ARHGDIA

Protein-coding gene in the species Homo sapiens
ARHGDIA
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1CC0, 1FSO, 1FST, 1FT0, 1FT3, 1HH4, 1KMT, 1QVY, 1RHO, 2BXW, 2JHS, 2JHT, 2JHU, 2JHV, 2JHW, 2JHX, 2JHY, 2JHZ, 2JI0, 2N80

Identifiers
AliasesARHGDIA, GDIA1, HEL-S-47e, NPHS8, RHOGDI, RHOGDI-1, Rho GDP dissociation inhibitor alpha
External IDsOMIM: 601925; MGI: 2178103; HomoloGene: 908; GeneCards: ARHGDIA; OMA:ARHGDIA - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for ARHGDIA
Genomic location for ARHGDIA
Band17q25.3Start81,867,721 bp[1]
End81,871,378 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for ARHGDIA
Genomic location for ARHGDIA
Band11|11 E2Start120,468,930 bp[2]
End120,472,450 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • granulocyte

  • epithelium of colon

  • mucosa of transverse colon

  • left uterine tube

  • upper lobe of left lung

  • right lung

  • ascending aorta

  • left coronary artery

  • tibial nerve

  • anterior pituitary
Top expressed in
  • tail of embryo

  • yolk sac

  • genital tubercle

  • tibiofemoral joint

  • lip

  • lactiferous gland

  • entorhinal cortex

  • mesenteric lymph nodes

  • perirhinal cortex

  • molar
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • GTPase activator activity
  • Rho GDP-dissociation inhibitor activity
  • protein binding
Cellular component
  • cytoplasm
  • cytosol
  • extracellular exosome
  • cytoskeleton
  • membrane
Biological process
  • negative regulation of cell adhesion
  • regulation of actin cytoskeleton reorganization
  • negative regulation of apoptotic process
  • positive regulation of axonogenesis
  • positive regulation of GTPase activity
  • negative regulation of axonogenesis
  • regulation of Rho protein signal transduction
  • regulation of small GTPase mediated signal transduction
  • semaphorin-plexin signaling pathway
  • regulation of catalytic activity
  • Rho protein signal transduction
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

396

192662

Ensembl

ENSG00000141522

ENSMUSG00000025132

UniProt

P52565

Q99PT1

RefSeq (mRNA)
NM_001185077
NM_001185078
NM_001301240
NM_001301241
NM_001301242

NM_001301243
NM_004309

NM_133796
NM_001363425

RefSeq (protein)
NP_001172006
NP_001172007
NP_001288169
NP_001288170
NP_001288171

NP_001288172
NP_004300

NP_598557
NP_001350354

Location (UCSC)Chr 17: 81.87 – 81.87 MbChr 11: 120.47 – 120.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Rho GDP-dissociation inhibitor 1 is a protein that in humans is encoded by the ARHGDIA gene.[5][6]

Interactions

ARHGDIA has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000141522 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025132 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Wagner T, Tommerup N, Wirth J, Leffers H, Zimmer J, Back E, Weissenbach J, Scherer G (July 1997). "A somatic cell hybrid panel for distal 17q: GDIA1 maps to 17q25.3". Cytogenet Cell Genet. 76 (3–4): 172–5. doi:10.1159/000134538. PMID 9186513.
  6. ^ "Entrez Gene: ARHGDIA Rho GDP dissociation inhibitor (GDI) alpha".
  7. ^ a b c Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  8. ^ a b c d Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (January 1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. 422 (2): 269–73. doi:10.1016/s0014-5793(98)00020-9. PMID 9490022. S2CID 10817327.
  9. ^ a b c d Fauré J, Dagher MC (May 2001). "Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)". Biochimie. 83 (5): 409–14. doi:10.1016/s0300-9084(01)01263-9. PMID 11368848.
  10. ^ Grizot S, Fauré J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E (August 2001). "Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation". Biochemistry. 40 (34): 10007–13. doi:10.1021/bi010288k. PMID 11513578.
  11. ^ Lian LY, Barsukov I, Golovanov AP, Hawkins DI, Badii R, Sze KH, Keep NH, Bokoch GM, Roberts GC (January 2000). "Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47–55. doi:10.1016/s0969-2126(00)00080-0. PMID 10673424.
  12. ^ Di-Poï N, Fauré J, Grizot S, Molnár G, Pick E, Dagher MC (August 2001). "Mechanism of NADPH oxidase activation by the Rac/Rho-GDI complex". Biochemistry. 40 (34): 10014–22. doi:10.1021/bi010289c. PMID 11513579.
  13. ^ Gajate C, Mollinedo F (March 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. doi:10.1074/jbc.M411781200. PMID 15659383.
  14. ^ Michaelson D, Silletti J, Murphy G, D'Eustachio P, Rush M, Philips MR (January 2001). "Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding". J. Cell Biol. 152 (1): 111–26. doi:10.1083/jcb.152.1.111. PMC 2193662. PMID 11149925.
  15. ^ Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B (February 2002). "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function". Mol. Cell. Biol. 22 (4): 1158–71. doi:10.1128/mcb.22.4.1158-1171.2002. PMC 134637. PMID 11809807.

