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P15153

- RAC2_HUMAN

UniProt

P15153 - RAC2_HUMAN

Protein

Ras-related C3 botulinum toxin substrate 2

Gene

RAC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    1. GTPase activity Source: ProtInc
    2. GTP binding Source: UniProtKB-KW

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. axon guidance Source: Reactome
    3. blood coagulation Source: Reactome
    4. bone resorption Source: Ensembl
    5. cell projection assembly Source: Ensembl
    6. platelet activation Source: Reactome
    7. positive regulation of cell proliferation Source: Ensembl
    8. regulation of hydrogen peroxide metabolic process Source: BHF-UCL
    9. regulation of respiratory burst Source: BHF-UCL
    10. regulation of small GTPase mediated signal transduction Source: Reactome
    11. signal transduction Source: ProtInc
    12. small GTPase mediated signal transduction Source: Reactome

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_172581. PCP/CE pathway.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    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: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:9802. RAC2.

    Subcellular locationi

    Cytoplasm
    Note: Membrane-associated when activated.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nuclear envelope Source: Ensembl
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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

    ArrayExpressiP15153.
    BgeeiP15153.
    CleanExiHS_RAC2.
    GenevestigatoriP15153.

    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. 19 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 – 119
    Helixi16 – 2510
    Beta strandi39 – 468
    Beta strandi49 – 568
    Helixi62 – 643
    Turni65 – 673
    Helixi68 – 714
    Beta strandi77 – 837
    Helixi87 – 959
    Helixi97 – 1048
    Beta strandi106 – 1083
    Beta strandi110 – 1156
    Helixi117 – 1193
    Helixi123 – 1308
    Turni131 – 1333
    Helixi139 – 14911
    Beta strandi152 – 1565
    Turni159 – 1613
    Helixi165 – 17511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    InParanoidiP15153.
    KOiK07860.
    OMAiREDRSYL.
    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

    MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP    50
    VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRAKWFPE 100
    VRHHCPSTPI ILVGTKLDLR DDKDTIEKLK EKKLAPITYP QGLALAKEID 150
    SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ PTRQQKRACS LL 192
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi131806.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13945.1.
    PIRi B34386.
    RefSeqi NP_002863.1. NM_002872.4.
    UniGenei Hs.517601.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DS6 X-ray 2.35 A 1-192 [» ]
    2W2T X-ray 1.95 A 2-179 [» ]
    2W2V X-ray 2.00 A/B/C/D 1-177 [» ]
    2W2X X-ray 2.30 A/B 2-179 [» ]
    ProteinModelPortali P15153.
    SMRi P15153. Positions 1-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111818. 19 interactions.
    DIPi DIP-34291N.
    IntActi P15153. 12 interactions.
    MINTi MINT-1616362.
    STRINGi 9606.ENSP00000249071.

    Chemistry

    ChEMBLi CHEMBL5581.

    PTM databases

    PhosphoSitei P15153.

    Polymorphism databases

    DMDMi 131806.

    Proteomic databases

    MaxQBi P15153.
    PaxDbi P15153.
    PeptideAtlasi P15153.
    PRIDEi P15153.

    Protocols and materials databases

    DNASUi 5880.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000249071 ; ENSP00000249071 ; ENSG00000128340 .
    GeneIDi 5880.
    KEGGi hsa:5880.
    UCSCi uc003arc.3. human.

    Organism-specific databases

    CTDi 5880.
    GeneCardsi GC22M037621.
    HGNCi HGNC:9802. RAC2.
    HPAi CAB022946.
    HPA047820.
    MIMi 602049. gene.
    608203. phenotype.
    neXtProti NX_P15153.
    Orphaneti 183707. Neutrophil immunodeficiency syndrome.
    PharmGKBi PA34163.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    InParanoidi P15153.
    KOi K07860.
    OMAi REDRSYL.
    OrthoDBi EOG764747.
    PhylomeDBi P15153.
    TreeFami TF101109.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_172581. PCP/CE pathway.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    SignaLinki P15153.

    Miscellaneous databases

    EvolutionaryTracei P15153.
    GeneWikii RAC2.
    GenomeRNAii 5880.
    NextBioi 22854.
    PROi P15153.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15153.
    Bgeei P15153.
    CleanExi HS_RAC2.
    Genevestigatori P15153.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00174. RHO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51420. RHO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 166 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