ARHGAP1

From Wikipedia, the free encyclopedia

Rho GTPase activating protein 1

PDB rendering based on 1am4.

Available structures: 1am4, 1grn, 1ow3, 1rgp, 1tx4, 2ngr

Identifiers

Symbol(s)

ARHGAP1; CDC42GAP; RHOGAP; RHOGAP1; p50rhoGAP

External IDs

OMIM: 602732 MGI: 2445003 HomoloGene: 20909

Gene ontology
Molecular Function:	• SH3/SH2 adaptor activity • GTPase activator activity • Rho GTPase activator activity • protein binding • GTP binding • Rac GTPase activator activity
Cellular Component:	• cellular_component • intracellular
Biological Process:	• cytoskeleton organization and biogenesis • signal transduction • small GTPase mediated signal transduction • Rho protein signal transduction • regulation of GTPase activity

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_004308 (mRNA)
NP_004299 (protein)

NM_146124 (mRNA)
NP_666236 (protein)

Location

Chr 11: 46.66 - 46.68 Mb

Chr 2: 91.45 - 91.47 Mb

Pubmed search

[1]

[2]

Rho GTPase activating protein 1, also known as ARHGAP1, is a human gene.^[1]

[edit] References

^ Entrez Gene: ARHGAP1 Rho GTPase activating protein 1.

[edit] Further reading

Diekmann D, Brill S, Garrett MD, 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): 833–6. PMID 1905930.
Barfod ET, Zheng Y, Kuang WJ, et al. (1994). "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.
Lancaster CA, Taylor-Harris PM, Self AJ, et al. (1994). "Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases.". J. Biol. Chem. 269 (2): 1137–42. PMID 8288572.
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. PMID 8805223.
Barrett T, Xiao B, Dodson EJ, 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. PMID 9034330.
Rittinger K, Walker PA, Eccleston JF, 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. PMID 9268338.
Li R, Zhang B, Zheng Y (1998). "Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190.". J. Biol. Chem. 272 (52): 32830–5. 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, et al. (2000). "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. 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. 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. PMID 10799524.
Low BC, Seow KT, Guy GR (2001). "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, et al. (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.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Fidyk NJ, Cerione RA (2003). "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. PMID 12501193.
Qin W, Hu J, Guo M, 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. 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.