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P52566

- GDIR2_HUMAN

UniProt

P52566 - GDIR2_HUMAN

Protein

Rho GDP-dissociation inhibitor 2

Gene

ARHGDIB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.

    GO - Molecular functioni

    1. GTPase activator activity Source: UniProtKB-KW
    2. Rho GDP-dissociation inhibitor activity Source: ProtInc

    GO - Biological processi

    1. actin cytoskeleton organization Source: ProtInc
    2. cellular component movement Source: UniProtKB
    3. immune response Source: ProtInc
    4. multicellular organismal development Source: ProtInc
    5. negative regulation of cell adhesion Source: ProtInc
    6. regulation of catalytic activity Source: GOC
    7. regulation of small GTPase mediated signal transduction Source: Reactome
    8. Rho protein signal transduction Source: ProtInc
    9. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho GDP-dissociation inhibitor 2
    Short name:
    Rho GDI 2
    Alternative name(s):
    Ly-GDI
    Rho-GDI beta
    Gene namesi
    Name:ARHGDIB
    Synonyms:GDIA2, GDID4, RAP1GN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:679. ARHGDIB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic membrane-bounded vesicle Source: ProtInc
    3. cytoskeleton Source: UniProtKB
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24964.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 201200Rho GDP-dissociation inhibitor 2PRO_0000219016Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei21 – 211N6-acetyllysine1 Publication
    Modified residuei24 – 241Phosphotyrosine1 Publication
    Modified residuei25 – 251N6-acetyllysine1 Publication
    Modified residuei40 – 401N6-acetyllysine1 Publication
    Modified residuei47 – 471N6-acetyllysine1 Publication
    Modified residuei102 – 1021N6-acetyllysine1 Publication
    Modified residuei124 – 1241N6-acetyllysine1 Publication
    Modified residuei145 – 1451Phosphoserine1 Publication
    Modified residuei175 – 1751N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP52566.
    PaxDbiP52566.
    PRIDEiP52566.

    2D gel databases

    OGPiP52566.
    SWISS-2DPAGEP52566.

    PTM databases

    PhosphoSiteiP52566.

    Miscellaneous databases

    PMAP-CutDBP52566.

    Expressioni

    Gene expression databases

    ArrayExpressiP52566.
    BgeeiP52566.
    CleanExiHS_ARHGDIB.
    GenevestigatoriP52566.

    Organism-specific databases

    HPAiCAB018584.
    HPA051235.

    Interactioni

    Subunit structurei

    Interacts with RHOA.1 Publication

    Protein-protein interaction databases

    BioGridi106890. 13 interactions.
    DIPiDIP-40959N.
    IntActiP52566. 8 interactions.
    MINTiMINT-1616342.
    STRINGi9606.ENSP00000228945.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 376
    Turni38 – 414
    Helixi43 – 5210
    Beta strandi62 – 643
    Beta strandi69 – 757
    Beta strandi84 – 863
    Helixi91 – 966
    Beta strandi98 – 1025
    Beta strandi106 – 1138
    Beta strandi120 – 13112
    Beta strandi134 – 14613
    Beta strandi153 – 1564
    Turni166 – 1683
    Beta strandi170 – 17910
    Beta strandi187 – 19812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DS6X-ray2.35B23-199[»]
    ProteinModelPortaliP52566.
    SMRiP52566. Positions 23-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52566.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Rho GDI family.Curated

    Phylogenomic databases

    eggNOGiNOG253438.
    HOGENOMiHOG000175765.
    HOVERGENiHBG000206.
    InParanoidiP52566.
    KOiK12462.
    OMAiEIKKDWA.
    OrthoDBiEOG72JWH9.
    PhylomeDBiP52566.
    TreeFamiTF105387.

    Family and domain databases

    Gene3Di2.70.50.30. 1 hit.
    InterProiIPR014756. Ig_E-set.
    IPR000406. Rho_GDI.
    IPR024792. RhoGDI_domain.
    [Graphical view]
    PANTHERiPTHR10980. PTHR10980. 1 hit.
    PfamiPF02115. Rho_GDI. 1 hit.
    [Graphical view]
    PRINTSiPR00492. RHOGDI.
    SUPFAMiSSF81296. SSF81296. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P52566-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEKAPEPHV EEDDDDELDS KLNYKPPPQK SLKELQEMDK DDESLIKYKK    50
    TLLGDGPVVT DPKAPNVVVT RLTLVCESAP GPITMDLTGD LEALKKETIV 100
    LKEGSEYRVK IHFKVNRDIV SGLKYVQHTY RTGVKVDKAT FMVGSYGPRP 150
    EEYEFLTPVE EAPKGMLARG TYHNKSFFTD DDKQDHLSWE WNLSIKKEWT 200
    E 201
    Length:201
    Mass (Da):22,988
    Last modified:January 23, 2007 - v3
    Checksum:iF1E840134F643E5F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531Y → V AA sequence (PubMed:2226408)Curated
    Sequence conflicti169 – 1702RG → QD in L07916. (PubMed:8434008)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20688 mRNA. Translation: AAA59539.1.
    X69549 mRNA. Translation: CAA49280.1.
    L07916 mRNA. No translation available.
    AF498927 mRNA. Translation: AAM21075.1.
    AB451315 mRNA. Translation: BAG70129.1.
    AB451445 mRNA. Translation: BAG70259.1.
    CH471094 Genomic DNA. Translation: EAW96336.1.
    BC009200 mRNA. Translation: AAH09200.1.
    CCDSiCCDS8671.1.
    PIRiA47742.
    RefSeqiNP_001166.3. NM_001175.5.
    UniGeneiHs.504877.