Further reading

  • Leffers H, Nielsen MS, Andersen AH, Honoré B, Madsen P, Vandekerckhove J, Celis JE (1994). "Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton". Exp. Cell Res. 209 (2): 165–74. doi:10.1006/excr.1993.1298. PMID 8262133.
  • Keep NH, Barnes M, Barsukov I, Badii R, Lian LY, Segal AW, Moody PC, Roberts GC (1997). "A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm". Structure. 5 (5): 623–33. doi:10.1016/S0969-2126(97)00218-9. PMID 9195882.
  • Takahashi K, Sasaki T, Mammoto A, Takaishi K, Kameyama T, Tsukita S, Takai Y (1997). "Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein". J. Biol. Chem. 272 (37): 23371–5. doi:10.1074/jbc.272.37.23371. PMID 9287351.
  • Gorvel JP, Chang TC, Boretto J, Azuma T, Chavrier P (1998). "Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity". FEBS Lett. 422 (2): 269–73. doi:10.1016/S0014-5793(98)00020-9. PMID 9490022. S2CID 10817327.
  • Takahashi K, Sasaki T, Mammoto A, Hotta I, Takaishi K, Imamura H, Nakano K, Kodama A, Takai Y (1998). "Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl". Oncogene. 16 (25): 3279–84. doi:10.1038/sj.onc.1201874. PMID 9681826. S2CID 21445282.
  • Newcombe AR, Stockley RW, Hunter JL, Webb MR (1999). "The interaction between rac1 and its guanine nucleotide dissociation inhibitor (GDI), monitored by a single fluorescent coumarin attached to GDI". Biochemistry. 38 (21): 6879–86. doi:10.1021/bi9829837. PMID 10346909.
  • Groysman M, Russek CS, Katzav S (2000). "Vav, a GDP/GTP nucleotide exchange factor, interacts with GDIs, proteins that inhibit GDP/GTP dissociation". FEBS Lett. 467 (1): 75–80. doi:10.1016/S0014-5793(00)01121-2. PMID 10664460. S2CID 40103095.
  • Lian LY, Barsukov I, Golovanov AP, Hawkins DI, Badii R, Sze KH, Keep NH, Bokoch GM, Roberts GC (2000). "Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1". Structure. 8 (1): 47–55. doi:10.1016/S0969-2126(00)00080-0. PMID 10673424.
  • Hoffman GR, Nassar N, Cerione RA (2000). "Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI". Cell. 100 (3): 345–56. doi:10.1016/S0092-8674(00)80670-4. PMID 10676816. S2CID 17115337.
  • Matarrese P, Conti L, Varano B, Gauzzi MC, Belardelli F, Gessani S, Malorni W (2000). "The HIV-1 vpr protein induces anoikis-resistance by modulating cell adhesion process and microfilament system assembly". Cell Death Differ. 7 (1): 25–36. doi:10.1038/sj.cdd.4400616. PMID 10713718.
  • Michaelson D, Silletti J, Murphy G, D'Eustachio P, Rush M, Philips MR (2001). "Differential Localization of Rho Gtpases in Live Cells: Regulation by Hypervariable Regions and Rhogdi Binding". J. Cell Biol. 152 (1): 111–26. doi:10.1083/jcb.152.1.111. PMC 2193662. PMID 11149925.
  • Longenecker KL, Garrard SM, Sheffield PJ, Derewenda ZS (2001). "Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI". Acta Crystallogr. D. 57 (Pt 5): 679–88. doi:10.1107/S0907444901003122. PMID 11320308.
  • Grizot S, Fauré J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E (2001). "Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation". Biochemistry. 40 (34): 10007–13. doi:10.1021/bi010288k. PMID 11513578.
  • Di-Poï N, Fauré J, Grizot S, Molnár G, Pick E, Dagher MC (2001). "Mechanism of NADPH oxidase activation by the Rac/Rho-GDI complex". Biochemistry. 40 (34): 10014–22. doi:10.1021/bi010289c. PMID 11513579.
  • DerMardirossian C, Schnelzer A, Bokoch GM (2004). "Phosphorylation of RhoGDI by Pak1 mediates dissociation of Rac GTPase". Mol. Cell. 15 (1): 117–27. doi:10.1016/j.molcel.2004.05.019. PMID 15225553.
