ARHGEF2

Rho guanine nucleotide exchange factor 2 is a protein that in humans is encoded by the ARHGEF2 gene.[5][6][7]

ARHGEF2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5EFX
Identifiers
Aliases	ARHGEF2, GEF, GEF-H1, GEFH1, LFP40, P40, Rho/Rac guanine nucleotide exchange factor 2, NEDMHM, Lfc
External IDs	OMIM: 607560 MGI: 103264 HomoloGene: 3468 GeneCards: ARHGEF2
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q22 Start 155,946,851 bp[1] End 156,007,070 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 F1 Start 88,605,966 bp[2] End 88,648,052 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • Rac guanyl-nucleotide exchange factor activity • Rac GTPase binding • microtubule binding • zinc ion binding • transcription factor binding • metal ion binding • GO:0001948 protein binding • Rho GTPase binding • Rho guanyl-nucleotide exchange factor activity • guanyl-nucleotide exchange factor activity Cellular component • cytoplasm • vesicle • cytosol • Golgi apparatus • cell projection • membrane • focal adhesion • bicellular tight junction • spindle • cell membrane • dendritic shaft • ruffle membrane • cell junction • neuronal cell body • microtubule • cytoskeleton • cytoplasmic vesicle • podosome • GO:0097483, GO:0097481 postsynaptic density • macromolecular complex • glutamatergic synapse • postsynaptic density, intracellular component Biological process • GO:0007243 intracellular signal transduction • negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress • negative regulation of necroptotic process • actin filament organization • immune system process • negative regulation of neurogenesis • cellular response to tumor necrosis factor • cell division • cellular response to muramyl dipeptide • cellular hyperosmotic response • negative regulation of microtubule depolymerization • regulation of cell proliferation • positive regulation of NF-kappaB transcription factor activity • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors • cell morphogenesis • establishment of mitotic spindle orientation • positive regulation of interleukin-6 production • positive regulation of tumor necrosis factor production • positive regulation of apoptotic process • positive regulation of peptidyl-tyrosine phosphorylation • cell cycle • regulation of Rho protein signal transduction • intracellular protein transport • innate immune system • regulation of small GTPase mediated signal transduction • positive regulation of transcription from RNA polymerase II promoter • negative regulation of podosome assembly • G-protein coupled receptor signaling pathway • positive regulation of neuron differentiation • asymmetric neuroblast division • positive regulation of neuron migration • multicellular organism development • nervous system development • cell differentiation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9181	16800
Ensembl	ENSG00000116584	ENSMUSG00000028059
UniProt	Q92974	Q60875
RefSeq (mRNA)	NM_001162383 NM_001162384 NM_004723 NM_001350110 NM_001350111 NM_001350112	NM_001198911 NM_001198912 NM_001198913 NM_008487 NM_001377126
RefSeq (protein)	NP_001155855 NP_001155856 NP_004714 NP_001337039 NP_001337040 NP_001337041	NP_001185840 NP_001185841 NP_001185842 NP_032513 NP_001364055
Location (UCSC)	Chr 1: 155.95 – 156.01 Mb	Chr 3: 88.61 – 88.65 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Rho GTPases play a fundamental role in numerous cellular processes that are initiated by extracellular stimuli that work through G protein-coupled receptors. The encoded protein may form complex with G proteins and stimulate rho-dependent signals.[7]

Interactions

ARHGEF2 has been shown to interact with PAK1.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000116584 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028059 - 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. Ren Y, Li R, Zheng Y, Busch H (Feb 1999). "Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases". J Biol Chem. 273 (52): 34954–60. doi:10.1074/jbc.273.52.34954. PMID 9857026.
6. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Dec 1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (3): 169–76. doi:10.1093/dnares/5.3.169. PMID 9734811.
7. "Entrez Gene: ARHGEF2 rho/rac guanine nucleotide exchange factor (GEF) 2".
8. Zenke FT, Krendel M, DerMardirossian C, King CC, Bohl BP, Bokoch GM (Apr 2004). "p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor". J. Biol. Chem. 279 (18): 18392–400. doi:10.1074/jbc.M400084200. PMID 14970201.

External links

• Human ARHGEF2 genome location and ARHGEF2 gene details page in the UCSC Genome Browser.

Further reading

• Ehrhardt A, Ehrhardt GR, Guo X, Schrader JW (2002). "Ras and relatives--job sharing and networking keep an old family together". Exp. Hematol. 30 (10): 1089–106. doi:10.1016/S0301-472X(02)00904-9. PMID 12384139.
• Reddy AB, Chatterjee A, Rothblum LI, Black A, Busch H (1989). "Isolation and characterization of complementary DNA to proliferating cell nucleolar antigen P40". Cancer Res. 49 (7): 1763–7. PMID 2466560.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
• Gao Y, Xing J, Streuli M, Leto TL, Zheng Y (2002). "Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors". J. Biol. Chem. 276 (50): 47530–41. doi:10.1074/jbc.M108865200. PMID 11595749.
• Krendel M, Zenke FT, Bokoch GM (2002). "Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton". Nat. Cell Biol. 4 (4): 294–301. doi:10.1038/ncb773. PMID 11912491.
• Brajenovic M, Joberty G, Küster B, Bouwmeester T, Drewes G (2004). "Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network". J. Biol. Chem. 279 (13): 12804–11. doi:10.1074/jbc.M312171200. PMID 14676191.
• Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
• Zenke FT, Krendel M, DerMardirossian C, King CC, Bohl BP, Bokoch GM (2004). "p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor". J. Biol. Chem. 279 (18): 18392–400. doi:10.1074/jbc.M400084200. PMID 14970201.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (2004). "From ORFeome to Biology: A Functional Genomics Pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
• Callow MG, Zozulya S, Gishizky ML, Jallal B, Smeal T (2005). "PAK4 mediates morphological changes through the regulation of GEF-H1". J. Cell Sci. 118 (Pt 9): 1861–72. doi:10.1242/jcs.02313. PMID 15827085.
• Aijaz S, D'Atri F, Citi S, Balda MS, Matter K (2005). "Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition". Dev. Cell. 8 (5): 777–86. doi:10.1016/j.devcel.2005.03.003. PMID 15866167.
• 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 (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.