MGN2_HUMAN
ID MGN2_HUMAN Reviewed; 148 AA.
AC Q96A72;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein mago nashi homolog 2;
GN Name=MAGOHB; Synonyms=MAGOH2;
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 [LARGE SCALE MRNA].
RC TISSUE=Hematopoietic stem cell;
RA Gu J., Huang Q., Yu Y., Xu S., Wang Y., Han Z., Chen Z., Zhou J., Tu Y.,
RA Gu W., Fu G., Huang C.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 2-10; 65-73 AND 106-116, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP FUNCTION, SUBUNIT, AND IDENTIFICATION IN THE EXON JUNCTION COMPLEX.
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 [9] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [10] {ECO:0007744|PDB:5YZG}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29301961; DOI=10.1126/science.aar6401;
RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.;
RT "Structure of a human catalytic step I spliceosome.";
RL Science 359:537-545(2018).
RN [11] {ECO:0007744|PDB:6QDV}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 5-145, FUNCTION,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=30705154; DOI=10.1126/science.aaw5569;
RA Fica S.M., Oubridge C., Wilkinson M.E., Newman A.J., Nagai K.;
RT "A human postcatalytic spliceosome structure reveals essential roles of
RT metazoan factors for exon ligation.";
RL Science 363:710-714(2019).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-119.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome (PubMed:28502770, PubMed:29301961, PubMed:30705154). Plays
CC a redundant role with MAGOH in the exon junction complex and in the
CC nonsense-mediated decay (NMD) pathway (PubMed:23917022).
CC {ECO:0000269|PubMed:23917022, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:30705154}.
CC -!- SUBUNIT: Component of the pre-catalytic, catalytic and post-catalytic
CC spliceosome complexes (PubMed:28502770, PubMed:29301961,
CC PubMed:30705154). Heterodimer with RBM8A. Core component of the mRNA
CC splicing-dependent exon junction complex (EJC); the core complex
CC contains CASC3, EIF4A3, MAGOH or MAGOHB, and RBM8A (PubMed:23917022).
CC {ECO:0000269|PubMed:23917022, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:30705154}.
CC -!- INTERACTION:
CC Q96A72; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-746778, EBI-10173507;
CC Q96A72; Q9Y2J4: AMOTL2; NbExp=4; IntAct=EBI-746778, EBI-746752;
CC Q96A72; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-746778, EBI-10181188;
CC Q96A72; Q13137: CALCOCO2; NbExp=6; IntAct=EBI-746778, EBI-739580;
CC Q96A72; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-746778, EBI-3866279;
CC Q96A72; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-746778, EBI-10171570;
CC Q96A72; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-746778, EBI-711501;
CC Q96A72; Q92997: DVL3; NbExp=3; IntAct=EBI-746778, EBI-739789;
CC Q96A72; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-746778, EBI-2349927;
CC Q96A72; Q5TD97: FHL5; NbExp=3; IntAct=EBI-746778, EBI-750641;
CC Q96A72; P51114-2: FXR1; NbExp=3; IntAct=EBI-746778, EBI-11022345;
CC Q96A72; Q8TDQ7-2: GNPDA2; NbExp=3; IntAct=EBI-746778, EBI-12197555;
CC Q96A72; Q08379: GOLGA2; NbExp=6; IntAct=EBI-746778, EBI-618309;
CC Q96A72; O95872: GPANK1; NbExp=3; IntAct=EBI-746778, EBI-751540;
CC Q96A72; Q9NP66: HMG20A; NbExp=4; IntAct=EBI-746778, EBI-740641;
CC Q96A72; O75031: HSF2BP; NbExp=3; IntAct=EBI-746778, EBI-7116203;
CC Q96A72; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-746778, EBI-8638439;
CC Q96A72; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-746778, EBI-11522367;
CC Q96A72; Q9UKT9: IKZF3; NbExp=7; IntAct=EBI-746778, EBI-747204;
CC Q96A72; Q0VD86: INCA1; NbExp=3; IntAct=EBI-746778, EBI-6509505;
CC Q96A72; Q6A162: KRT40; NbExp=3; IntAct=EBI-746778, EBI-10171697;
