ARHGAP9

Rho GTPase activating protein 9
PDB rendering based on 2p0d.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2P0D​, 2P0F​, 2P0H​
Identifiers
Symbols	ARHGAP9 ; 10C; RGL1
External IDs	OMIM: 610576 HomoloGene: 13041 GeneCards: ARHGAP9 Gene
Gene ontology Molecular function • GTPase activator activity • protein binding • phosphatidylinositol-3,4,5-trisphosphate binding Cellular component • cytosol Biological process • small GTPase mediated signal transduction • positive regulation of GTPase activity • regulation of small GTPase mediated signal transduction Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	64333	216445
Ensembl	ENSG00000123329	ENSMUSG00000040345
UniProt	Q9BRR9	Q1HDU4
RefSeq (mRNA)	NM_001080156	NM_001285785
RefSeq (protein)	NP_001073625	NP_001272714
Location (UCSC)	Chr 12: 57.47 – 57.49 Mb	Chr 10: 127.32 – 127.33 Mb
PubMed search

Rho GTPase-activating protein 9 is an enzyme that in humans is encoded by the ARHGAP9 gene.^[1][2]

Function

This gene encodes a member of the Rho-GAP family of GTPase activating proteins. The protein has substantial GAP activity towards several Rho-family GTPases in vitro, converting them to an inactive GDP-bound state. It is implicated in regulating adhesion of hematopoietic cells to the extracellular matrix. Multiple transcript variants encoding different isoforms have been found for this gene.^[2]

References

1. Furukawa Y, Kawasoe T, Daigo Y, Nishiwaki T, Ishiguro H, Takahashi M, Kitayama J, Nakamura Y (Jun 2001). "Isolation of a novel human gene, ARHGAP9, encoding a rho-GTPase activating protein". Biochemical and Biophysical Research Communications 284 (3): 643–9. doi:10.1006/bbrc.2001.5022. PMID 11396949.
2. "Entrez Gene: ARHGAP9 Rho GTPase activating protein 9".

Further reading

• Peck J, Douglas G, Wu CH, Burbelo PD (Sep 2002). "Human RhoGAP domain-containing proteins: structure, function and evolutionary relationships". FEBS Letters 528 (1-3): 27–34. doi:10.1016/S0014-5793(02)03331-8. PMID 12297274.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (Jan 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.