872
RefSeq genomic (Entrez)AC_000154 NC_000022 NC_018933 NG_007288 NT_011520 NW_001838745 NW_004929430
Consensus coding sequences : CCDS (NCBI)RAC2
Cluster EST : UnigeneHs.517601 [ NCBI ]
CGAP (NCI)Hs.517601
Alternative Splicing : Fast-db (Paris)GSHG0020372
Alternative Splicing GalleryENSG00000128340
Gene ExpressionRAC2 [ NCBI-GEO ]     RAC2 [ SEEK ]   RAC2 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP15153 (Uniprot)
NextProtP15153  [Medical]
With graphics : InterProP15153
Splice isoforms : SwissVarP15153 (Swissvar)
Domaine pattern : Prosite (Expaxy)RHO (PS51420)   
Domains : Interpro (EBI)P-loop_NTPase    Small_GTP-bd_dom    Small_GTPase    Small_GTPase_Rho   
Related proteins : CluSTrP15153
Domain families : Pfam (Sanger)Ras (PF00071)   
Domain families : Pfam (NCBI)pfam00071   
Domain families : Smart (EMBL)RHO (SM00174)  
DMDM Disease mutations5880
Blocks (Seattle)P15153
PDB (SRS)1DS6    2W2T    2W2V    2W2X   
PDB (PDBSum)1DS6    2W2T    2W2V    2W2X   
PDB (IMB)1DS6    2W2T    2W2V    2W2X   
PDB (RSDB)1DS6    2W2T    2W2V    2W2X   
Human Protein AtlasENSG00000128340
Peptide AtlasP15153
HPRD03628
IPIIPI00010270   IPI00877816   IPI00879948   IPI00878066   IPI00877663   
Protein Interaction databases
DIP (DOE-UCLA)P15153
IntAct (EBI)P15153
FunCoupENSG00000128340
BioGRIDRAC2
InParanoidP15153
Interologous Interaction database P15153
IntegromeDBRAC2
STRING (EMBL)RAC2
Ontologies - Pathways
Ontology : AmiGOGTPase activity  GTP binding  nuclear envelope  cytosol  plasma membrane  signal transduction  small GTPase mediated signal transduction  axon guidance  blood coagulation  positive regulation of cell proliferation  regulation of hydrogen peroxide metabolic process  cell projection assembly  actin cytoskeleton organization  platelet activation  bone resorption  regulation of small GTPase mediated signal transduction  regulation of respiratory burst  
Ontology : EGO-EBIGTPase activity  GTP binding  nuclear envelope  cytosol  plasma membrane  signal transduction  small GTPase mediated signal transduction  axon guidance  blood coagulation  positive regulation of cell proliferation  regulation of hydrogen peroxide metabolic process  cell projection assembly  actin cytoskeleton organization  platelet activation  bone resorption  regulation of small GTPase mediated signal transduction  regulation of respiratory burst  
Pathways : KEGGMAPK signaling pathway    Ras signaling pathway    Rap1 signaling pathway    Chemokine signaling pathway    Wnt signaling pathway    Axon guidance    VEGF signaling pathway    Focal adhesion    Adherens junction    Natural killer cell mediated cytotoxicity    B cell receptor signaling pathway    Fc epsilon RI signaling pathway    Fc gamma R-mediated phagocytosis    Leukocyte transendothelial migration    Regulation of actin cytoskeleton    Pathways in cancer    Colorectal cancer    Pancreatic cancer    Viral myocarditis   
REACTOMERAC2
Protein Interaction DatabaseRAC2
Wikipedia pathwaysRAC2
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)RAC2
SNP (GeneSNP Utah)RAC2
SNP : HGBaseRAC2
Genetic variants : HAPMAPRAC2
1000_GenomesRAC2 
ICGC programENSG00000128340 
Somatic Mutations in Cancer : COSMICRAC2 
CONAN: Copy Number AnalysisRAC2 
Mutations and Diseases : HGMDRAC2
OMIM602049    608203   
GENETestsRAC2
Disease Genetic AssociationRAC2
Huge Navigator RAC2 [HugePedia]  RAC2 [HugeCancerGEM]
Genomic VariantsRAC2  RAC2 [DGVbeta]
Exome VariantRAC2
dbVarRAC2
ClinVarRAC2
snp3D : Map Gene to Disease5880
General knowledge
Homologs : HomoloGeneRAC2
Homology/Alignments : Family Browser (UCSC)RAC2
Phylogenetic Trees/Animal Genes : TreeFamRAC2
Chemical/Protein Interactions : CTD5880
Chemical/Pharm GKB GenePA34163
Clinical trialRAC2
Cancer Resource (Charite)ENSG00000128340
Other databases
Probes
Litterature
PubMed95 Pubmed reference(s) in Entrez
CoreMineRAC2
iHOPRAC2

