ARHGAP5

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)
End	32,159,728 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	52,618,758 bp
RNA expression pattern
	Top expressed in
	Achilles tendon; ; endothelial cell; ; Brodmann area 23; ; corpus callosum; ; retinal pigment epithelium; ; corpus epididymis; ; caput epididymis; ; entorhinal cortex; ; ganglionic eminence; ; islet of Langerhans;
	Top expressed in
	ciliary body; ; retinal pigment epithelium; ; cerebellar vermis; ; spermatocyte; ; iris; ; parotid gland; ; substantia nigra; ; mammillary body; ; atrioventricular valve; ; primitive streak;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	GTP binding ; SH2 domain binding ; protein binding ; GTPase activator activity ; GTPase activity ;
Cellular component	endoplasmic reticulum ; membrane ; cytoplasm ; cytosol ; plasma membrane ;
Biological process	cell adhesion ; regulation of small GTPase mediated signal transduction ; Rho protein signal transduction ; signal transduction ; mammary gland development ; positive regulation of GTPase activity ;
	Sources:Amigo / QuickGO
Orthologs
	394
	11855
	ENSG00000100852
	ENSMUSG00000035133
	Q13017
	P97393
	NM_001030055 ; NM_001173
	NM_009706
	NP_001025226 ; NP_001164
	NP_033836
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 14, 2022

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

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]

Related Research Articles

The Rho family of GTPases is a family of small signaling G proteins, and is a subfamily of the Ras superfamily. The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic kingdoms, including yeasts and some plants. Three members of the family have been studied in detail: Cdc42, Rac1, and RhoA. All G proteins are "molecular switches", and Rho proteins play a role in organelle development, cytoskeletal dynamics, cell movement, and other common cellular functions.

Ras homolog gene family, member B, also known as RHOB, is a protein which in humans is encoded by the RHOB gene.

RAS p21 protein activator 1 or RasGAP, also known as RASA1, is a 120-kDa cytosolic human protein that provides two principal activities:

Rho GTPase-activating protein 1 is an enzyme that in humans is encoded by the ARHGAP1 gene.

Rho guanine nucleotide exchange factor 12 is a protein that in humans is encoded by the ARHGEF12 gene. This protein is also called RhoGEF12 or Leukemia-associated Rho guanine nucleotide exchange factor (LARG).

RhoG is a small monomeric GTP-binding protein, and is an important component of many intracellular signalling pathways. It is a member of the Rac subfamily of the Rho family of small G proteins and is encoded by the gene RHOG.

Rnd1 is a small signaling G protein, and is a member of the Rnd subgroup of the Rho family of GTPases. It is encoded by the gene RND1.

Rnd3 is a small signaling G protein, and is a member of the Rnd subgroup of the Rho family of GTPases. It is encoded by the gene RND3.

Rnd2 is a small signaling G protein, and is a member of the Rnd subgroup of the Rho family of GTPases. It is encoded by the gene RND2.

BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 is a protein that in humans is encoded by the BNIP2 gene.

The Ras superfamily, derived from "Rat sarcoma virus", is a protein superfamily of small GTPases. Members of the superfamily are divided into families and subfamilies based on their structure, sequence and function. The five main families are Ras, Rho, Ran, Rab and Arf GTPases. The Ras family itself is further divided into 6 subfamilies: Ras, Ral, Rap, Rheb, Rad and Rit. Miro is a recent contributor to the superfamily. Each subfamily shares the common core G domain, which provides essential GTPase and nucleotide exchange activity.

Rho GTPase-activating protein 32 is a protein that in humans is encoded by the RICS gene. RICS has two known isoforms, RICS that are expressed primarily at neurite growth cones, and at the post synaptic membranes, and PX-RICS which is more widely expressed in the endoplasmic reticulum, Golgi apparatus and endosomes. The only known domain of the RICS is the RhoGAP domain, whilst PX-RICS has an additional Phox homology and SH3 domain.

Rho GTPase activating protein 26 (ARHGAP26) also known as GTPase Regulator Associated with Focal Adhesion Kinase (GRAF) is a protein that in humans is encoded by the ARHGAP26 gene.

Rho GTPase-activating protein 24 is an enzyme that in humans is encoded by the ARHGAP24 gene.

Rho GTPase-activating protein 8 is a protein that in humans is encoded by the ARHGAP8 gene.

UBX domain-containing protein 11 is a protein that in humans is encoded by the UBXN11 gene.

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

The Rho GTPase activating protein 31 is encoded in humans by the ARHGAP31 gene. It is a Cdc42/Rac1 GTPase regulator.

ARHGAP29 is a gene located on chromosome 1p22 that encodes Rho GTPase activating protein (GAP) 29, a protein that mediates the cyclical regulation of small GTP binding proteins such as RhoA.

Rho GTPase activating protein 21 is a protein that in humans is encoded by the ARHGAP21 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000100852 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000035133 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 "Entrez Gene: ARHGAP5 Rho GTPase activating protein 5".
1 2 3 4 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 .

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. Bibcode:1990Natur.343..377E. doi:10.1038/343377a0. hdl: 1807/9436 . PMID 1689011. S2CID 4350408.
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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100852 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid8537347-5] 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.

[entrez-6] 1 2 "Entrez Gene: ARHGAP5 Rho GTPase activating protein 5".

[pmid12842009-7] 1 2 3 4 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.

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