ARHGAP1

Rho GTPase activating protein 1

PDB rendering based on 1am4.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsARHGAP1 ; CDC42GAP; RHOGAP; RHOGAP1; p50rhoGAP
External IDsOMIM: 602732 MGI: 2445003 HomoloGene: 20909 GeneCards: ARHGAP1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez392228359
EnsemblENSG00000175220ENSMUSG00000027247
UniProtQ07960Q5FWK3
RefSeq (mRNA)NM_004308NM_001145902
RefSeq (protein)NP_004299NP_001139374
Location (UCSC)Chr 11:
46.68 – 46.7 Mb		Chr 2:
91.65 – 91.67 Mb
PubMed search

Rho GTPase-activating protein 1 is an enzyme that in humans is encoded by the ARHGAP1 gene.[1][2]

Interactions

ARHGAP1 has been shown to interact with:

References

  1. ↑ Lancaster CA, Taylor-Harris PM, Self AJ, Brill S, van Erp HE, Hall A (February 1994). "Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases". J. Biol. Chem. 269 (2): 1137–42. PMID 8288572.
  2. ↑ "Entrez Gene: ARHGAP1 Rho GTPase activating protein 1".
  3. ↑ 3.0 3.1 Low BC, Lim YP, Lim J, Wong ES, Guy GR (November 1999). "Tyrosine phosphorylation of the Bcl-2-associated protein BNIP-2 by fibroblast growth factor receptor-1 prevents its binding to Cdc42GAP and Cdc42". J. Biol. Chem. 274 (46): 33123–30. doi:10.1074/jbc.274.46.33123. PMID 10551883.
  4. ↑ Low BC, Seow KT, Guy GR (December 2000). "The BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAP". J. Biol. Chem. 275 (48): 37742–51. doi:10.1074/jbc.M004897200. PMID 10954711.
  5. ↑ Nagata K, Puls A, Futter C, Aspenstrom P, Schaefer E, Nakata T et al. (January 1998). "The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3". EMBO J. 17 (1): 149–58. doi:10.1093/emboj/17.1.149. PMC 1170366. PMID 9427749.
  6. ↑ 6.0 6.1 Li R, Zhang B, Zheng Y (December 1997). "Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190". J. Biol. Chem. 272 (52): 32830–5. doi:10.1074/jbc.272.52.32830. PMID 9407060.
  7. ↑ 7.0 7.1 Zhang B, Chernoff J, Zheng Y (April 1998). "Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA". J. Biol. Chem. 273 (15): 8776–82. doi:10.1074/jbc.273.15.8776. PMID 9535855.
  8. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  9. ↑ Zhang B, Zheng Y (April 1998). "Regulation of RhoA GTP hydrolysis by the GTPase-activating proteins p190, p50RhoGAP, Bcr, and 3BP-1". Biochemistry 37 (15): 5249–57. doi:10.1021/bi9718447. PMID 9548756.

