MGN_HUMAN
ID MGN_HUMAN Reviewed; 146 AA.
AC P61326; B1ARP8; B2R5A2; O35169; P50606; Q5SW69;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Protein mago nashi homolog;
GN Name=MAGOH; Synonyms=MAGOHA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9479507; DOI=10.1006/geno.1997.5126;
RA Zhao X.F., Colaizzo-Anas T., Nowak N.J., Shows T.B., Elliott R.W.,
RA Aplan P.D.;
RT "The mammalian homologue of mago nashi encodes a serum-inducible protein.";
RL Genomics 47:319-322(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH RBM8A.
RX PubMed=10662555; DOI=10.1006/geno.1999.6064;
RA Zhao X.F., Nowak N.J., Shows T.B., Aplan P.D.;
RT "MAGOH interacts with a novel RNA-binding protein.";
RL Genomics 63:145-148(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH RBM8A.
RX PubMed=12730685; DOI=10.1038/nsb926;
RA Fribourg S., Gatfield D., Izaurralde E., Conti E.;
RT "A novel mode of RBD-protein recognition in the Y14-Mago complex.";
RL Nat. Struct. Biol. 10:433-439(2003).
RN [10]
RP INTERACTION WITH PYM1.
RX PubMed=14968132; DOI=10.1038/sj.embor.7400091;
RA Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E., Conti E.;
RT "Molecular insights into the interaction of PYM with the Mago-Y14 core of
RT the exon junction complex.";
RL EMBO Rep. 5:304-310(2004).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF 16-LYS-GLU-17; 41-LYS-ASN-42; 66-ASP--GLU-68;
RP 72-GLU-ASP-73; 85-ARG--GLU-87; 130-LYS--PHE-134 AND LEU-136.
RX PubMed=16209946; DOI=10.1016/j.molcel.2005.08.012;
RA Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W.,
RA Kulozik A.E.;
RT "Exon-junction complex components specify distinct routes of nonsense-
RT mediated mRNA decay with differential cofactor requirements.";
RL Mol. Cell 20:65-75(2005).
RN [12]
RP IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX.
RX PubMed=16170325; DOI=10.1038/nsmb990;
RA Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H.;
RT "The exon junction core complex is locked onto RNA by inhibition of
RT eIF4AIII ATPase activity.";
RL Nat. Struct. Mol. Biol. 12:861-869(2005).
RN [13]
RP IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA
RP SPLICING-DEPENDENT EXON JUNCTION COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16314458; DOI=10.1261/rna.2155905;
RA Tange T.O., Shibuya T., Jurica M.S., Moore M.J.;
RT "Biochemical analysis of the EJC reveals two new factors and a stable
RT tetrameric protein core.";
RL RNA 11:1869-1883(2005).
RN [14]
RP INTERACTION WITH PYM1.
RX PubMed=18026120; DOI=10.1038/nsmb1321;
RA Diem M.D., Chan C.C., Younis I., Dreyfuss G.;
RT "PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance
RT translation of spliced mRNAs.";
RL Nat. Struct. Mol. Biol. 14:1173-1179(2007).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP INTERACTION WITH PYM1, AND MUTAGENESIS OF GLU-68; GLU-72; ASP-73 AND
RP GLU-117.
RX PubMed=19410547; DOI=10.1016/j.cell.2009.02.042;
RA Gehring N.H., Lamprinaki S., Kulozik A.E., Hentze M.W.;
RT "Disassembly of exon junction complexes by PYM.";
RL Cell 137:536-548(2009).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=19324961; DOI=10.1261/rna.1387009;
RA Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P.,
RA Wachsmuth M.;
RT "Assembly and mobility of exon-exon junction complexes in living cells.";
RL RNA 15:862-876(2009).
RN [18]
RP FUNCTION.
RX PubMed=22203037; DOI=10.1128/mcb.06130-11;
RA Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M.,
RA Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R.,
RA Elela S.A., Prinos P., Chabot B.;
RT "Proteins associated with the exon junction complex also control the
RT alternative splicing of apoptotic regulators.";
RL Mol. Cell. Biol. 32:954-967(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP FUNCTION, AND SUBUNIT.
