ARHGAP1

Rho GTPase activating protein 1

PDB rendering based on 1am4.

Available structures
PDB	1AM4, 1GRN, 1OW3, 1RGP, 1TX4, 2NGR

Identifiers

Symbols

ARHGAP1; CDC42GAP; RHOGAP; RHOGAP1; p50rhoGAP

External IDs

OMIM: 602732 MGI: 2445003 HomoloGene: 20909 GeneCards: ARHGAP1 Gene

Gene Ontology
Molecular function	• SH3/SH2 adaptor activity • GTPase activator activity • Rho GTPase activator activity • protein binding • SH3 domain binding • Rac GTPase activator activity
Cellular component	• ruffle • intracellular • cytoplasm • cytosol • plasma membrane • intracellular membrane-bounded organelle
Biological process	• signal transduction • small GTPase mediated signal transduction • small GTPase mediated signal transduction • Rho protein signal transduction • positive regulation of Rho GTPase activity • positive regulation of GTPase activity • regulation of small GTPase mediated signal transduction
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
46.7 – 46.72 Mb

Chr 2:
91.49 – 91.51 Mb

PubMed search

[1]

[2]

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 CDC42,^[3]^[4]^[5]^[6] BNIP2^[5]^[7] and RHOA.^[4]^[6]^[8]^[9]

References

^ 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.
^ "Entrez Gene: ARHGAP1 Rho GTPase activating protein 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=392.
^ Nagata, K i; Puls A, Futter C, Aspenstrom P, Schaefer E, Nakata T, Hirokawa N, Hall A (January 1998). "The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3". EMBO J. (ENGLAND) 17 (1): 149–58. doi:10.1093/emboj/17.1.149. ISSN 0261-4189. PMC 1170366. PMID 9427749. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1170366.
^ ^a ^b 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. (UNITED STATES) 272 (52): 32830–5. doi:10.1074/jbc.272.52.32830. ISSN 0021-9258. PMID 9407060.
^ ^a ^b Low, B C; Lim Y P, Lim J, Wong E S, Guy G R (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. (UNITED STATES) 274 (46): 33123–30. doi:10.1074/jbc.274.46.33123. ISSN 0021-9258. PMID 10551883.
^ ^a ^b 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. (UNITED STATES) 273 (15): 8776–82. doi:10.1074/jbc.273.15.8776. ISSN 0021-9258. PMID 9535855.
^ Low, B C; Seow K T, Guy G R (December 2000). "The BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAP". J. Biol. Chem. (UNITED STATES) 275 (48): 37742–51. doi:10.1074/jbc.M004897200. ISSN 0021-9258. PMID 10954711.
^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
^ Zhang, B; Zheng Y (April 1998). "Regulation of RhoA GTP hydrolysis by the GTPase-activating proteins p190, p50RhoGAP, Bcr, and 3BP-1". Biochemistry (UNITED STATES) 37 (15): 5249–57. doi:10.1021/bi9718447. ISSN 0006-2960. PMID 9548756.

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. PMC 1151079. PMID 1905930. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1151079.
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.
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.
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. PMC 1169651. PMID 9034330. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169651.
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. doi:10.1074/jbc.272.35.21999. 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. 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, 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. 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 (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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. doi:10.1021/bi026413p. 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. 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.

PDB gallery

1am4: COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)

1grn: CRYSTAL STRUCTURE OF THE CDC42/CDC42GAP/ALF3 COMPLEX.

1ow3: Crystal Structure of RhoA.GDP.MgF3-in Complex with RhoGAP

1rgp: GTPASE-ACTIVATION DOMAIN FROM RHOGAP

1tx4: RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX

2ngr: TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS BY CDC42: COMPARISONS OF THE HIGH RESOLUTION STRUCTURES FOR CDC42 BOUND TO THE ACTIVE AND CATALYTICALLY COMPROMISED FORMS OF THE CDC42-GAP.

ARHGAP1

Interactions

References

Further reading