  • Dransart E, Morin A, Cherfils J, Olofsson B (2005). "Uncoupling of inhibitory and shuttling functions of rho GDP dissociation inhibitors". J. Biol. Chem. 280 (6): 4674–83. doi:10.1074/jbc.M409741200. PMID 15513926.
  • Gajate C, Mollinedo F (2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. doi:10.1074/jbc.M411781200. PMID 15659383.
  • v
  • t
  • e
  • 1ajw: STRUCTURE OF RHOGDI: A C-TERMINAL BINDING DOMAIN TARGETS AN N-TERMINAL INHIBITORY PEPTIDE TO GTPASES, NMR, 20 STRUCTURES
    1ajw: STRUCTURE OF RHOGDI: A C-TERMINAL BINDING DOMAIN TARGETS AN N-TERMINAL INHIBITORY PEPTIDE TO GTPASES, NMR, 20 STRUCTURES
  • 1cc0: CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX
    1cc0: CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX
  • 1doa: STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI
    1doa: STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 IN COMPLEX WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI
  • 1fso: CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI QUADRUPLE MUTANT
    1fso: CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI QUADRUPLE MUTANT
  • 1fst: CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI TRIPLE MUTANT
    1fst: CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI TRIPLE MUTANT
  • 1ft0: CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANT
    1ft0: CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A MUTANT
  • 1ft3: CRYSTAL STRUCTURE OF TRUNCATED RHOGDI K141A MUTANT
    1ft3: CRYSTAL STRUCTURE OF TRUNCATED RHOGDI K141A MUTANT
  • 1gdf: STRUCTURE OF RHOGDI: A C-TERMINAL BINDING DOMAIN TARGETS AN N-TERMINAL INHIBITORY PEPTIDE TO GTPASES, NMR, MINIMIZED AVERAGE STRUCTURE
    1gdf: STRUCTURE OF RHOGDI: A C-TERMINAL BINDING DOMAIN TARGETS AN N-TERMINAL INHIBITORY PEPTIDE TO GTPASES, NMR, MINIMIZED AVERAGE STRUCTURE
  • 1hh4: RAC1-RHOGDI COMPLEX INVOLVED IN NADPH OXIDASE ACTIVATION
    1hh4: RAC1-RHOGDI COMPLEX INVOLVED IN NADPH OXIDASE ACTIVATION
  • 1kmt: Crystal structure of RhoGDI Glu(154,155)Ala mutant
    1kmt: Crystal structure of RhoGDI Glu(154,155)Ala mutant
  • 1qvy: Crystal structure of RhoGDI K(199,200)R double mutant
    1qvy: Crystal structure of RhoGDI K(199,200)R double mutant
  • 1rho: STRUCTURE OF RHO GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR
    1rho: STRUCTURE OF RHO GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR
  • 2bxw: CRYSTAL STRUCTURE OF RHOGDI LYS(135,138,141)TYR MUTANT
    2bxw: CRYSTAL STRUCTURE OF RHOGDI LYS(135,138,141)TYR MUTANT
  • 2jhs: CRYSTAL STRUCTURE OF RHOGDI K135H,K138H,K141H MUTANT
    2jhs: CRYSTAL STRUCTURE OF RHOGDI K135H,K138H,K141H MUTANT
  • 2jht: CRYSTAL STRUCTURE OF RHOGDI K135T,K138T,K141T MUTANT
    2jht: CRYSTAL STRUCTURE OF RHOGDI K135T,K138T,K141T MUTANT
  • 2jhu: CRYSTAL STRUCTURE OF RHOGDI E154A,E155A MUTANT
    2jhu: CRYSTAL STRUCTURE OF RHOGDI E154A,E155A MUTANT
  • 2jhv: CRYSTAL STRUCTURE OF RHOGDI E154A,E155A MUTANT
    2jhv: CRYSTAL STRUCTURE OF RHOGDI E154A,E155A MUTANT
  • 2jhw: CRYSTAL STRUCTURE OF RHOGDI E155A, E157A MUTANT
    2jhw: CRYSTAL STRUCTURE OF RHOGDI E155A, E157A MUTANT
  • 2jhx: CRYSTAL STRUCTURE OF RHOGDI E155H, E157H MUTANT
    2jhx: CRYSTAL STRUCTURE OF RHOGDI E155H, E157H MUTANT
  • 2jhy: CRYSTAL STRUCTURE OF RHOGDI E155H, E157H MUTANT
    2jhy: CRYSTAL STRUCTURE OF RHOGDI E155H, E157H MUTANT
  • 2jhz: CRYSTAL STRUCTURE OF RHOGDI E155S, E157S MUTANT
    2jhz: CRYSTAL STRUCTURE OF RHOGDI E155S, E157S MUTANT
  • 2ji0: CRYSTAL STRUCTURE OF RHOGDI K138Y, K141Y MUTANT
    2ji0: CRYSTAL STRUCTURE OF RHOGDI K138Y, K141Y MUTANT