RX PubMed=23917022; DOI=10.4161/rna.25827;
RA Singh K.K., Wachsmuth L., Kulozik A.E., Gehring N.H.;
RT "Two mammalian MAGOH genes contribute to exon junction complex composition
RT and nonsense-mediated decay.";
RL RNA Biol. 10:1291-1298(2013).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RBM8A.
RX PubMed=12781131; DOI=10.1016/s0960-9822(03)00328-2;
RA Lau C.K., Diem M.D., Dreyfuss G., Van Duyne G.D.;
RT "Structure of the Y14-Magoh core of the exon junction complex.";
RL Curr. Biol. 13:933-941(2003).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3;
RP EIF4A3; RBM8A AND AMP-PNP.
RX PubMed=16923391; DOI=10.1016/j.cell.2006.08.006;
RA Bono F., Ebert J., Lorentzen E., Conti E.;
RT "The crystal structure of the exon junction complex reveals how it
RT maintains a stable grip on mRNA.";
RL Cell 126:713-725(2006).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3;
RP EIF4A3; RBM8A AND ADP-NP.
RX PubMed=16931718; DOI=10.1126/science.1131981;
RA Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H.,
RA Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R.;
RT "Structure of the exon junction core complex with a trapped DEAD-box ATPase
RT bound to RNA.";
RL Science 313:1968-1972(2006).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3;
RP EIF4A3; RBM8A AND TRANSITION STATE ANALOG ADP-ALF3.
RX PubMed=19033377; DOI=10.1261/rna.1283109;
RA Nielsen K.H., Chamieh H., Andersen C.B., Fredslund F., Hamborg K.,
RA Le Hir H., Andersen G.R.;
RT "Mechanism of ATP turnover inhibition in the EJC.";
RL RNA 15:67-75(2009).
RN [26] {ECO:0007744|PDB:2XB2}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) IN THE EJC COMPLEX WITH CASC3;
RP EIF4A3; RBM8A; UPF3B; UPF2 AND RNA, AND IDENTIFICATION IN THE EJC CORE
RP COMPLEX WITH UPF3A.
RX PubMed=20479275; DOI=10.1073/pnas.1000993107;
RA Buchwald G., Ebert J., Basquin C., Sauliere J., Jayachandran U., Bono F.,
RA Le Hir H., Conti E.;
RT "Insights into the recruitment of the NMD machinery from the crystal
RT structure of a core EJC-UPF3b complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10050-10055(2010).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome (PubMed:11991638). Plays a redundant role with MAGOHB as
CC core component of the exon junction complex (EJC) and in the nonsense-
CC mediated decay (NMD) pathway (PubMed:23917022). The EJC is a dynamic
CC structure consisting of core proteins and several peripheral nuclear
CC and cytoplasmic associated factors that join the complex only
CC transiently either during EJC assembly or during subsequent mRNA
CC metabolism. The EJC marks the position of the exon-exon junction in the
CC mature mRNA for the gene expression machinery and the core components
CC remain bound to spliced mRNAs throughout all stages of mRNA metabolism
CC thereby influencing downstream processes including nuclear mRNA export,
CC subcellular mRNA localization, translation efficiency and nonsense-
CC mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the
CC ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto
CC spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer
CC interacts with the EJC key regulator PYM1 leading to EJC disassembly in
CC the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs
CC by recruiting them to the ribosomal 48S preinitiation complex. Involved
CC in the splicing modulation of BCL2L1/Bcl-X (and probably other
CC apoptotic genes); specifically inhibits formation of proapoptotic
CC isoforms such as Bcl-X(S); the function is different from the
CC established EJC assembly. {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12730685, ECO:0000269|PubMed:16209946,
CC ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:23917022}.
