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P52565

- GDIR1_HUMAN

UniProt

P52565 - GDIR1_HUMAN

Protein

Rho GDP-dissociation inhibitor 1

Gene

ARHGDIA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Controls Rho proteins homeostasis. 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. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1.2 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular component movement Source: UniProtKB
    2. negative regulation of apoptotic process Source: UniProtKB
    3. negative regulation of axonogenesis Source: Reactome
    4. negative regulation of cell adhesion Source: ProtInc
    5. neurotrophin TRK receptor signaling pathway Source: Reactome
    6. positive regulation of axonogenesis Source: Reactome
    7. regulation of axonogenesis Source: Reactome
    8. regulation of catalytic activity Source: GOC
    9. regulation of protein localization Source: Ensembl
    10. regulation of small GTPase mediated signal transduction Source: Reactome
    11. Rho protein signal transduction Source: ProtInc
    12. semaphorin-plexin signaling pathway Source: UniProtKB
    13. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_13779. Axonal growth stimulation.
    REACT_13815. Axonal growth inhibition (RHOA activation).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho GDP-dissociation inhibitor 1
    Short name:
    Rho GDI 1
    Alternative name(s):
    Rho-GDI alpha
    Gene namesi
    Name:ARHGDIA
    Synonyms:GDIA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:678. ARHGDIA.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. immunological synapse Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Nephrotic syndrome 8 (NPHS8) [MIM:615244]: A form of nephrotic syndrome, a renal disease clinically characterized by progressive renal failure, severe proteinuria, hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show diffuse mesangial sclerosis, with small glomeruli, hypercellularity, increased extracellular matrix, and contracted/collapsed glomerular tufts surrounded by immature or abnormal podocytes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti185 – 1851Missing in NPHS8; produces mislocalization into the nucleus, hyperactivation of Rho-GTPases RHOA, RAC1 and CDC42 and impaired cell motility. 1 Publication
    VAR_069814

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451D → A: Loss of RHOA interaction; when associated with A-185. 1 Publication
    Mutagenesisi185 – 1851D → A: Loss of RHOA interaction; when associated with A-45. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615244. phenotype.
    Orphaneti93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
    PharmGKBiPA24963.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 204203Rho GDP-dissociation inhibitor 1PRO_0000219013Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei34 – 341PhosphoserineBy similarity
    Modified residuei43 – 431N6-acetyllysineBy similarity
    Modified residuei105 – 1051N6-acetyllysine1 Publication
    Modified residuei127 – 1271N6-acetyllysine1 Publication
    Modified residuei141 – 1411N6-acetyllysine; alternate2 Publications
    Modified residuei141 – 1411N6-succinyllysine; alternateBy similarity
    Modified residuei178 – 1781N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP52565.
    PaxDbiP52565.
    PRIDEiP52565.

    2D gel databases

    DOSAC-COBS-2DPAGEP52565.
    OGPiP52565.
    REPRODUCTION-2DPAGEIPI00003815.

    PTM databases

    PhosphoSiteiP52565.

    Expressioni

    Gene expression databases

    ArrayExpressiP52565.
    BgeeiP52565.
    CleanExiHS_ARHGDIA.
    GenevestigatoriP52565.

    Organism-specific databases

    HPAiCAB010005.
    HPA021407.

    Interactioni

    Subunit structurei

    Monomer. Interacts with FER. Interacts with PLXNB3 By similarity. Forms a heterodimer with RAC1. Interacts with RHOA, the affinity is increased by three orders of magnitude when RHOA is prenylated. Interacts with PSMD10; the interaction increases ARHGDIA association with RHOA, leading to ARHGDIA-mediated inactivation of RHOA and ROCK and prolonged AKT activation. Interacts with RHOC and CDC42.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAC1P630006EBI-712693,EBI-413628
    RHOAP615862EBI-712693,EBI-446668

    Protein-protein interaction databases

    BioGridi106889. 64 interactions.
    IntActiP52565. 32 interactions.
    MINTiMINT-93856.
    STRINGi9606.ENSP00000269321.

