ARHGAP9

ARHGAP9
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesARHGAP9, 10C, RGL1, Rho GTPase activating protein 9
External IDsMGI: 2143764 HomoloGene: 13041 GeneCards: ARHGAP9
Gene location (Human)
Chr.Chromosome 12 (human)[1]
Band12q13.3Start57,472,255 bp[1]
End57,488,814 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

64333

216445

Ensembl

ENSG00000123329

ENSMUSG00000040345

UniProt

Q9BRR9

n/a

RefSeq (mRNA)

NM_001285785
NM_146011
NM_001359656
NM_001359657

RefSeq (protein)

n/a

Location (UCSC)Chr 12: 57.47 – 57.49 MbChr 10: 127.32 – 127.33 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Rho GTPase-activating protein 9 is an enzyme that in humans is encoded by the ARHGAP9 gene.[5][6]

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.[6]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000123329 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000040345 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ 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.
  6. 1 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.


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