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Reviewed, UniProtKB/Swiss-Prot P15153 (RAC2_HUMAN)

Last modified February 9, 2010. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ras-related C3 botulinum toxin substrate 2
Alternative name(s):
    p21-Rac2
    Small G protein
    GX
Gene names
Name: RAC2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

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. Seems to be involved in the regulation of the NADPH oxidase.

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 structure

Interacts with DOCK2, which may activate it. Ref.10

Subcellular location

Cytoplasm. Note: Membrane-associated when activated.

Tissue specificity

Hematopoietic specific.

Involvement in disease

Defects in RAC2 are the cause of neutrophil immunodeficiency syndrome [MIM:608203]. Ref.15

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCF2P198781EBI-489652,EBI-489611

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Ras-related C3 botulinum toxin substrate 2
PRO_0000042046
Propeptide190 – 1923Removed in mature form By similarity
PRO_0000042047

Regions

Nucleotide binding10 – 178GTP By similarity
Nucleotide binding57 – 615GTP By similarity
Nucleotide binding115 – 1184GTP By similarity
Motif32 – 409Effector region Potential

Amino acid modifications

Modified residue391ADP-ribosylasparagine; by botulinum toxin By similarity
Modified residue1471N6-acetyllysine Ref.13
Modified residue1891Cysteine methyl ester Probable
Lipidation1891S-geranylgeranyl cysteine Ref.11

Natural variations

Natural variant291P → L in a breast cancer sample; somatic mutation. Ref.16
VAR_036569
Natural variant571D → N in neutrophil immunodeficiency syndrome; dominant-negative mutant; binds GDP, but not GTP; inhibits oxidase activation and superoxide anion production in vitro. Ref.15
VAR_017452

Experimental info

Mutagenesis1891C → W: Abolishes in vitro prenylation. Ref.11

Secondary structure

1 ............................................ 192
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P15153-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 2A1F1266B07C3210

FASTA19221,429
        10         20         30         40         50         60 
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP VNLGLWDTAG 

        70         80         90        100        110        120 
QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRAKWFPE VRHHCPSTPI ILVGTKLDLR 

       130        140        150        160        170        180 
DDKDTIEKLK EKKLAPITYP QGLALAKEID SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ 

       190 
PTRQQKRACS LL

« Hide

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References

« Hide 'large scale' references
[1]"Rac, a novel ras-related family of proteins that are botulinum toxin substrates."
Didsbury J., Weber R.F., Bokoch G.M., Evans T., Snyderman R.
J. Biol. Chem. 264:16378-16382(1989) [PubMed: 2674130] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"A genome annotation-driven approach to cloning the human ORFeome."
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.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence of human chromosome 22."
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. expand/collapse author list , 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.
Nature 402:489-495(1999) [PubMed: 10591208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"A hemopoietic specific gene encoding a small GTP binding protein is overexpressed during T cell activation."
Reibel L., Dorseuil O., Stancou R., Bertoglio J., Gacon G.
Biochem. Biophys. Res. Commun. 175:451-458(1991) [PubMed: 1902092] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-192.
[8]"Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins."
Mizuno T., Kaibuchi K., Ando S., Musha T., Hiraoka K., Takaishi K., Asada M., Nunoi H., Matsuda I., Takai Y.
J. Biol. Chem. 267:10215-10218(1992) [PubMed: 1316893] [Abstract]
Cited for: PROTEIN SEQUENCE OF 6-15; 97-107 AND 134-165.
[9]"Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins."
Kwong C.H., Malech H.L., Rotrosen D., Leto T.L.
Biochemistry 32:5711-5717(1993) [PubMed: 8504089] [Abstract]
Cited for: PROTEIN SEQUENCE OF 97-102 AND 167-174.
Tissue: Neutrophil.
[10]"Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins."
Nishihara H., Kobayashi S., Hashimoto Y., Ohba F., Mochizuki N., Kurata T., Nagashima K., Matsuda M.
Biochim. Biophys. Acta 1452:179-187(1999) [PubMed: 10559471] [Abstract]
Cited for: INTERACTION WITH DOCK2.
[11]"Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA."
Kinsella B.T., Erdman R.A., Maltese W.A.
J. Biol. Chem. 266:9786-9794(1991) [PubMed: 1903399] [Abstract]
Cited for: ISOPRENYLATION AT CYS-189, MUTAGENESIS OF CYS-189.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, MASS SPECTROMETRY.
[14]"The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI."
Scheffzek K., Stephan I., Jensen O.N., Illenberger D., Gierschik P.
Nat. Struct. Biol. 7:122-126(2000) [PubMed: 10655614] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH ARHGDIB.
[15]"Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation."
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.
Proc. Natl. Acad. Sci. U.S.A. 97:4654-4659(2000) [PubMed: 10758162] [Abstract]
Cited for: VARIANT NEUTROPHIL IMMUNODEFICIENCY SYNDROME ASN-57.
[16]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-29.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M29871 mRNA. Translation: AAA36538.1.
AF498965 mRNA. Translation: AAM21112.1.
CR456555 mRNA. Translation: CAG30441.1.
BT006919 mRNA. Translation: AAP35565.1.
Z82188 Genomic DNA. Translation: CAB45265.1.
BC001485 mRNA. Translation: AAH01485.1.
M64595 mRNA. Translation: AAA35941.1.
IPIIPI00010270.
PIRB34386.
RefSeqNP_002863.1.
UniGeneHs.517601

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DS6X-ray2.35A1-192[»]
2W2TX-ray1.95A2-179[»]
2W2VX-ray2.00A/B/C/D1-177[»]
2W2XX-ray2.30A/B2-179[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP15153. 1 interaction.
STRINGP15153.

PTM databases

PhosphoSiteP15153.

Proteomic databases

PeptideAtlasP15153.
PRIDEP15153.

Genome annotation databases

EnsemblENST00000249071; ENSP00000249071; ENSG00000128340; Homo sapiens. [Genome view]
ENST00000458421; ENSP00000396686; ENSG00000128340; Homo sapiens. [Genome view]
GeneID5880.
KEGGhsa:5880.
UCSCuc003arc.1. human.

Organism-specific databases

CTD5880.
GeneCardsGC22M035945.
H-InvDBHIX0016439.
HGNCHGNC:9802. RAC2.
HPACAB022946.
MIM602049. gene.
608203. phenotype.
Orphanet183707. Neutrophil immunodeficiency syndrome.
PharmGKBPA34163.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG19849.
HOGENOMHBG745225.
HOVERGENP15153.
InParanoidP15153.
OMACPQPTRT.
OrthoDBEOG9X0QC9.
PhylomeDBP15153.

Enzyme and pathway databases

ReactomeREACT_11044. Signaling by Rho GTPases.
REACT_14797. Signaling by GPCR.
REACT_18266. Axon guidance.

Gene expression databases

ArrayExpressP15153.
BgeeP15153.
CleanExHS_RAC2.
GenevestigatorP15153.
GermOnlineENSG00000128340. Homo sapiens.

Family and domain databases

InterProIPR003578. GTPase_Rho.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio22854.
SOURCESearch...

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Entry information

Entry nameRAC2_HUMAN
AccessionPrimary (citable) accession number: P15153
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 9, 2010
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents