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Q61599

- GDIR2_MOUSE

UniProt

Q61599 - GDIR2_MOUSE

Protein

Rho GDP-dissociation inhibitor 2

Gene

Arhgdib

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (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: InterPro

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_210090. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho GDP-dissociation inhibitor 2
    Short name:
    Rho GDI 2
    Alternative name(s):
    D4
    Rho-GDI beta
    Gene namesi
    Name:Arhgdib
    Synonyms:Gdid4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:101940. Arhgdib.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 200199Rho GDP-dissociation inhibitor 2PRO_0000219017Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineBy similarity
    Modified residuei20 – 201N6-acetyllysineBy similarity
    Modified residuei23 – 231PhosphotyrosineBy similarity
    Modified residuei24 – 241N6-acetyllysineBy similarity
    Modified residuei39 – 391N6-acetyllysineBy similarity
    Modified residuei46 – 461N6-acetyllysineBy similarity
    Modified residuei101 – 1011N6-acetyllysineBy similarity
    Modified residuei123 – 1231N6-acetyllysineBy similarity
    Modified residuei144 – 1441PhosphoserineBy similarity
    Modified residuei174 – 1741N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ61599.
    PaxDbiQ61599.
    PRIDEiQ61599.

    2D gel databases

    COMPLUYEAST-2DPAGEQ61599.

    PTM databases

    PhosphoSiteiQ61599.

    Expressioni

    Tissue specificityi

    Preferentially expressed in hematopoietic cells.

    Gene expression databases

    BgeeiQ61599.
    CleanExiMM_ARHGDIB.
    GenevestigatoriQ61599.

    Interactioni

    Subunit structurei

    Interacts with RHOA.By similarity

    Protein-protein interaction databases

    BioGridi198201. 6 interactions.
    IntActiQ61599. 3 interactions.
    MINTiMINT-1613948.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61599.
    SMRiQ61599. Positions 22-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Rho GDI family.Curated

    Phylogenomic databases

    eggNOGiNOG253438.
    GeneTreeiENSGT00390000006233.
    HOGENOMiHOG000175765.
    HOVERGENiHBG000206.
    InParanoidiQ61599.
    KOiK12462.
    OMAiQDHLTWE.
    OrthoDBiEOG72JWH9.
    PhylomeDBiQ61599.
    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.

    Q61599-1 [UniParc]FASTAAdd to Basket

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    MTEKDAQPQL EEADDDLDSK LNYKPPPQKS LKELQEMDKD DESLTKYKKT    50
    LLGDVPVVAD PTVPNVTVTR LSLVCDSAPG PITMDLTGDL EALKKDTFVL 100
    KEGIEYRVKI NFKVNKDIVS GLKYVQHTYR TGMRVDKATF MVGSYGPRPE 150
    EYEFLTPVEE APKGMLARGT YHNKSFFTDD DKQDHLTWEW NLAIKKDWTE 200
    Length:200
    Mass (Da):22,851
    Last modified:January 23, 2007 - v3
    Checksum:iEA78C965F1AB6F5C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07918 mRNA. Translation: AAA61613.1.
    AK002516 mRNA. Translation: BAB22155.1.
    AK169733 mRNA. Translation: BAE41335.1.
    BC031763 mRNA. Translation: AAH31763.1.
    CCDSiCCDS20661.1.
    PIRiI49687.
    RefSeqiNP_031512.1. NM_007486.4.
    XP_006505466.1. XM_006505403.1.
    XP_006505467.1. XM_006505404.1.
    XP_006505468.1. XM_006505405.1.
    XP_006505469.1. XM_006505406.1.
    UniGeneiMm.2241.

    Genome annotation databases

    EnsembliENSMUST00000032344; ENSMUSP00000032344; ENSMUSG00000030220.
    ENSMUST00000111891; ENSMUSP00000107522; ENSMUSG00000030220.
    ENSMUST00000111892; ENSMUSP00000107523; ENSMUSG00000030220.
    GeneIDi11857.
    KEGGimmu:11857.
    UCSCiuc009emo.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07918 mRNA. Translation: AAA61613.1 .
    AK002516 mRNA. Translation: BAB22155.1 .
    AK169733 mRNA. Translation: BAE41335.1 .
    BC031763 mRNA. Translation: AAH31763.1 .
    CCDSi CCDS20661.1.
    PIRi I49687.
    RefSeqi NP_031512.1. NM_007486.4.
    XP_006505466.1. XM_006505403.1.
    XP_006505467.1. XM_006505404.1.
    XP_006505468.1. XM_006505405.1.
    XP_006505469.1. XM_006505406.1.
    UniGenei Mm.2241.

    3D structure databases

    ProteinModelPortali Q61599.
    SMRi Q61599. Positions 22-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198201. 6 interactions.
    IntActi Q61599. 3 interactions.
    MINTi MINT-1613948.

    PTM databases

    PhosphoSitei Q61599.

    2D gel databases

    COMPLUYEAST-2DPAGE Q61599.

    Proteomic databases

    MaxQBi Q61599.
    PaxDbi Q61599.
    PRIDEi Q61599.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032344 ; ENSMUSP00000032344 ; ENSMUSG00000030220 .
    ENSMUST00000111891 ; ENSMUSP00000107522 ; ENSMUSG00000030220 .
    ENSMUST00000111892 ; ENSMUSP00000107523 ; ENSMUSG00000030220 .
    GeneIDi 11857.
    KEGGi mmu:11857.
    UCSCi uc009emo.1. mouse.

    Organism-specific databases

    CTDi 397.
    MGIi MGI:101940. Arhgdib.

    Phylogenomic databases

    eggNOGi NOG253438.
    GeneTreei ENSGT00390000006233.
    HOGENOMi HOG000175765.
    HOVERGENi HBG000206.
    InParanoidi Q61599.
    KOi K12462.
    OMAi QDHLTWE.
    OrthoDBi EOG72JWH9.
    PhylomeDBi Q61599.
    TreeFami TF105387.

    Enzyme and pathway databases

    Reactomei REACT_210090. Rho GTPase cycle.

    Miscellaneous databases

    ChiTaRSi ARHGDIB. mouse.
    NextBioi 279847.
    PROi Q61599.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61599.
    CleanExi MM_ARHGDIB.
    Genevestigatori Q61599.

    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. "Identification of a novel protein with GDP dissociation inhibitor activity for the ras-like proteins CDC42Hs and rac I."
      Adra C.N., Ko J., Leonard D., Wirth L.J., Cerione R.A., Lim B.
      Genes Chromosomes Cancer 8:253-261(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NIH Swiss.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Kidney and Thymus.
    3. "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].
      Strain: FVB/N.
      Tissue: Salivary gland.

    Entry informationi

    Entry nameiGDIR2_MOUSE
    AccessioniPrimary (citable) accession number: Q61599
    Secondary accession number(s): Q3TEB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3