    Structurei

    Secondary structure

    1
    204
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi35 – 395
    Helixi46 – 5611
    Beta strandi69 – 7810
    Beta strandi82 – 843
    Beta strandi87 – 893
    Helixi94 – 996
    Beta strandi102 – 1054
    Beta strandi109 – 11810
    Beta strandi123 – 13412
    Beta strandi137 – 14913
    Beta strandi156 – 1594
    Turni169 – 1713
    Beta strandi173 – 18210
    Beta strandi189 – 20012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CC0X-ray5.00E/F1-204[»]
    1FSOX-ray2.00A67-204[»]
    1FSTX-ray2.70A/B24-204[»]
    1FT0X-ray2.60A/B67-204[»]
    1FT3X-ray2.80A/B67-204[»]
    1HH4X-ray2.70D/E1-204[»]
    1KMTX-ray1.30A/B67-204[»]
    1QVYX-ray1.60A/B/C/D67-204[»]
    1RHOX-ray2.50A/B/C59-203[»]
    2BXWX-ray2.40A/B67-204[»]
    2JHSX-ray1.95A67-202[»]
    2JHTX-ray1.88A/B/C/D67-202[»]
    2JHUX-ray1.65A/B67-202[»]
    2JHVX-ray2.07A/B/C/D/E/F67-202[»]
    2JHWX-ray2.50A/B67-202[»]
    2JHXX-ray1.60A/B67-202[»]
    2JHYX-ray1.90A67-202[»]
    2JHZX-ray2.20A/B67-202[»]
    2JI0X-ray2.10A67-202[»]
    ProteinModelPortaliP52565.
    SMRiP52565. Positions 23-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52565.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Rho GDI family.Curated

    Phylogenomic databases

    eggNOGiNOG289931.
    HOGENOMiHOG000175765.
    HOVERGENiHBG000206.
    InParanoidiP52565.
    KOiK12462.
    OMAiEGVEYQI.
    OrthoDBiEOG72JWH9.
    PhylomeDBiP52565.
    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.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P52565-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAEQEPTAEQ LAQIAAENEE DEHSVNYKPP AQKSIQEIQE LDKDDESLRK    50
    YKEALLGRVA VSADPNVPNV VVTGLTLVCS SAPGPLELDL TGDLESFKKQ 100
    SFVLKEGVEY RIKISFRVNR EIVSGMKYIQ HTYRKGVKID KTDYMVGSYG 150
    PRAEEYEFLT PVEEAPKGML ARGSYSIKSR FTDDDKTDHL SWEWNLTIKK 200
    DWKD 204
    Length:204
    Mass (Da):23,207
    Last modified:January 23, 2007 - v3
    Checksum:i59CB6F42E3B3BCCA
    GO
    Isoform 2 (identifier: P52565-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         139-183: IDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTD → N

    Show »
    Length:160
    Mass (Da):18,233
    Checksum:i0E14B24C9B7AFCA2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti139 – 1391I → V in CAA45344. 1 PublicationCurated
    Sequence conflicti139 – 1391I → V in BAG35268. (PubMed:14702039)Curated
    Sequence conflicti188 – 1881D → R AA sequence 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti185 – 1851Missing in NPHS8; produces mislocalization into the nucleus, hyperactivation of Rho-GTPases RHOA, RAC1 and CDC42 and impaired cell motility. 1 Publication
    VAR_069814

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei139 – 18345IDKTD…SRFTD → N in isoform 2. 1 PublicationVSP_046699Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69550 mRNA. Translation: CAA49281.1.
    D13989 mRNA. Translation: BAA03096.1.
    M97579 mRNA. Translation: AAA36566.1.
    X63863 Genomic DNA. Translation: CAA45344.1.
    AK300816 mRNA. Translation: BAG62471.1.
    AK312347 mRNA. Translation: BAG35268.1.
    AF498926 mRNA. Translation: AAM21074.1.
    BT006884 mRNA. Translation: AAP35530.1.
    CR456777 mRNA. Translation: CAG33058.1.
    AC145207 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89697.1.
    BC005851 mRNA. Translation: AAH05851.1.
    BC005875 mRNA. Translation: AAH05875.1.
    BC008701 mRNA. Translation: AAH08701.1.
    BC009759 mRNA. Translation: AAH09759.1.
    BC016031 mRNA. Translation: AAH16031.1.
    BC016185 mRNA. Translation: AAH16185.1.
    BC024258 mRNA. Translation: AAH24258.1.
    BC027730 mRNA. Translation: AAH27730.1.
    BC075827 mRNA. Translation: AAH75827.1.
    BC106044 mRNA. Translation: AAI06045.1.
    CCDSiCCDS11788.1. [P52565-1]
    CCDS58609.1. [P52565-2]
    PIRiI38156.
    RefSeqiNP_001172006.1. NM_001185077.1. [P52565-1]
    NP_001172007.1. NM_001185078.1. [P52565-2]
    NP_004300.1. NM_004309.4. [P52565-1]
    UniGeneiHs.159161.