CC -!- SUBUNIT: Heterodimer with RBM8A (PubMed:12730685, PubMed:12781131,
CC PubMed:23917022). Core component of the mRNA splicing-dependent exon
CC junction complex (EJC); the core complex contains CASC3, EIF4A3, MAGOH
CC or MAGOHB, and RBM8A (PubMed:11991638, PubMed:16170325,
CC PubMed:16314458, PubMed:23917022, PubMed:16923391, PubMed:16931718,
CC PubMed:19033377, PubMed:20479275). Interacts with PYM1; the interaction
CC is direct and dissociates the EJC from spliced mRNAs (PubMed:14968132,
CC PubMed:18026120, PubMed:19410547). Identified in a complex composed of
CC the EJC core, UPF3B and UPF2. The EJC core can also interact with UPF3A
CC (in vitro) (PubMed:20479275). Identified in the spliceosome C complex
CC (PubMed:11991638). {ECO:0000269|PubMed:10662555,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12730685,
CC ECO:0000269|PubMed:12781131, ECO:0000269|PubMed:14968132,
CC ECO:0000269|PubMed:16170325, ECO:0000269|PubMed:16314458,
CC ECO:0000269|PubMed:16923391, ECO:0000269|PubMed:16931718,
CC ECO:0000269|PubMed:18026120, ECO:0000269|PubMed:19033377,
CC ECO:0000269|PubMed:19410547, ECO:0000269|PubMed:20479275,
CC ECO:0000269|PubMed:23917022}.
CC -!- INTERACTION:
CC P61326; O15234: CASC3; NbExp=24; IntAct=EBI-299134, EBI-299118;
CC P61326; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-299134, EBI-739624;
CC P61326; Q9BQC3: DPH2; NbExp=3; IntAct=EBI-299134, EBI-10237931;
CC P61326; Q7L190: DPPA4; NbExp=3; IntAct=EBI-299134, EBI-710457;
CC P61326; P38919: EIF4A3; NbExp=30; IntAct=EBI-299134, EBI-299104;
CC P61326; P51114-2: FXR1; NbExp=3; IntAct=EBI-299134, EBI-11022345;
CC P61326; Q08379: GOLGA2; NbExp=6; IntAct=EBI-299134, EBI-618309;
CC P61326; O94829: IPO13; NbExp=4; IntAct=EBI-299134, EBI-747310;
CC P61326; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-299134, EBI-10293968;
CC P61326; Q9BRP8: PYM1; NbExp=16; IntAct=EBI-299134, EBI-2352802;
CC P61326; Q9Y5S9: RBM8A; NbExp=40; IntAct=EBI-299134, EBI-447231;
CC P61326; Q9Y5S9-1: RBM8A; NbExp=7; IntAct=EBI-299134, EBI-5773674;
CC P61326; O75478: TADA2A; NbExp=3; IntAct=EBI-299134, EBI-742268;
CC P61326; Q9BZI7: UPF3B; NbExp=7; IntAct=EBI-299134, EBI-372780;
CC P61326; Q9BZI7-2: UPF3B; NbExp=2; IntAct=EBI-299134, EBI-15674130;
CC P61326; Q15776: ZKSCAN8; NbExp=3; IntAct=EBI-299134, EBI-2602314;
CC P61326; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-299134, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19324961}. Nucleus
CC speckle {ECO:0000269|PubMed:19324961}. Cytoplasm
CC {ECO:0000269|PubMed:19324961}. Note=Detected in granule-like structures
CC in the dendroplasm (By similarity). Travels to the cytoplasm as part of
CC the exon junction complex (EJC) bound to mRNA. Colocalizes with the
CC core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear
CC speckles (PubMed:19324961). {ECO:0000250, ECO:0000250|UniProtKB:Q27W02,
CC ECO:0000269|PubMed:19324961}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61326-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61326-2; Sequence=VSP_056246;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the mago nashi family. {ECO:0000305}.
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DR EMBL; AF035940; AAC39606.1; -; mRNA.
DR EMBL; AF067173; AAD32457.1; -; mRNA.
DR EMBL; AK297895; BAG60216.1; -; mRNA.
DR EMBL; AK312113; BAG35049.1; -; mRNA.
DR EMBL; AL606760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06747.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06748.1; -; Genomic_DNA.
DR EMBL; BC018211; AAH18211.1; -; mRNA.
