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Ras-related C3 botulinum toxin substrate 2 (GX) (Small G protein) (p21-Rac2)

 RAC2_HUMAN              Reviewed;         192 AA.
P15153; Q9UDJ4;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 197.
RecName: Full=Ras-related C3 botulinum toxin substrate 2;
AltName: Full=GX;
AltName: Full=Small G protein;
AltName: Full=p21-Rac2;
Flags: Precursor;
Name=RAC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2674130;
Didsbury J., Weber R.F., Bokoch G.M., Evans T., Snyderman R.;
"Rac, a novel ras-related family of proteins that are botulinum toxin
substrates.";
J. Biol. Chem. 264:16378-16382(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 6-15; 97-107 AND 134-165.
PubMed=1316893;
Mizuno T., Kaibuchi K., Ando S., Musha T., Hiraoka K., Takaishi K.,
Asada M., Nunoi H., Matsuda I., Takai Y.;
"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. 267:10215-10218(1992).
[8]
PROTEIN SEQUENCE OF 7-16; 19-49; 154-163 AND 175-183, AND FUNCTION.
TISSUE=Neutrophil;
PubMed=1660188; DOI=10.1126/science.1660188;
Knaus U.G., Heyworth P.G., Evans T., Curnutte J.T., Bokoch G.M.;
"Regulation of phagocyte oxygen radical production by the GTP-binding
protein Rac 2.";
Science 254:1512-1515(1991).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 13-192.
PubMed=1902092; DOI=10.1016/0006-291X(91)91585-Z;
Reibel L., Dorseuil O., Stancou R., Bertoglio J., Gacon G.;
"A hemopoietic specific gene encoding a small GTP binding protein is
overexpressed during T cell activation.";
Biochem. Biophys. Res. Commun. 175:451-458(1991).
[10]
PROTEIN SEQUENCE OF 97-102 AND 167-174.
TISSUE=Neutrophil;
PubMed=8504089; DOI=10.1021/bi00072a029;
Kwong C.H., Malech H.L., Rotrosen D., Leto T.L.;
"Regulation of the human neutrophil NADPH oxidase by rho-related G-
proteins.";
Biochemistry 32:5711-5717(1993).
[11]
ISOPRENYLATION AT CYS-189, AND MUTAGENESIS OF CYS-189.
PubMed=1903399;
Kinsella B.T., Erdman R.A., Maltese W.A.;
"Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins
encoded by rac1, rac2, and ralA.";
J. Biol. Chem. 266:9786-9794(1991).
[12]
INTERACTION WITH DOCK2.
PubMed=10559471; DOI=10.1016/S0167-4889(99)00133-0;
Nishihara H., Kobayashi S., Hashimoto Y., Ohba F., Mochizuki N.,
Kurata T., Nagashima K., Matsuda M.;
"Non-adherent cell-specific expression of DOCK2, a member of the human
CDM-family proteins.";
Biochim. Biophys. Acta 1452:179-187(1999).
[13]
INTERACTION WITH S100A8 AND CALPROTECTIN.
PubMed=15642721; DOI=10.1096/fj.04-2377fje;
Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C.,
Doussiere J.;
"The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase
activation by interaction with p67phox and Rac-2.";
FASEB J. 19:467-469(2005).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
GLYCOSYLATION AT TYR-32 (MICROBIAL INFECTION).
PubMed=24141704; DOI=10.1038/nsmb.2688;
Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
Aktories K.;
"A bacterial toxin catalyzing tyrosine glycosylation of Rho and
deamidation of Gq and Gi proteins.";
Nat. Struct. Mol. Biol. 20:1273-1280(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH ARHGDIB.
PubMed=10655614; DOI=10.1038/72392;
Scheffzek K., Stephan I., Jensen O.N., Illenberger D., Gierschik P.;
"The Rac-RhoGDI complex and the structural basis for the regulation of
Rho proteins by RhoGDI.";
Nat. Struct. Biol. 7:122-126(2000).
[19]
VARIANT NEUID ASN-57.
