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Protein

Ras-related C3 botulinum toxin substrate 2

Gene

RAC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Enzyme regulationi

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi115 – 1184GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: ProtInc
  • GTP binding Source: UniProtKB
  • protein kinase regulator activity Source: Ensembl

GO - Biological processi

  • actin filament organization Source: UniProtKB
  • axon guidance Source: Reactome
  • blood coagulation Source: Reactome
  • bone resorption Source: Ensembl
  • cell projection assembly Source: Ensembl
  • G-protein coupled receptor signaling pathway Source: Ensembl
  • lymphocyte aggregation Source: UniProtKB
  • platelet activation Source: Reactome
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of lamellipodium assembly Source: UniProtKB
  • positive regulation of neutrophil chemotaxis Source: UniProtKB
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • regulation of cell-substrate adhesion Source: UniProtKB
  • regulation of hydrogen peroxide metabolic process Source: BHF-UCL
  • regulation of mast cell chemotaxis Source: Ensembl
  • regulation of mast cell degranulation Source: Ensembl
  • regulation of neutrophil migration Source: UniProtKB
  • regulation of respiratory burst Source: BHF-UCL
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • regulation of T cell proliferation Source: Ensembl
  • signal transduction Source: ProtInc
  • small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_1695. GPVI-mediated activation cascade.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_264199. PCP/CE pathway.
REACT_355141. RHO GTPases Activate NADPH Oxidases.
SignaLinkiP15153.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related C3 botulinum toxin substrate 2
Alternative name(s):
GX
Small G protein
p21-Rac2
Gene namesi
Name:RAC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:9802. RAC2.

Subcellular locationi

  • Cytoplasm

  • Note: Membrane-associated when activated.

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • nuclear envelope Source: Ensembl
  • phagocytic vesicle membrane Source: Reactome
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Neutrophil immunodeficiency syndrome (NEUID)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn immunodeficiency syndrome due to defective neutrophils. Affected individuals present with leukocytosis, neutrophilia, severe recurrent bacterial infections and poor wound healing.

See also OMIM:608203
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571D → N in NEUID; dominant-negative mutant; binds GDP, but not GTP; inhibits oxidase activation and superoxide anion production in vitro. 1 Publication
VAR_017452

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi189 – 1891C → W: Abolishes in vitro prenylation. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi608203. phenotype.
Orphaneti183707. Neutrophil immunodeficiency syndrome.
PharmGKBiPA34163.

Chemistry

DrugBankiDB00514. Dextromethorphan.

Polymorphism and mutation databases

DMDMi131806.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Ras-related C3 botulinum toxin substrate 2PRO_0000042046Add
BLAST
Propeptidei190 – 1923Removed in mature formBy similarityPRO_0000042047

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391ADP-ribosylasparagine; by botulinum toxinBy similarity
Modified residuei147 – 1471N6-acetyllysine1 Publication
Modified residuei189 – 1891Cysteine methyl esterBy similarity
Lipidationi189 – 1891S-geranylgeranyl cysteine1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP15153.
PaxDbiP15153.
PeptideAtlasiP15153.
PRIDEiP15153.

PTM databases

PhosphoSiteiP15153.

Expressioni

Tissue specificityi

Hematopoietic specific.

Gene expression databases

BgeeiP15153.
CleanExiHS_RAC2.
ExpressionAtlasiP15153. baseline and differential.
GenevisibleiP15153. HS.

Organism-specific databases

HPAiCAB022946.
HPA047820.

Interactioni

Subunit structurei

Interacts with DOCK2, which may activate it. Interacts with S100A8 and calprotectin (S100A8/9).2 Publications