Bibliography

Abr and Bcr are multifunctional regulators of the Rho GTP-binding protein family.
Chuang TH, Xu X, Kaartinen V, Heisterkamp N, Groffen J, Bokoch GM.
Proc Natl Acad Sci U S A 1995; 92: 10282-6.
PMID 7479768
 
Structure and chromosomal assignment to 22q12 and 17qter of the ras-related Rac2 and Rac3 human genes.
Courjal F, Chuchana P, Theillet C, Fort P.
Genomics 1997; 44: 242-246.
PMID 9299243
 
Deficiency of the hematopoietic cell-specific Rho family GTPase Rac2 is characterized by abnormalities in neutrophil function and host defense.
Roberts AW, Kim C, Zhen L, Lowe JB, Kapur R, Petryniak B, Spaetti A, Pollock JD, Borneo JB, Bradford GB, Atkinson SJ, Dinauer MC, Williams DA.
Immunity 1999; 10: 183-196.
PMID 10072071
 
Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation.
Ambruso DR, Knall C, Abell AN, Panepinto J, Kurkchubasche A, Thurman G, Gonzalez-Aller C, Hiester A, deBoer M, Harbeck RJ, Oyer R, Johnson GL, Roos D.
Proc Natl Acad Sci USA 2000, 97: 4654-4659.
PMID 10758162
 
Role of the guanosine triphosphatase Rac2 in T helper 1 cell differentiation.
Li B, Yu H, Zheng W, Voll R, Na S, Roberts AW, Williams DA, Davis RJ, Ghosh S, Flavell RA.
Science 2000; 288: 2219-2222.
PMID 10864872
 
Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency.
Williams DA, Tao W, Yang F, Kim C, Gu Y, Mansfield P, Levine JE, Petryniak B, Derrow CW, Harris C, Jia B, Zheng Y, Ambruso DR, Lowe JB, Atkinson SJ, Dinauer MC, Boxer L.
Blood 2000; 96: 1646-1654.
PMID 10961859
 
Rac2 stimulates Akt activation affecting BAD/Bcl-XL expression while mediating survival and actin function in primary mast cells.
Yang FC, Kapur R, King AJ, Tao W, Kim C, Borneo J, Breese R, Marshall M, Dinauer MC, Williams DA.
Immunity 2000; 12: 557-568.
PMID 10843388
 
Motility-related proteins as markers for head and neck squamous cell cancer.
Abraham MT, Kuriakose MA, Sacks PG, Yee H, Chiriboga L, Bearer EL, Delacure MD.
Laryngoscope 2001;111: 1285-1289.
PMID 11568556
 
Molecular basis for Rac2 regulation of phagocyte NADPH oxidase.
Diebold BA, Bokoch GM.
Nat Immunol 2001; 2: 211-215.
PMID 11224519
 
Specific association of nitric oxide synthase-2 with Rac isoforms in activated murine macrophages.
Kuncewicz T, Balakrishnan P, Snuggs MB, Kone BC.
Am J Physiol Renal Physiol 2001; 281: F326-F336.
PMID 11457725
 
The Rac2 guanosine triphosphatase regulates B lymphocyte antigen receptor responses and chemotaxis and is required for establishment of B-1a and marginal zone B lymphocytes.
Croker BA, Tarlinton DM, Cluse LA, Tuxen AJ, Light A, Yang FC, Williams DA, Roberts AW.
J Immunol 2002; 168: 3376-3386.
PMID 11907095
 
Activation of Rac-1, Rac-2, and Cdc42 by hemopoietic growth factors or cross-linking of the B-lymphocyte receptor for antigen.
Grill B, Schrader JW.
Blood 2002; 100: 3183-3192.
PMID 12384416
 
DOCK2 mediates T cell receptor-induced activation of Rac2 and IL-2 transcription.
Nishihara H, Maeda M, Tsuda M, Makino Y, Sawa H, Nagashima K, Tanaka S.
Biochem Biophys Res Commun 2002; 296: 716-720.
PMID 12176041
 
P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac.
Welch HC, Coadwell WJ, Ellson CD, Ferguson GJ, Andrews SR, Erdjument-Bromage H, Tempst P, Hawkins PT, Stephens LR.
Cell 2002; 108: 809-821.
PMID 11955434
 
