ARHGAP5

Rho GTPase-activating protein 5 is an enzyme that in humans is encoded by the ARHGAP5 gene.[5][6]

ARHGAP5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2EE4, 2EE5
Identifiers
Aliases	ARHGAP5, GFI2, RhoGAP5, p190-B, p190BRhoGAP, Rho GTPase activating protein 5
External IDs	OMIM: 602680 MGI: 1332637 HomoloGene: 907 GeneCards: ARHGAP5
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q12 Start 32,076,114 bp[1] End 32,159,728 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12 C1|12 22.16 cM Start 52,503,972 bp[2] End 52,571,975 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GTP binding • SH2 domain binding • GO:0001948 protein binding • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity • GTPase activity Cellular component • endoplasmic reticulum • membrane • cytoplasm • cytosol • cell membrane Biological process • cell adhesion • regulation of small GTPase mediated signal transduction • Rho protein signal transduction • signal transduction • mammary gland development • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	394	11855
Ensembl	ENSG00000100852	ENSMUSG00000035133
UniProt	Q13017	P97393
RefSeq (mRNA)	NM_001030055 NM_001173	NM_009706
RefSeq (protein)	NP_001025226 NP_001164	NP_033836
Location (UCSC)	Chr 14: 32.08 – 32.16 Mb	Chr 12: 52.5 – 52.57 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Rho GTPase activating protein 5 negatively regulates RHO GTPases, a family that may mediate cytoskeleton changes by stimulating the hydrolysis of bound GTP. Two transcript variants encoding different isoforms have been found for this gene.[6]

Interactions

ARHGAP5 has been shown to interact with Rnd1,[7] Rnd2,[7] Rnd3[7] and RHOA.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000100852 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000035133 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Burbelo PD, Miyamoto S, Utani A, Brill S, Yamada KM, Hall A, Yamada Y (1995). "p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking". J. Biol. Chem. 270 (52): 30919–26. doi:10.1074/jbc.270.52.30919. PMID 8537347.
6. "Entrez Gene: ARHGAP5 Rho GTPase activating protein 5".
7. Wennerberg K, Forget MA, Ellerbroek SM, Arthur WT, Burridge K, Settleman J, Der CJ, Hansen SH (Jul 2003). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Curr. Biol. 13 (13): 1106–15. doi:10.1016/S0960-9822(03)00418-4. PMC 6918695. PMID 12842009.

External links

• Human ARHGAP5 genome location and ARHGAP5 gene details page in the UCSC Genome Browser.

Further reading

• Ellis C, Moran M, McCormick F, Pawson T (1990). "Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases". Nature. 343 (6256): 377–81. doi:10.1038/343377a0. hdl:1807/9436. PMID 1689011.
• Foster R, Hu KQ, Shaywitz DA, Settleman J (1994). "p190 RhoGAP, the major RasGAP-associated protein, binds GTP directly". Mol. Cell. Biol. 14 (11): 7173–81. doi:10.1128/mcb.14.11.7173. PMC 359251. PMID 7935432.
• McGlade J, Brunkhorst B, Anderson D, Mbamalu G, Settleman J, Dedhar S, Rozakis-Adcock M, Chen LB, Pawson T (1993). "The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion". EMBO J. 12 (8): 3073–81. doi:10.1002/j.1460-2075.1993.tb05976.x. PMC 413572. PMID 8344248.
• Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Zrihan-Licht S, Fu Y, Settleman J, Schinkmann K, Shaw L, Keydar I, Avraham S, Avraham H (2000). "RAFTK/Pyk2 tyrosine kinase mediates the association of p190 RhoGAP with RasGAP and is involved in breast cancer cell invasion". Oncogene. 19 (10): 1318–28. doi:10.1038/sj.onc.1203422. PMID 10713673.
• Kulkarni SV, Gish G, van der Geer P, Henkemeyer M, Pawson T (2000). "Role of p120 Ras-GAP in directed cell movement". J. Cell Biol. 149 (2): 457–70. doi:10.1083/jcb.149.2.457. PMC 2175152. PMID 10769036.
• Chakravarty G, Roy D, Gonzales M, Gay J, Contreras A, Rosen JM (2000). "P190-B, a Rho-GTPase-activating protein, is differentially expressed in terminal end buds and breast cancer". Cell Growth Differ. 11 (7): 343–54. PMID 10939588.
• Shiota M, Tanihiro T, Nakagawa Y, Aoki N, Ishida N, Miyazaki K, Ullrich A, Miyazaki H (2003). "Protein tyrosine phosphatase PTP20 induces actin cytoskeleton reorganization by dephosphorylating p190 RhoGAP in rat ovarian granulosa cells stimulated with follicle-stimulating hormone". Mol. Endocrinol. 17 (4): 534–49. doi:10.1210/me.2002-0187. PMID 12554790.
• Wennerberg K, Forget MA, Ellerbroek SM, Arthur WT, Burridge K, Settleman J, Der CJ, Hansen SH (2003). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Curr. Biol. 13 (13): 1106–15. doi:10.1016/S0960-9822(03)00418-4. PMC 6918695. PMID 12842009.
• Su L, Agati JM, Parsons SJ (2003). "p190RhoGAP is cell cycle regulated and affects cytokinesis". J. Cell Biol. 163 (3): 571–82. doi:10.1083/jcb.200308007. PMC 2173658. PMID 14610059.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Blanchetot C, Chagnon M, Dubé N, Hallé M, Tremblay ML (2005). "Substrate-trapping techniques in the identification of cellular PTP targets". Methods. 35 (1): 44–53. doi:10.1016/j.ymeth.2004.07.007. PMID 15588985.
• Vargo-Gogola T, Heckman BM, Gunther EJ, Chodosh LA, Rosen JM (2006). "P190-B Rho GTPase-activating protein overexpression disrupts ductal morphogenesis and induces hyperplastic lesions in the developing mammary gland". Mol. Endocrinol. 20 (6): 1391–405. doi:10.1210/me.2005-0426. PMID 16469769.
• Zhan X, Desiderio DM (2006). "Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry". Anal. Biochem. 354 (2): 279–89. doi:10.1016/j.ab.2006.05.024. PMID 16777052.