CC Q96A72; O95678: KRT75; NbExp=3; IntAct=EBI-746778, EBI-2949715;
CC Q96A72; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-746778, EBI-11959885;
CC Q96A72; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-746778, EBI-11953846;
CC Q96A72; Q8IYD9: LAS2; NbExp=3; IntAct=EBI-746778, EBI-749878;
CC Q96A72; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-746778, EBI-10172526;
CC Q96A72; P17568: NDUFB7; NbExp=3; IntAct=EBI-746778, EBI-1246238;
CC Q96A72; Q9BYG5: PARD6B; NbExp=3; IntAct=EBI-746778, EBI-295391;
CC Q96A72; P23759-2: PAX7; NbExp=3; IntAct=EBI-746778, EBI-12859446;
CC Q96A72; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-746778, EBI-10302990;
CC Q96A72; Q99959-2: PKP2; NbExp=3; IntAct=EBI-746778, EBI-10987518;
CC Q96A72; P41219: PRPH; NbExp=3; IntAct=EBI-746778, EBI-752074;
CC Q96A72; Q14558: PRPSAP1; NbExp=3; IntAct=EBI-746778, EBI-724449;
CC Q96A72; Q16825: PTPN21; NbExp=3; IntAct=EBI-746778, EBI-2860264;
CC Q96A72; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-746778, EBI-1210429;
CC Q96A72; Q9Y5S9: RBM8A; NbExp=12; IntAct=EBI-746778, EBI-447231;
CC Q96A72; P38159: RBMX; NbExp=3; IntAct=EBI-746778, EBI-743526;
CC Q96A72; Q04864: REL; NbExp=3; IntAct=EBI-746778, EBI-307352;
CC Q96A72; Q04864-2: REL; NbExp=3; IntAct=EBI-746778, EBI-10829018;
CC Q96A72; Q59EK9: RUNDC3A; NbExp=3; IntAct=EBI-746778, EBI-747225;
CC Q96A72; Q13573: SNW1; NbExp=3; IntAct=EBI-746778, EBI-632715;
CC Q96A72; Q9NWH7-2: SPATA6; NbExp=3; IntAct=EBI-746778, EBI-17860101;
CC Q96A72; A6NLX3: SPDYE4; NbExp=5; IntAct=EBI-746778, EBI-12047907;
CC Q96A72; O75558: STX11; NbExp=3; IntAct=EBI-746778, EBI-714135;
CC Q96A72; O75478: TADA2A; NbExp=3; IntAct=EBI-746778, EBI-742268;
CC Q96A72; P15884: TCF4; NbExp=3; IntAct=EBI-746778, EBI-533224;
CC Q96A72; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-746778, EBI-750109;
CC Q96A72; Q9BT49: THAP7; NbExp=3; IntAct=EBI-746778, EBI-741350;
CC Q96A72; Q08117: TLE5; NbExp=3; IntAct=EBI-746778, EBI-717810;
CC Q96A72; Q08117-2: TLE5; NbExp=3; IntAct=EBI-746778, EBI-11741437;
CC Q96A72; Q13595: TRA2A; NbExp=3; IntAct=EBI-746778, EBI-2685506;
CC Q96A72; P62995: TRA2B; NbExp=3; IntAct=EBI-746778, EBI-725485;
CC Q96A72; P14373: TRIM27; NbExp=3; IntAct=EBI-746778, EBI-719493;
CC Q96A72; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-746778, EBI-5235829;
CC Q96A72; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-746778, EBI-12017160;
CC Q96A72; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-746778, EBI-12287587;
CC Q96A72; Q9HCL3: ZFP14; NbExp=3; IntAct=EBI-746778, EBI-6381556;
CC Q96A72; Q9HBF4: ZFYVE1; NbExp=3; IntAct=EBI-746778, EBI-4401611;
CC Q96A72; P17023: ZNF19; NbExp=3; IntAct=EBI-746778, EBI-12884200;
CC Q96A72; P15622-3: ZNF250; NbExp=3; IntAct=EBI-746778, EBI-10177272;
CC Q96A72; Q8TD17: ZNF398; NbExp=6; IntAct=EBI-746778, EBI-8643207;
CC Q96A72; Q9BUY5: ZNF426; NbExp=4; IntAct=EBI-746778, EBI-743265;
CC Q96A72; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-746778, EBI-11962468;
CC Q96A72; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-746778, EBI-740232;
CC Q96A72; Q6P9G9: ZNF449; NbExp=3; IntAct=EBI-746778, EBI-10215956;
CC Q96A72; Q8IVP9: ZNF547; NbExp=3; IntAct=EBI-746778, EBI-12895421;
CC Q96A72; Q969W8: ZNF566; NbExp=3; IntAct=EBI-746778, EBI-2555762;
CC Q96A72; Q68EA5: ZNF57; NbExp=3; IntAct=EBI-746778, EBI-8490788;
CC Q96A72; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-746778, EBI-4395669;
CC Q96A72; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-746778, EBI-10251462;
CC Q96A72; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-746778, EBI-5667516;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:30705154}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the mago nashi family. {ECO:0000305}.