Further reading

  • Diekmann D, Brill S, Garrett MD, Totty N, Hsuan J, Monfries C et al. (1991). "Bcr encodes a GTPase-activating protein for p21rac". Nature 351 (6325): 400–2. doi:10.1038/351400a0. PMID 1903516.
  • Garrett MD, Major GN, Totty N, Hall A (1991). "Purification and N-terminal sequence of the p21rho GTPase-activating protein, rho GAP". Biochem. J. 276 ( Pt 3) (3): 833–6. PMC 1151079. PMID 1905930.
  • Barfod ET, Zheng Y, Kuang WJ, Hart MJ, Evans T, Cerione RA et al. (1993). "Cloning and expression of a human CDC42 GTPase-activating protein reveals a functional SH3-binding domain". J. Biol. Chem. 268 (35): 26059–62. PMID 8253717.
  • Aspenström P, Lindberg U, Hall A (1996). "Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome". Curr. Biol. 6 (1): 70–5. doi:10.1016/S0960-9822(02)00423-2. PMID 8805223. Vancouver style error (help)
  • Barrett T, Xiao B, Dodson EJ, Dodson G, Ludbrook SB, Nurmahomed K et al. (1997). "The structure of the GTPase-activating domain from p50rhoGAP". Nature 385 (6615): 458–61. doi:10.1038/385458a0. PMID 9009196.
  • Hu KQ, Settleman J (1997). "Tandem SH2 binding sites mediate the RasGAP-RhoGAP interaction: a conformational mechanism for SH3 domain regulation". EMBO J. 16 (3): 473–83. doi:10.1093/emboj/16.3.473. PMC 1169651. PMID 9034330.
  • Rittinger K, Walker PA, Eccleston JF, Nurmahomed K, Owen D, Laue E et al. (1997). "Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP". Nature 388 (6643): 693–7. doi:10.1038/41805. PMID 9262406.
  • Zhang B, Wang ZX, Zheng Y (1997). "Characterization of the interactions between the small GTPase Cdc42 and its GTPase-activating proteins and putative effectors. Comparison of kinetic properties of Cdc42 binding to the Cdc42-interactive domains". J. Biol. Chem. 272 (35): 21999–2007. doi:10.1074/jbc.272.35.21999. PMID 9268338.
  • Li R, Zhang B, Zheng Y (1997). "Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190". J. Biol. Chem. 272 (52): 32830–5. doi:10.1074/jbc.272.52.32830. PMID 9407060.
  • Zhang B, Zheng Y (1998). "Regulation of RhoA GTP hydrolysis by the GTPase-activating proteins p190, p50RhoGAP, Bcr, and 3BP-1". Biochemistry 37 (15): 5249–57. doi:10.1021/bi9718447. PMID 9548756.
  • Low BC, Lim YP, Lim J, Wong ES, Guy GR (1999). "Tyrosine phosphorylation of the Bcl-2-associated protein BNIP-2 by fibroblast growth factor receptor-1 prevents its binding to Cdc42GAP and Cdc42". J. Biol. Chem. 274 (46): 33123–30. doi:10.1074/jbc.274.46.33123. PMID 10551883.
  • Graham DL, Eccleston JF, Chung CW, Lowe PN (1999). "Magnesium fluoride-dependent binding of small G proteins to their GTPase-activating proteins". Biochemistry 38 (45): 14981–7. doi:10.1021/bi991358e. PMID 10555980.
  • Low BC, Seow KT, Guy GR (2000). "Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2". J. Biol. Chem. 275 (19): 14415–22. doi:10.1074/jbc.275.19.14415. PMID 10799524.
  • Low BC, Seow KT, Guy GR (2000). "The BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAP". J. Biol. Chem. 275 (48): 37742–51. doi:10.1074/jbc.M004897200. PMID 10954711.
  • Zhou YT, Soh UJ, Shang X, Guy GR, Low BC (2002). "The BNIP-2 and Cdc42GAP homology/Sec14p-like domain of BNIP-Salpha is a novel apoptosis-inducing sequence". J. Biol. Chem. 277 (9): 7483–92. doi:10.1074/jbc.M109459200. PMID 11741952.
  • Fidyk NJ, Cerione RA (2002). "Understanding the catalytic mechanism of GTPase-activating proteins: demonstration of the importance of switch domain stabilization in the stimulation of GTP hydrolysis". Biochemistry 41 (52): 15644–53. doi:10.1021/bi026413p. PMID 12501193.
  • Qin W, Hu J, Guo M, Xu J, Li J, Yao G et al. (2003). "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis". Biochem. Biophys. Res. Commun. 308 (2): 379–85. doi:10.1016/S0006-291X(03)01387-1. PMID 12901880.
  • Shang X, Zhou YT, Low BC (2003). "Concerted regulation of cell dynamics by BNIP-2 and Cdc42GAP homology/Sec14p-like, proline-rich, and GTPase-activating protein domains of a novel Rho GTPase-activating protein, BPGAP1". J. Biol. Chem. 278 (46): 45903–14. doi:10.1074/jbc.M304514200. PMID 12944407.