PubMed=10758162; DOI=10.1073/pnas.080074897;
Ambruso D.R., Knall C., Abell A.N., Panepinto J., Kurkchubasche A.,
Thurman G., Gonzalez-Aller C., Hiester A., deBoer M., Harbeck R.J.,
Oyer R., Johnson G.L., Roos D.;
"Human neutrophil immunodeficiency syndrome is associated with an
inhibitory Rac2 mutation.";
Proc. Natl. Acad. Sci. U.S.A. 97:4654-4659(2000).
[20]
VARIANT [LARGE SCALE ANALYSIS] LEU-29.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Plasma membrane-associated small GTPase which cycles
between an active GTP-bound and inactive GDP-bound state. In
active state binds to a variety of effector proteins to regulate
cellular responses, such as secretory processes, phagocytose of
apoptotic cells and epithelial cell polarization. Augments the
production of reactive oxygen species (ROS) by NADPH oxidase.
{ECO:0000269|PubMed:1660188}.
-!- ENZYME REGULATION: 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.
-!- SUBUNIT: Interacts with DOCK2, which may activate it. Interacts
with S100A8 and calprotectin (S100A8/9).
{ECO:0000269|PubMed:10559471, ECO:0000269|PubMed:15642721}.
-!- INTERACTION:
O14939:PLD2; NbExp=4; IntAct=EBI-489652, EBI-1053996;
Q6P589:TNFAIP8L2; NbExp=2; IntAct=EBI-489652, EBI-9073209;
-!- SUBCELLULAR LOCATION: Cytoplasm. Note=Membrane-associated when
activated.
-!- TISSUE SPECIFICITY: Hematopoietic specific.
-!- PTM: (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 Rac and leads to actin
disassembly. {ECO:0000269|PubMed:24141704}.
-!- DISEASE: Neutrophil immunodeficiency syndrome (NEUID)
[MIM:608203]: An immunodeficiency syndrome due to defective
neutrophils. Affected individuals present with leukocytosis,
neutrophilia, severe recurrent bacterial infections and poor wound
healing. {ECO:0000269|PubMed:10758162}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RAC2ID42021ch22q13.html";
-!- WEB RESOURCE: Name=RAC2base; Note=RAC2 mutation db;
URL="http://structure.bmc.lu.se/idbase/RAC2base/";
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EMBL; M29871; AAA36538.1; -; mRNA.
EMBL; AF498965; AAM21112.1; -; mRNA.
EMBL; CR456555; CAG30441.1; -; mRNA.
EMBL; BT006919; AAP35565.1; -; mRNA.
EMBL; Z82188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001485; AAH01485.1; -; mRNA.
EMBL; M64595; AAA35941.1; -; mRNA.
CCDS; CCDS13945.1; -.
PIR; B34386; B34386.
RefSeq; NP_002863.1; NM_002872.4.
UniGene; Hs.517601; -.
PDB; 1DS6; X-ray; 2.35 A; A=1-192.
PDB; 2W2T; X-ray; 1.95 A; A=2-179.
PDB; 2W2V; X-ray; 2.00 A; A/B/C/D=1-177.
PDB; 2W2X; X-ray; 2.30 A; A/B=2-179.
PDBsum; 1DS6; -.
PDBsum; 2W2T; -.
PDBsum; 2W2V; -.
PDBsum; 2W2X; -.
ProteinModelPortal; P15153; -.
SMR; P15153; -.
BioGrid; 111818; 24.
DIP; DIP-34291N; -.
IntAct; P15153; 16.
MINT; MINT-1616362; -.
STRING; 9606.ENSP00000249071; -.
ChEMBL; CHEMBL5581; -.
DrugBank; DB00514; Dextromethorphan.
iPTMnet; P15153; -.
PhosphoSitePlus; P15153; -.
SwissPalm; P15153; -.
DMDM; 131806; -.
EPD; P15153; -.
MaxQB; P15153; -.
PaxDb; P15153; -.
PeptideAtlas; P15153; -.