    Genome annotation databases

    EnsembliENST00000228945; ENSP00000228945; ENSG00000111348.
    ENST00000541546; ENSP00000440560; ENSG00000111348.
    ENST00000541644; ENSP00000444860; ENSG00000111348.
    GeneIDi397.
    KEGGihsa:397.
    UCSCiuc001rcq.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20688 mRNA. Translation: AAA59539.1 .
    X69549 mRNA. Translation: CAA49280.1 .
    L07916 mRNA. No translation available.
    AF498927 mRNA. Translation: AAM21075.1 .
    AB451315 mRNA. Translation: BAG70129.1 .
    AB451445 mRNA. Translation: BAG70259.1 .
    CH471094 Genomic DNA. Translation: EAW96336.1 .
    BC009200 mRNA. Translation: AAH09200.1 .
    CCDSi CCDS8671.1.
    PIRi A47742.
    RefSeqi NP_001166.3. NM_001175.5.
    UniGenei Hs.504877.

    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 B 23-199 [» ]
    ProteinModelPortali P52566.
    SMRi P52566. Positions 23-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106890. 13 interactions.
    DIPi DIP-40959N.
    IntActi P52566. 8 interactions.
    MINTi MINT-1616342.
    STRINGi 9606.ENSP00000228945.

    PTM databases

    PhosphoSitei P52566.

    2D gel databases

    OGPi P52566.
    SWISS-2DPAGE P52566.

    Proteomic databases

    MaxQBi P52566.
    PaxDbi P52566.
    PRIDEi P52566.

    Protocols and materials databases

    DNASUi 397.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228945 ; ENSP00000228945 ; ENSG00000111348 .
    ENST00000541546 ; ENSP00000440560 ; ENSG00000111348 .
    ENST00000541644 ; ENSP00000444860 ; ENSG00000111348 .
    GeneIDi 397.
    KEGGi hsa:397.
    UCSCi uc001rcq.1. human.

    Organism-specific databases

    CTDi 397.
    GeneCardsi GC12M015094.
    H-InvDB HIX0036989.
    HGNCi HGNC:679. ARHGDIB.
    HPAi CAB018584.
    HPA051235.
    MIMi 602843. gene.
    neXtProti NX_P52566.
    PharmGKBi PA24964.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG253438.
    HOGENOMi HOG000175765.
    HOVERGENi HBG000206.
    InParanoidi P52566.
    KOi K12462.
    OMAi EIKKDWA.
    OrthoDBi EOG72JWH9.
    PhylomeDBi P52566.
    TreeFami TF105387.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.

    Miscellaneous databases

    EvolutionaryTracei P52566.
    GeneWikii ARHGDIB.
    GenomeRNAii 397.
    NextBioi 1665.
    PMAP-CutDB P52566.
    PROi P52566.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52566.
    Bgeei P52566.
    CleanExi HS_ARHGDIB.
    Genevestigatori P52566.

    Family and domain databases

    Gene3Di 2.70.50.30. 1 hit.
    InterProi IPR014756. Ig_E-set.
    IPR000406. Rho_GDI.
    IPR024792. RhoGDI_domain.
    [Graphical view ]
    PANTHERi PTHR10980. PTHR10980. 1 hit.
    Pfami PF02115. Rho_GDI. 1 hit.
    [Graphical view ]
    PRINTSi PR00492. RHOGDI.
    SUPFAMi SSF81296. SSF81296. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes."
      Scherle P., Behrens T., Staudt L.M.
      Proc. Natl. Acad. Sci. U.S.A. 90:7568-7572(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton."
      Leffers H., Nielsen M.S., Andersen A.H., Honore B., Madsen P., Vandekerckhove J., Celis J.E.
      Exp. Cell Res. 209:165-174(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins."
      Lelias J.M., Adra C.N., Wulf G.M., Guillemot J.-C., Caput D., Lim B.
      Proc. Natl. Acad. Sci. U.S.A. 90:1479-1483(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
      Tissue: Brain.
    5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Lymph.
    8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-20; 33-46 AND 50-62, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    9. "Sequence analysis of proteins separated by polyacrylamide gel electrophoresis: towards an integrated protein database."
      Aebersold R., Leavitt J.
      Electrophoresis 11:517-527(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 10-19; 21-25; 51-58; 142-148 AND 150-156.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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-21; LYS-25; LYS-40; LYS-47; LYS-102; LYS-124 AND LYS-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1."
      Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G., Brennwald P.J., Burridge K.
      Nat. Cell Biol. 12:477-483(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RHOA.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 RAC2.

    Entry informationi

    Entry nameiGDIR2_HUMAN
    AccessioniPrimary (citable) accession number: P52566
    Secondary accession number(s): B5BU79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3