Comparative functional analysis of the Rac GTPases.
Haeusler LC, Blumenstein L, Stege P, Dvorsky R, Ahmadian MR.
FEBS Lett 2003; 555: 556-560.
PMID 14675773
 
Hematopoietic cell regulation by Rac1 and Rac2 guanosine triphosphatases.
Gu Y, Filippi MD, Cancelas JA, Siefring JE, Williams EP, Jasti AC, Harris CE, Lee AW, Prabhakar R, Atkinson SJ, Kwiatkowski DJ, Williams DA.
Science 2003; 302: 445-449.
PMID 14564009
 
Identification of a genomic fragment that directs hematopoietic-specific expression of Rac2 and analysis of the DNA methylation profile of the gene locus.
Ladd PD, Butler JS, Skalnik DG.
Gene 2004; 341: 323-333.
PMID 15474314
 
SWAP-70 regulates c-kit-induced mast cell activation, cell-cell adhesion, and migration.
Sivalenka RR, Jessberger R.
Mol Cell Biol 2004; 24: 10277-10288.
PMID 15542837
 
Rac2 regulates neutrophil chemotaxis, superoxide production, and myeloid colony formation through multiple distinct effector pathways.
Carstanjen D, Yamauchi A, Koornneef A, Zang H, Filippi MD, Harris C, Towe J, Atkinson S, Zheng Y, Dinauer MC, Williams DA.
J Immunol 2005; 174: 4613-4620.
PMID 15814684
 
Rho GTPase expression in tumourigenesis: evidence for a significant link.
Gómez del Pulgar T, Benitah SA, Valerón PF, Espina C, Lacal JC.
Bioessays 2005; 27: 602-613. (REVIEW)
PMID 15892119
 
Rac2 expression and mutation in human brain tumors.
Hwang SL, Lieu AS, Chang JH, Cheng TS, Cheng CY, Lee KS, Lin CL, Howng SL, Hong YR.
Acta Neurochir (Wien) 2005; 147: 551-554.
PMID 15812594
 
Isozyme-specific stimulation of phospholipase C-gamma2 by Rac GTPases.
Piechulek T, Rehlen T, Walliser C, Vatter P, Moepps B, Gierschik P.
J Biol Chem 2005; 280: 38923-38931.
PMID 16172125
 
The Rac effector p67phox regulates phagocyte NADPH oxidase by stimulating Vav1 guanine nucleotide exchange activity.
Ming W, Li S, Billadeau DD, Quilliam LA, Dinauer MC.
Mol Cell Biol 2007; 27: 312-323.
PMID 17060455
 
Genetic and pharmacologic evidence implicating the p85 alpha, but not p85 beta, regulatory subunit of PI3K and Rac2 GTPase in regulating oncogenic KIT-induced transformation in acute myeloid leukemia and systemic mastocytosis.
Munugalavadla V, Sims EC, Borneo J, Chan RJ, Kapur R.
Blood 2007; 110: 1612-1620.
PMID 17483298
 
Rac guanosine triphosphatases represent integrating molecular therapeutic targets for BCR-ABL-induced myeloproliferative disease.
Thomas EK, Cancelas JA, Chae HD, Cox AD, Keller PJ, Perrotti D, Neviani P, Druker BJ, Setchell KD, Zheng Y, Harris CE, Williams DA.
Cancer Cell 2007; 12: 467-478.
PMID 17996650
 
Mutational analysis of Rac2 in gliomas.
Idbaih A, Paris S, Boisselier B, Marie Y, Sanson M, Thillet J, Hoang-Xuan K, Delattre JY.
J Neurooncol 2008; 87: 365-366.
PMID 18217210
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Contributor(s)

Written08-2008Teresa Gómez del Pulgar, Juan Carlos Lacal
Centro Nacional de Biotecnología (CNB), Darwin 3, 28049 Madrid, Spain

Citation

This paper should be referenced as such :
Gómez del Pulgar T, Lacal JC . RAC2 (ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)). Atlas Genet Cytogenet Oncol Haematol. August 2008 .
URL : http://AtlasGeneticsOncology.org/Genes/RAC2ID42021ch22q13.html

The various updated versions of this paper are referenced and archived by INIST as such :
http://documents.irevues.inist.fr/bitstream/2042/44516/1/08-2008-RAC2ID42021ch22q13.pdf   [ Bibliographic record ]

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indexed on : Fri Apr 18 17:32:04 CEST 2014

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