    Genome annotation databases

    EnsembliENST00000269321; ENSP00000269321; ENSG00000141522. [P52565-1]
    ENST00000400721; ENSP00000383556; ENSG00000141522. [P52565-2]
    ENST00000541078; ENSP00000441348; ENSG00000141522. [P52565-1]
    ENST00000580685; ENSP00000464205; ENSG00000141522. [P52565-1]
    GeneIDi396.
    KEGGihsa:396.
    UCSCiuc002kbq.3. human. [P52565-1]

    Polymorphism databases

    DMDMi1707892.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69550 mRNA. Translation: CAA49281.1 .
    D13989 mRNA. Translation: BAA03096.1 .
    M97579 mRNA. Translation: AAA36566.1 .
    X63863 Genomic DNA. Translation: CAA45344.1 .
    AK300816 mRNA. Translation: BAG62471.1 .
    AK312347 mRNA. Translation: BAG35268.1 .
    AF498926 mRNA. Translation: AAM21074.1 .
    BT006884 mRNA. Translation: AAP35530.1 .
    CR456777 mRNA. Translation: CAG33058.1 .
    AC145207 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89697.1 .
    BC005851 mRNA. Translation: AAH05851.1 .
    BC005875 mRNA. Translation: AAH05875.1 .
    BC008701 mRNA. Translation: AAH08701.1 .
    BC009759 mRNA. Translation: AAH09759.1 .
    BC016031 mRNA. Translation: AAH16031.1 .
    BC016185 mRNA. Translation: AAH16185.1 .
    BC024258 mRNA. Translation: AAH24258.1 .
    BC027730 mRNA. Translation: AAH27730.1 .
    BC075827 mRNA. Translation: AAH75827.1 .
    BC106044 mRNA. Translation: AAI06045.1 .
    CCDSi CCDS11788.1. [P52565-1 ]
    CCDS58609.1. [P52565-2 ]
    PIRi I38156.
    RefSeqi NP_001172006.1. NM_001185077.1. [P52565-1 ]
    NP_001172007.1. NM_001185078.1. [P52565-2 ]
    NP_004300.1. NM_004309.4. [P52565-1 ]
    UniGenei Hs.159161.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CC0 X-ray 5.00 E/F 1-204 [» ]
    1FSO X-ray 2.00 A 67-204 [» ]
    1FST X-ray 2.70 A/B 24-204 [» ]
    1FT0 X-ray 2.60 A/B 67-204 [» ]
    1FT3 X-ray 2.80 A/B 67-204 [» ]
    1HH4 X-ray 2.70 D/E 1-204 [» ]
    1KMT X-ray 1.30 A/B 67-204 [» ]
    1QVY X-ray 1.60 A/B/C/D 67-204 [» ]
    1RHO X-ray 2.50 A/B/C 59-203 [» ]
    2BXW X-ray 2.40 A/B 67-204 [» ]
    2JHS X-ray 1.95 A 67-202 [» ]
    2JHT X-ray 1.88 A/B/C/D 67-202 [» ]
    2JHU X-ray 1.65 A/B 67-202 [» ]
    2JHV X-ray 2.07 A/B/C/D/E/F 67-202 [» ]
    2JHW X-ray 2.50 A/B 67-202 [» ]
    2JHX X-ray 1.60 A/B 67-202 [» ]
    2JHY X-ray 1.90 A 67-202 [» ]
    2JHZ X-ray 2.20 A/B 67-202 [» ]
    2JI0 X-ray 2.10 A 67-202 [» ]
    ProteinModelPortali P52565.
    SMRi P52565. Positions 23-202.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106889. 64 interactions.
    IntActi P52565. 32 interactions.
    MINTi MINT-93856.
    STRINGi 9606.ENSP00000269321.

    PTM databases

    PhosphoSitei P52565.

    Polymorphism databases

    DMDMi 1707892.

    2D gel databases

    DOSAC-COBS-2DPAGE P52565.
    OGPi P52565.
    REPRODUCTION-2DPAGE IPI00003815.

