ARHGAP5

From Wikipedia, the free encyclopedia

Rho GTPase activating protein 5

Identifiers

ARHGAP5; RhoGAP5; p190-B

External IDs

OMIM: 602680 MGI: 1332637 HomoloGene: 907

Gene ontology
Molecular Function:	• GTPase activity • GTPase activator activity • Rho GTPase activator activity • GTP binding • SH2 domain binding
Cellular Component:	• intracellular • cytoplasm • membrane
Biological Process:	• cell adhesion • signal transduction • small GTPase mediated signal transduction • Rho protein signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001030055 (mRNA)
NP_001025226 (protein)

NM_009706 (mRNA)
NP_033836 (protein)

Location

Chr 14: 31.62 - 31.7 Mb

Chr 12: 53.44 - 53.49 Mb

Pubmed search

[1]

[2]

Rho GTPase activating protein 5, also known as ARHGAP5, is a human gene.^[1]

Rho GTPase activating protein 5 negatively regulates RHO GTPases, a family which may mediate cytoskeleton changes by stimulating the hydrolysis of bound GTP. Two transcript variants encoding different isoforms have been found for this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: ARHGAP5 Rho GTPase activating protein 5.

[edit] 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. 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. 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. PMID 8344248.
Burbelo PD, Miyamoto S, Utani A, et al. (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. PMID 8537347.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. 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. 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. 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. 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. 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. 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.