DR CCDS; CCDS577.1; -. [P61326-1]
DR RefSeq; NP_002361.1; NM_002370.3. [P61326-1]
DR PDB; 1P27; X-ray; 2.00 A; A/C=2-145.
DR PDB; 2HYI; X-ray; 2.30 A; A/G=1-146.
DR PDB; 2J0Q; X-ray; 3.20 A; C/F=1-146.
DR PDB; 2J0S; X-ray; 2.21 A; C=1-146.
DR PDB; 2XB2; X-ray; 3.40 A; C/Y=1-146.
DR PDB; 3EX7; X-ray; 2.30 A; A/E=1-146.
DR PDB; 7A5P; EM; 5.00 A; v=1-146.
DR PDBsum; 1P27; -.
DR PDBsum; 2HYI; -.
DR PDBsum; 2J0Q; -.
DR PDBsum; 2J0S; -.
DR PDBsum; 2XB2; -.
DR PDBsum; 3EX7; -.
DR PDBsum; 7A5P; -.
DR AlphaFoldDB; P61326; -.
DR SMR; P61326; -.
DR BioGRID; 110290; 225.
DR ComplexPortal; CPX-1941; Exon junction core complex, MAGOH variant.
DR ComplexPortal; CPX-1942; Exon junction subcomplex MAGOH-Y14.
DR CORUM; P61326; -.
DR DIP; DIP-33069N; -.
DR IntAct; P61326; 152.
DR MINT; P61326; -.
DR STRING; 9606.ENSP00000360525; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR GlyGen; P61326; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61326; -.
DR PhosphoSitePlus; P61326; -.
DR BioMuta; MAGOH; -.
DR DMDM; 47117708; -.
DR EPD; P61326; -.
DR jPOST; P61326; -.
DR MassIVE; P61326; -.
DR MaxQB; P61326; -.
DR PaxDb; P61326; -.
DR PeptideAtlas; P61326; -.
DR PRIDE; P61326; -.
DR ProteomicsDB; 3350; -.
DR ProteomicsDB; 57294; -. [P61326-1]
DR TopDownProteomics; P61326-1; -. [P61326-1]
DR Antibodypedia; 4217; 309 antibodies from 33 providers.
DR DNASU; 4116; -.
DR Ensembl; ENST00000371466.4; ENSP00000360521.4; ENSG00000162385.11. [P61326-2]
DR Ensembl; ENST00000371470.8; ENSP00000360525.3; ENSG00000162385.11. [P61326-1]
DR GeneID; 4116; -.
DR KEGG; hsa:4116; -.
DR MANE-Select; ENST00000371470.8; ENSP00000360525.3; NM_002370.4; NP_002361.1.
DR UCSC; uc001cvf.2; human. [P61326-1]
DR CTD; 4116; -.
DR DisGeNET; 4116; -.
DR GeneCards; MAGOH; -.
DR HGNC; HGNC:6815; MAGOH.
DR HPA; ENSG00000162385; Low tissue specificity.
DR MIM; 602603; gene.
DR neXtProt; NX_P61326; -.
DR OpenTargets; ENSG00000162385; -.
DR PharmGKB; PA30563; -.
DR VEuPathDB; HostDB:ENSG00000162385; -.
DR eggNOG; KOG3392; Eukaryota.
DR GeneTree; ENSGT00390000003156; -.
DR HOGENOM; CLU_109497_1_1_1; -.
DR InParanoid; P61326; -.
DR OMA; IRKEMWI; -.
DR OrthoDB; 1373136at2759; -.
DR PhylomeDB; P61326; -.
DR TreeFam; TF300128; -.
DR PathwayCommons; P61326; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P61326; -.
DR SIGNOR; P61326; -.
DR BioGRID-ORCS; 4116; 538 hits in 1070 CRISPR screens.
DR ChiTaRS; MAGOH; human.
DR EvolutionaryTrace; P61326; -.
DR GeneWiki; MAGOH; -.
DR GenomeRNAi; 4116; -.
DR Pharos; P61326; Tbio.
DR PRO; PR:P61326; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P61326; protein.
DR Bgee; ENSG00000162385; Expressed in oocyte and 202 other tissues.
