ARHGAP5

From Wikipedia, the free encyclopedia

Rho GTPase activating protein 5

Rendering based on PDB 2EE4.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2EE4, 2EE5

Identifiers

Symbols

ARHGAP5; GFI2; RhoGAP5; p190-B; p190BRhoGAP

External IDs

OMIM: 602680 MGI: 1332637 HomoloGene: 907 GeneCards: ARHGAP5 Gene

Gene Ontology
Molecular function	• GTPase activity • Rho GTPase activator activity • GTP binding • SH2 domain binding
Cellular component	• cytoplasm • cytosol • membrane
Biological process	• positive regulation of mesenchymal cell proliferation • GTP catabolic process • cell adhesion • small GTPase mediated signal transduction • Rho protein signal transduction • regulation of cell size • positive regulation of cell migration • positive regulation of Rho GTPase activity • regulation of small GTPase mediated signal transduction
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
32.55 – 32.63 Mb

Chr 12:
52.52 – 52.57 Mb

PubMed search

Rho GTPase-activating protein 5 is an enzyme that in humans is encoded by the ARHGAP5 gene.^[1]^[2]

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.^[2]

Interactions

ARHGAP5 has been shown to interact with Rnd1,^[3] Rnd2,^[3] Rnd3^[3] and RHOA.^[3]

References

↑ Burbelo PD, Miyamoto S, Utani A, Brill S, Yamada KM, Hall A, Yamada Y (Feb 1996). "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.
↑ 2.0 2.1 "Entrez Gene: ARHGAP5 Rho GTPase activating protein 5".
↑ 3.0 3.1 3.2 3.3 Wennerberg, Krister; Forget Marie-Annick, Ellerbroek Shawn M, Arthur William T, Burridge Keith, Settleman Jeffrey, Der Channing J, Hansen Steen H (Jul 2003). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Curr. Biol. (England) 13 (13): 1106–15. doi:10.1016/S0960-9822(03)00418-4. ISSN 0960-9822. PMID 12842009. Cite uses deprecated parameters (help)

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. 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. PMC 359251. PMID 7935432.
McGlade J, Brunkhorst B, Anderson D, et al. (1993). "The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion". EMBO J. 12 (8): 3073–81. PMC 413572. PMID 8344248.
Bonaldo MF, Lennon G, Soares MB (1997). "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, et al. (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, et al. (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, et al. (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.
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.
Shiota M, Tanihiro T, Nakagawa Y, et al. (2004). "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, et al. (2004). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Curr. Biol. 13 (13): 1106–15. doi:10.1016/S0960-9822(03)00418-4. PMID 12842009.
Su L, Agati JM, Parsons SJ (2004). "p190RhoGAP is cell cycle regulated and affects cytokinesis". J. Cell Biol. 163 (3): 571–82. doi:10.1083/jcb.200308007. PMC 2173658. PMID 14610059.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Colland F, Jacq X, Trouplin V, et al. (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, et al. (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, et al. (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.

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ARHGAP5

Interactions

References

Further reading