ARHGEF2

Mammalian protein found in Homo sapiens
ARHGEF2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

5EFX

Identifiers
AliasesARHGEF2, GEF, GEF-H1, GEFH1, LFP40, P40, Rho/Rac guanine nucleotide exchange factor 2, NEDMHM, Lfc
External IDsOMIM: 607560; MGI: 103264; HomoloGene: 3468; GeneCards: ARHGEF2; OMA:ARHGEF2 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for ARHGEF2
Genomic location for ARHGEF2
Band1q22Start155,946,851 bp[1]
End156,007,070 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for ARHGEF2
Genomic location for ARHGEF2
Band3|3 F1Start88,513,273 bp[2]
End88,555,359 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • inferior ganglion of vagus nerve

  • ganglionic eminence

  • corpus callosum

  • C1 segment

  • olfactory bulb

  • blood

  • granulocyte

  • sural nerve

  • upper lobe of left lung

  • right lung
Top expressed in
  • spermatid

  • seminiferous tubule

  • superior frontal gyrus

  • granulocyte

  • dentate gyrus of hippocampal formation granule cell

  • ventricular zone

  • primary visual cortex

  • neural layer of retina

  • neural tube

  • thymus
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • microtubule binding
  • zinc ion binding
  • transcription factor binding
  • metal ion binding
  • protein binding
  • guanyl-nucleotide exchange factor activity
Cellular component
  • cytoplasm
  • vesicle
  • cytosol
  • Golgi apparatus
  • cell projection
  • membrane
  • focal adhesion
  • bicellular tight junction
  • spindle
  • plasma membrane
  • dendritic shaft
  • ruffle membrane
  • cell junction
  • neuronal cell body
  • microtubule
  • cytoskeleton
  • cytoplasmic vesicle
  • podosome
  • postsynaptic density
  • protein-containing complex
  • glutamatergic synapse
  • postsynaptic density, intracellular component
Biological process
  • 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 population 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 response
  • regulation of small GTPase mediated signal transduction
  • positive regulation of transcription by RNA polymerase II
  • 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
SpeciesHumanMouse
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 MbChr 3: 88.51 – 88.56 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000116584 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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

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. S2CID 25681168.
  • 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. S2CID 11683986.
  • 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. Bibcode:2004PNAS..10112130B. 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. S2CID 2371325.
  • 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • 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.


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