MAGOH

Protein mago nashi homolog is a human protein encoded by the MAGOH gene. This gene encodes the mammalian homolog of the Drosophila mago nashi gene. In mammals, mRNA expression is not limited to the germplasm, but is ubiquitous in adult tissues and can be induced by serum stimulation of quiescent fibroblasts.

MAGOH
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1P27, 2HYI, 2J0Q, 2J0S, 2XB2, 3EX7
Identifiers
Aliases	MAGOH, MAGOH1, MAGOHA, mago homolog, exon junction complex core component, mago homolog, exon junction complex subunit
External IDs	OMIM: 602603; MGI: 1330312; HomoloGene: 1776; GeneCards: MAGOH; OMA:MAGOH - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p32.3 Start 53,226,900 bp End 53,238,518 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4 C7|4 50.18 cM Start 107,736,952 bp End 107,744,621 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte secondary oocyte monocyte olfactory zone of nasal mucosa rectum mucosa of transverse colon left lobe of thyroid gland ventricular zone body of uterus granulocyte Top expressed in zygote secondary oocyte yolk sac epiblast embryo ventricular zone embryo placenta morula primary oocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding RNA binding Cellular component cytoplasm nuclear speck catalytic step 2 spliceosome exon-exon junction complex nucleoplasm spliceosomal complex nucleus Biological process mRNA splicing, via spliceosome termination of RNA polymerase II transcription mRNA transport mRNA processing regulation of alternative mRNA splicing, via spliceosome mRNA export from nucleus nuclear-transcribed mRNA catabolic process, nonsense-mediated decay mRNA 3'-end processing regulation of translation RNA splicing RNA export from nucleus transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4116 17149 Ensembl ENSG00000162385 ENSMUSG00000028609 UniProt P61326 P61327 RefSeq (mRNA) NM_002370 NM_001282737 RefSeq (protein) NP_002361 NP_001269666 Location (UCSC) Chr 1: 53.23 – 53.24 Mb Chr 4: 107.74 – 107.74 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

In Drosophila

Drosophila flies produce unfit progeny when they have mutations in their mago nashi (Japanese: 孫なし, Hepburn: mago nashi, lit. 'grandchildless') gene. The progeny have defects in germplasm assembly and germline development.

Interactions

MAGOH interacts with RBM8A and NXF1.

In Drosophila melanogaster, Mago Nashi and Tsunagi/Y14 are core components of the exon junction complex. They complex with novel zinc finger protein Ranshi, which is involved in oocyte differentiation.

Further reading

• Newmark PA, Mohr SE, Gong L, Boswell RE (1997). "mago nashi mediates the posterior follicle cell-to-oocyte signal to organize axis formation in Drosophila". Development. 124 (16): 3197–207. doi:10.1242/dev.124.16.3197. PMID 9272960.
• Zhao XF, Nowak NJ, Shows TB, Aplan PD (2000). "MAGOH interacts with a novel RNA-binding protein". Genomics. 63 (1): 145–8. doi:10.1006/geno.1999.6064. PMID 10662555.
• Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
• Mingot JM, Kostka S, Kraft R, et al. (2001). "Importin 13: a novel mediator of nuclear import and export". EMBO J. 20 (14): 3685–94. doi:10.1093/emboj/20.14.3685. PMC 125545. PMID 11447110.
• Hachet O, Ephrussi A (2002). "Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport". Curr. Biol. 11 (21): 1666–74. doi:10.1016/S0960-9822(01)00508-5. PMID 11696323. S2CID 2373806.
• Kataoka N, Diem MD, Kim VN, et al. (2002). "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex". EMBO J. 20 (22): 6424–33. doi:10.1093/emboj/20.22.6424. PMC 125744. PMID 11707413.
• Jurica MS, Licklider LJ, Gygi SR, et al. (2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA. 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Fribourg S, Gatfield D, Izaurralde E, Conti E (2003). "A novel mode of RBD-protein recognition in the Y14-Mago complex". Nat. Struct. Biol. 10 (6): 433–9. doi:10.1038/nsb926. PMID 12730685. S2CID 40116577.
• Lau CK, Diem MD, Dreyfuss G, Van Duyne GD (2004). "Structure of the Y14-Magoh core of the exon junction complex". Curr. Biol. 13 (11): 933–41. doi:10.1016/S0960-9822(03)00328-2. PMID 12781131. S2CID 14752714.
• Chan CC, Dostie J, Diem MD, et al. (2004). "eIF4A3 is a novel component of the exon junction complex". RNA. 10 (2): 200–9. doi:10.1261/rna.5230104. PMC 1370532. PMID 14730019.
• Palacios IM, Gatfield D, St Johnston D, Izaurralde E (2004). "An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay". Nature. 427 (6976): 753–7. Bibcode:2004Natur.427..753P. doi:10.1038/nature02351. PMID 14973490. S2CID 4400243.
• Jin J, Smith FD, Stark C, et al. (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. Bibcode:2004CBio...14.1436J. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Ballut L, Marchadier B, Baguet A, et al. (2005). "The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity". Nat. Struct. Mol. Biol. 12 (10): 861–9. doi:10.1038/nsmb990. PMID 16170325. S2CID 1359792.
• Gehring NH, Kunz JB, Neu-Yilik G, et al. (2005). "Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements". Mol. Cell. 20 (1): 65–75. doi:10.1016/j.molcel.2005.08.012. PMID 16209946.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
• Andersen CB, Ballut L, Johansen JS, et al. (2006). "Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA". Science. 313 (5795): 1968–72. Bibcode:2006Sci...313.1968A. doi:10.1126/science.1131981. PMID 16931718. S2CID 26409491.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Quaresma AJ, Sievert R, Nickerson JA (2013). "Regulation of mRNA export by the PI3 kinase/AKT signal transduction pathway". Mol. Biol. Cell. 24 (8): 1208–21. doi:10.1091/mbc.E12-06-0450. PMC 3623641. PMID 23427269.