    Proteomic databases

    MaxQBi P52565.
    PaxDbi P52565.
    PRIDEi P52565.

    Protocols and materials databases

    DNASUi 396.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269321 ; ENSP00000269321 ; ENSG00000141522 . [P52565-1 ]
    ENST00000400721 ; ENSP00000383556 ; ENSG00000141522 . [P52565-2 ]
    ENST00000541078 ; ENSP00000441348 ; ENSG00000141522 . [P52565-1 ]
    ENST00000580685 ; ENSP00000464205 ; ENSG00000141522 . [P52565-1 ]
    GeneIDi 396.
    KEGGi hsa:396.
    UCSCi uc002kbq.3. human. [P52565-1 ]

    Organism-specific databases

    CTDi 396.
    GeneCardsi GC17M079825.
    HGNCi HGNC:678. ARHGDIA.
    HPAi CAB010005.
    HPA021407.
    MIMi 601925. gene.
    615244. phenotype.
    neXtProti NX_P52565.
    Orphaneti 93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
    PharmGKBi PA24963.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289931.
    HOGENOMi HOG000175765.
    HOVERGENi HBG000206.
    InParanoidi P52565.
    KOi K12462.
    OMAi EGVEYQI.
    OrthoDBi EOG72JWH9.
    PhylomeDBi P52565.
    TreeFami TF105387.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_13779. Axonal growth stimulation.
    REACT_13815. Axonal growth inhibition (RHOA activation).

    Miscellaneous databases

    EvolutionaryTracei P52565.
    GeneWikii ARHGDIA.
    GenomeRNAii 396.
    NextBioi 1661.
    PROi P52565.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52565.
    Bgeei P52565.
    CleanExi HS_ARHGDIA.
    Genevestigatori P52565.

    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 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] (ISOFORM 1).
    2. "Molecular cloning of human rho GDI."
      Maeda A., Kaibuchi K., Takai Y.
      Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "cDNA sequence of human rho GDP dissociation inhibitor."
      Chuang T.H., Bokoch G.M.
      Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Genomic sequence of a human rho GDP dissociation inhibitor (GDI)."
      Mulheron J.G., Schwinn D.A., Caron M.G., Liggett S.B.
      Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain cortex and Neuroblastoma.
    6. "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] (ISOFORM 1).
      Tissue: Brain.
    7. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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] (ISOFORM 1).
      Tissue: Colon, Lung, Muscle, Skin, Tonsil and Uterus.
    12. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-42, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    13. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 34-50; 139-167 AND 181-199, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    14. "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 34-37; 136-142 AND 181-199.
      Tissue: Neutrophil.
    15. "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
      Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
      Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-105; LYS-127; LYS-141 AND LYS-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "The Fer tyrosine kinase regulates interactions of Rho GDP-Dissociation Inhibitor alpha with the small GTPase Rac."
      Fei F., Kweon S.M., Haataja L., De Sepulveda P., Groffen J., Heisterkamp N.
      BMC Biochem. 11:48-48(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FER.
    19. "Gankyrin plays an essential role in Ras-induced tumorigenesis through regulation of the RhoA/ROCK pathway in mammalian cells."
      Man J.H., Liang B., Gu Y.X., Zhou T., Li A.L., Li T., Jin B.F., Bai B., Zhang H.Y., Zhang W.N., Li W.H., Gong W.L., Li H.Y., Zhang X.M.
      J. Clin. Invest. 120:2829-2841(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PSMD10 AND RHOA.
    20. "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: FUNCTION, INTERACTION WITH RHOA AND RHOC, MUTAGENESIS OF ASP-45 AND ASP-185.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm."
      Keep N.H., Barnes M., Barsukov I., Badii R., Lian L.-Y., Segal A.W., Moody P.C.E., Roberts G.C.K.
      Structure 5:623-633(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 59-204.
    24. Cited for: VARIANT NPHS8 ASP-185 DEL, CHARACTERIZATION OF VARIANT NPHS8 ASP-185 DEL, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAC1; RHOA AND CDC42.

    Entry informationi

    Entry nameiGDIR1_HUMAN
    AccessioniPrimary (citable) accession number: P52565
    Secondary accession number(s): A8MXW0
    , B2R5X1, B4DDD3, B4DUV9, Q6IBM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 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 17
      Human chromosome 17: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3