PRIDE; P15153; -.
DNASU; 5880; -.
Ensembl; ENST00000249071; ENSP00000249071; ENSG00000128340.
GeneID; 5880; -.
KEGG; hsa:5880; -.
UCSC; uc003arc.5; human.
CTD; 5880; -.
DisGeNET; 5880; -.
EuPathDB; HostDB:ENSG00000128340.14; -.
GeneCards; RAC2; -.
HGNC; HGNC:9802; RAC2.
HPA; CAB022946; -.
HPA; HPA047820; -.
MalaCards; RAC2; -.
MIM; 602049; gene.
MIM; 608203; phenotype.
neXtProt; NX_P15153; -.
OpenTargets; ENSG00000128340; -.
Orphanet; 183707; Neutrophil immunodeficiency syndrome.
PharmGKB; PA34163; -.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000118978; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; P15153; -.
KO; K07860; -.
OMA; RRGCSIF; -.
OrthoDB; EOG091G0KCM; -.
PhylomeDB; P15153; -.
TreeFam; TF101109; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-4086400; PCP/CE pathway.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
SignaLink; P15153; -.
SIGNOR; P15153; -.
ChiTaRS; RAC2; human.
EvolutionaryTrace; P15153; -.
GeneWiki; RAC2; -.
GenomeRNAi; 5880; -.
PRO; PR:P15153; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000128340; -.
CleanEx; HS_RAC2; -.
ExpressionAtlas; P15153; baseline and differential.
Genevisible; P15153; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
GO; GO:0019887; F:protein kinase regulator activity; IEA:Ensembl.
GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0030031; P:cell projection assembly; IEA:Ensembl.
GO; GO:0006935; P:chemotaxis; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0071593; P:lymphocyte aggregation; IMP:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:UniProtKB.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0010810; P:regulation of cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; TAS:BHF-UCL.
GO; GO:0060753; P:regulation of mast cell chemotaxis; IEA:Ensembl.
GO; GO:0043304; P:regulation of mast cell degranulation; IEA:Ensembl.
GO; GO:1902622; P:regulation of neutrophil migration; IMP:UniProtKB.
GO; GO:0060263; P:regulation of respiratory burst; IDA:BHF-UCL.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; Glycoprotein;
GTP-binding; Lipoprotein; Methylation; Nucleotide-binding;
Polymorphism; Prenylation; Reference proteome.
CHAIN 1 189 Ras-related C3 botulinum toxin substrate
2.
/FTId=PRO_0000042046.
PROPEP 190 192 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000042047.
NP_BIND 10 17 GTP. {ECO:0000250}.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 115 118 GTP. {ECO:0000250}.
MOTIF 32 40 Effector region. {ECO:0000255}.
MOD_RES 39 39 ADP-ribosylasparagine; by botulinum
toxin. {ECO:0000250}.
MOD_RES 147 147 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 189 189 Cysteine methyl ester. {ECO:0000250}.
LIPID 189 189 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:1903399}.
CARBOHYD 32 32 O-linked (GlcNAc) tyrosine; by
Photorhabdus PAU_02230.
{ECO:0000269|PubMed:24141704}.
VARIANT 29 29 P -> L (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036569.
VARIANT 57 57 D -> N (in NEUID; dominant-negative
mutant; binds GDP, but not GTP; inhibits
oxidase activation and superoxide anion
production in vitro; dbSNP:rs74315507).
{ECO:0000269|PubMed:10758162}.
/FTId=VAR_017452.
MUTAGEN 189 189 C->W: Abolishes in vitro prenylation.
{ECO:0000269|PubMed:1903399}.
STRAND 3 11 {ECO:0000244|PDB:2W2T}.
HELIX 16 25 {ECO:0000244|PDB:2W2T}.
STRAND 39 46 {ECO:0000244|PDB:2W2T}.
STRAND 49 56 {ECO:0000244|PDB:2W2T}.
HELIX 62 64 {ECO:0000244|PDB:2W2T}.