DR Genevisible; P61326; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB.
DR GO; GO:1990501; C:exon-exon junction subcomplex mago-y14; IPI:ComplexPortal.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; IDA:ComplexPortal.
DR GO; GO:2000622; P:regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:ComplexPortal.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR CDD; cd11295; Mago_nashi; 1.
DR Gene3D; 3.30.1560.10; -; 1.
DR IDEAL; IID00375; -.
DR InterPro; IPR004023; Mago_nashi.
DR InterPro; IPR036605; Mago_nashi_sf.
DR PANTHER; PTHR12638; PTHR12638; 1.
DR Pfam; PF02792; Mago_nashi; 1.
DR SUPFAM; SSF89817; SSF89817; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW mRNA processing; mRNA splicing; mRNA transport;
KW Nonsense-mediated mRNA decay; Nucleus; Reference proteome; RNA-binding;
KW Spliceosome; Translation regulation; Transport.
FT CHAIN 1..146
FT /note="Protein mago nashi homolog"
FT /id="PRO_0000174145"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VAR_SEQ 50..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056246"
FT MUTAGEN 16..17
FT /note="KF->EA: Impaired nonsense-mediated decay activity."
FT /evidence="ECO:0000269|PubMed:16209946"
FT MUTAGEN 41..42
FT /note="KN->DA: Complete loss of nonsense-mediated decay
FT activity."
FT /evidence="ECO:0000269|PubMed:16209946"
FT MUTAGEN 66..68
FT /note="DSE->RSR: Slightly reduced nonsense-mediated decay
FT activity."
FT /evidence="ECO:0000269|PubMed:16209946"
FT MUTAGEN 68
FT /note="E->R: Abolishes interaction with PYM1 leading to
FT increase EJC association with spliced mRNAs; when
FT associated with R-72; K-73 and R-117."
FT /evidence="ECO:0000269|PubMed:19410547"
FT MUTAGEN 72..73
FT /note="ED->RK: Fully active."
FT /evidence="ECO:0000269|PubMed:16209946"
FT MUTAGEN 72
FT /note="E->R: Abolishes interaction with PYM1 leading to
FT increase EJC association with spliced mRNAs; when
FT associated with R-68; K-73 and R-117."
FT /evidence="ECO:0000269|PubMed:19410547"
FT MUTAGEN 73
FT /note="D->K: Abolishes interaction with PYM1 leading to
FT increase EJC association with spliced mRNAs; when
FT associated with R-68; R-72 and R-117."
FT /evidence="ECO:0000269|PubMed:19410547"
FT MUTAGEN 85..87
FT /note="RQE->EQR: Fully active."
FT /evidence="ECO:0000269|PubMed:16209946"
FT MUTAGEN 117
FT /note="E->R: Abolishes interaction with PYM1 leading to
FT increase EJC association with spliced mRNAs; when
FT associated with R-68; R-72 and K-73."
FT /evidence="ECO:0000269|PubMed:19410547"
FT MUTAGEN 130..134
FT /note="KCLVF->ECLVA: Complete loss of nonsense-mediated
FT decay activity."
FT /evidence="ECO:0000269|PubMed:16209946"
FT MUTAGEN 136
FT /note="L->R: Complete loss of nonsense-mediated decay
FT activity."
FT /evidence="ECO:0000269|PubMed:16209946"
FT STRAND 5..15
FT /evidence="ECO:0007829|PDB:1P27"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:1P27"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:1P27"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1P27"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:1P27"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:1P27"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1P27"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2XB2"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1P27"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1P27"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1P27"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2HYI"
FT HELIX 116..141
FT /evidence="ECO:0007829|PDB:1P27"
SQ SEQUENCE 146 AA; 17164 MW; FFAD0B075E045875 CRC64;
MESDFYLRYY VGHKGKFGHE FLEFEFRPDG KLRYANNSNY KNDVMIRKEA YVHKSVMEEL
KRIIDDSEIT KEDDALWPPP DRVGRQELEI VIGDEHISFT TSKIGSLIDV NQSKDPEGLR
VFYYLVQDLK CLVFSLIGLH FKIKPI