Protein-protein interaction databases

BioGridi111818. 18 interactions.
DIPiDIP-34291N.
IntActiP15153. 12 interactions.
MINTiMINT-1616362.
STRINGi9606.ENSP00000249071.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi16 – 2510Combined sources
Beta strandi39 – 468Combined sources
Beta strandi49 – 568Combined sources
Helixi62 – 643Combined sources
Turni65 – 673Combined sources
Helixi68 – 714Combined sources
Beta strandi77 – 837Combined sources
Helixi87 – 959Combined sources
Helixi97 – 1048Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi110 – 1156Combined sources
Helixi117 – 1193Combined sources
Helixi123 – 1308Combined sources
Turni131 – 1333Combined sources
Helixi139 – 14911Combined sources
Beta strandi152 – 1565Combined sources
Turni159 – 1613Combined sources
Helixi165 – 17511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DS6X-ray2.35A1-192[»]
2W2TX-ray1.95A2-179[»]
2W2VX-ray2.00A/B/C/D1-177[»]
2W2XX-ray2.30A/B2-179[»]
ProteinModelPortaliP15153.
SMRiP15153. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15153.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector regionSequence Analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP15153.
KOiK07860.
OMAiSYENVHA.
OrthoDBiEOG764747.
PhylomeDBiP15153.
TreeFamiTF101109.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP
60 70 80 90 100
VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRAKWFPE
110 120 130 140 150
VRHHCPSTPI ILVGTKLDLR DDKDTIEKLK EKKLAPITYP QGLALAKEID
160 170 180 190
SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ PTRQQKRACS LL
Length:192
Mass (Da):21,429
Last modified:April 1, 1990 - v1
Checksum:i2A1F1266B07C3210
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291P → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_036569
Natural varianti57 – 571D → N in NEUID; dominant-negative mutant; binds GDP, but not GTP; inhibits oxidase activation and superoxide anion production in vitro. 1 Publication
VAR_017452

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13945.1.
PIRiB34386.
RefSeqiNP_002863.1. NM_002872.4.
UniGeneiHs.517601.

Genome annotation databases

EnsembliENST00000249071; ENSP00000249071; ENSG00000128340.
GeneIDi5880.
KEGGihsa:5880.
UCSCiuc003arc.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
RAC2base

RAC2 mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13945.1.
PIRiB34386.
RefSeqiNP_002863.1. NM_002872.4.
UniGeneiHs.517601.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DS6X-ray2.35A1-192[»]
2W2TX-ray1.95A2-179[»]
2W2VX-ray2.00A/B/C/D1-177[»]
2W2XX-ray2.30A/B2-179[»]
ProteinModelPortaliP15153.
SMRiP15153. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111818. 18 interactions.
DIPiDIP-34291N.
IntActiP15153. 12 interactions.
MINTiMINT-1616362.
STRINGi9606.ENSP00000249071.

Chemistry

ChEMBLiCHEMBL5581.
DrugBankiDB00514. Dextromethorphan.

PTM databases

PhosphoSiteiP15153.

Polymorphism and mutation databases

DMDMi131806.

Proteomic databases

MaxQBiP15153.
PaxDbiP15153.
PeptideAtlasiP15153.
PRIDEiP15153.

Protocols and materials databases

DNASUi5880.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249071; ENSP00000249071; ENSG00000128340.
GeneIDi5880.
KEGGihsa:5880.
UCSCiuc003arc.3. human.

Organism-specific databases

CTDi5880.
GeneCardsiGC22M037621.
HGNCiHGNC:9802. RAC2.
HPAiCAB022946.
HPA047820.
MIMi602049. gene.
608203. phenotype.
neXtProtiNX_P15153.
Orphaneti183707. Neutrophil immunodeficiency syndrome.
PharmGKBiPA34163.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP15153.
KOiK07860.
OMAiSYENVHA.
OrthoDBiEOG764747.
PhylomeDBiP15153.
TreeFamiTF101109.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_1695. GPVI-mediated activation cascade.
REACT_18407. G alpha (12/13) signalling events.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_264199. PCP/CE pathway.
REACT_355141. RHO GTPases Activate NADPH Oxidases.
SignaLinkiP15153.

Miscellaneous databases

ChiTaRSiRAC2. human.
EvolutionaryTraceiP15153.
GeneWikiiRAC2.
GenomeRNAii5880.
NextBioi22854.
PROiP15153.
SOURCEiSearch...

Gene expression databases

BgeeiP15153.
CleanExiHS_RAC2.
ExpressionAtlasiP15153. baseline and differential.
GenevisibleiP15153. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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. 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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 6-15; 97-107 AND 134-165.
  8. "Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2."
    Knaus U.G., Heyworth P.G., Evans T., Curnutte J.T., Bokoch G.M.
    Science 254:1512-1515(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-16; 19-49; 154-163 AND 175-183, FUNCTION.
    Tissue: Neutrophil.
  9. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-192.
  10. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 97-102 AND 167-174.
    Tissue: Neutrophil.
  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] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-189, MUTAGENESIS OF CYS-189.
  12. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DOCK2.
  13. "The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2."
    Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C., Doussiere J.
    FASEB J. 19:467-469(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH S100A8 AND CALPROTECTIN.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH ARHGDIB.
  17. Cited for: VARIANT NEUID ASN-57.
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-29.

Entry informationi

Entry nameiRAC2_HUMAN
AccessioniPrimary (citable) accession number: P15153
Secondary accession number(s): Q9UDJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 22, 2015
This is version 175 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.