TURN 65 67 {ECO:0000244|PDB:2W2T}.
HELIX 68 71 {ECO:0000244|PDB:2W2T}.
STRAND 77 83 {ECO:0000244|PDB:2W2T}.
HELIX 87 95 {ECO:0000244|PDB:2W2T}.
HELIX 97 104 {ECO:0000244|PDB:2W2T}.
STRAND 106 108 {ECO:0000244|PDB:2W2T}.
STRAND 110 115 {ECO:0000244|PDB:2W2T}.
HELIX 117 119 {ECO:0000244|PDB:2W2T}.
HELIX 123 130 {ECO:0000244|PDB:2W2T}.
TURN 131 133 {ECO:0000244|PDB:2W2T}.
HELIX 139 149 {ECO:0000244|PDB:2W2T}.
STRAND 152 156 {ECO:0000244|PDB:2W2T}.
TURN 159 161 {ECO:0000244|PDB:2W2T}.
HELIX 165 175 {ECO:0000244|PDB:2W2T}.
SEQUENCE 192 AA; 21429 MW; 2A1F1266B07C3210 CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP VNLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRAKWFPE VRHHCPSTPI ILVGTKLDLR
DDKDTIEKLK EKKLAPITYP QGLALAKEID SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ
PTRQQKRACS LL


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Catalog number Product name Quantity
RAC2 RAC2 Gene ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)
201-20-4719 RAC2{ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)}rabbit.pAb 0.2ml
201-20-6722 RAC2{ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)}mouse.mAb 0.2ml
EIAAB33637 GX,Homo sapiens,Human,p21-Rac2,RAC2,Ras-related C3 botulinum toxin substrate 2,Small G protein
201-20-0064 RAC2{ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)}goat.pAb 0.2ml
CSB-EL019248GU Guinea pig ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2) (RAC2) ELISA kit, Species Guinea pig, Sample Type serum, plasma 96T
CSB-EL019248BO Bovine ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2) (RAC2) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL019248HU Human ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2) (RAC2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL019248MO Mouse ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2) (RAC2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
GS-1815a ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2) primary antibody, Host: Rabbit 200ul
EIAAB33636 Mouse,Mus musculus,p21-Rac2,Protein EN-7,Rac2,Ras-related C3 botulinum toxin substrate 2
OBT1390 ras_related C3 botulinum toxin substrate 2 (RAC2) [rho family, small GTP binding protein Rac2], EN_7, ~20kD, Goat anti_; WB 100 µg.
EIAAB33635 Bos taurus,Bovine,p21-Rac2,RAC2,Ras-related C3 botulinum toxin substrate 2
CSB-PA019248GA01HU Rabbit anti-human ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA019248GA01HU Rabbit anti-human ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
pro-719 Recombinant Human Ras-Related C3 Botulinum Toxin Substrate 2 (1-189) RAC2 (189) 20
pro-619 Recombinant Human Ras-Related C3 Botulinum Toxin Substrate 2 RAC2 20
pro-719 Recombinant Human Ras-Related C3 Botulinum Toxin Substrate 2 (1-189) RAC2 (189) 5
pro-619 Recombinant Human Ras-Related C3 Botulinum Toxin Substrate 2 RAC2 5
pro-719 Recombinant Human Ras-Related C3 Botulinum Toxin Substrate 2 (1-189) RAC2 (189) 1mg
pro-619 Recombinant Human Ras-Related C3 Botulinum Toxin Substrate 2 RAC2 1mg
orb81299 Human Ras-Related C3 Botulinum Toxin substrate His Tag protein Ras-Related C3 Botulinum Toxin substrate Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 10
orb81298 Human Ras-Related C3 Botulinum Toxin substrate 1 protein Ras-Related C3 Botulinum Toxin substrate Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 192 am 10
G6454 Ras-related C3 botulinum toxin substrate 2 (RAC2), Mouse, ELISA Kit 96T
CSB-EL019248HU Human Ras-related C3 botulinum toxin substrate 2(RAC2) ELISA kit 96T


 

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