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DR EMBL; AF165518; AAF86648.1; -; mRNA.
DR EMBL; AK001154; BAA91522.1; -; mRNA.
DR EMBL; AK022720; BAB14202.1; -; mRNA.
DR EMBL; BC010905; AAH10905.1; -; mRNA.
DR CCDS; CCDS8628.1; -.
DR RefSeq; NP_001306914.1; NM_001319985.1.
DR RefSeq; NP_060518.1; NM_018048.4.
DR PDB; 5XJC; EM; 3.60 A; v=1-148.
DR PDB; 5YZG; EM; 4.10 A; v=1-148.
DR PDB; 6ICZ; EM; 3.00 A; v=1-148.
DR PDB; 6QDV; EM; 3.30 A; 9=5-145.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6QDV; -.
DR AlphaFoldDB; Q96A72; -.
DR SMR; Q96A72; -.
DR BioGRID; 120420; 115.
DR ComplexPortal; CPX-680; Exon junction subcomplex MAGOHB-Y14.
DR ComplexPortal; CPX-682; Exon junction core complex, MAGOHB variant.
DR IntAct; Q96A72; 84.
DR MINT; Q96A72; -.
DR STRING; 9606.ENSP00000319240; -.
DR iPTMnet; Q96A72; -.
DR PhosphoSitePlus; Q96A72; -.
DR SwissPalm; Q96A72; -.
DR BioMuta; MAGOHB; -.
DR DMDM; 74731095; -.
DR EPD; Q96A72; -.
DR jPOST; Q96A72; -.
DR MassIVE; Q96A72; -.
DR MaxQB; Q96A72; -.
DR PaxDb; Q96A72; -.
DR PeptideAtlas; Q96A72; -.
DR PRIDE; Q96A72; -.
DR ProteomicsDB; 75929; -.
DR TopDownProteomics; Q96A72; -.
DR Antibodypedia; 23361; 68 antibodies from 14 providers.
DR DNASU; 55110; -.
DR Ensembl; ENST00000320756.7; ENSP00000319240.2; ENSG00000111196.10.
DR GeneID; 55110; -.
DR KEGG; hsa:55110; -.
DR MANE-Select; ENST00000320756.7; ENSP00000319240.2; NM_018048.5; NP_060518.1.
DR UCSC; uc001qyq.3; human.
DR CTD; 55110; -.
DR DisGeNET; 55110; -.
DR GeneCards; MAGOHB; -.
DR HGNC; HGNC:25504; MAGOHB.
DR HPA; ENSG00000111196; Low tissue specificity.
DR MIM; 619552; gene.
DR neXtProt; NX_Q96A72; -.
DR OpenTargets; ENSG00000111196; -.
DR PharmGKB; PA162394899; -.
DR VEuPathDB; HostDB:ENSG00000111196; -.
DR eggNOG; KOG3392; Eukaryota.
DR GeneTree; ENSGT00390000003156; -.
DR HOGENOM; CLU_109497_1_1_1; -.
DR InParanoid; Q96A72; -.
DR OMA; VSECEIM; -.
DR OrthoDB; 1373136at2759; -.
DR PhylomeDB; Q96A72; -.
DR TreeFam; TF300128; -.
DR PathwayCommons; Q96A72; -.
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; Q96A72; -.
DR BioGRID-ORCS; 55110; 45 hits in 1077 CRISPR screens.
DR ChiTaRS; MAGOHB; human.
DR GenomeRNAi; 55110; -.
DR Pharos; Q96A72; Tbio.
DR PRO; PR:Q96A72; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96A72; protein.
DR Bgee; ENSG00000111196; Expressed in calcaneal tendon and 132 other tissues.
DR ExpressionAtlas; Q96A72; baseline and differential.
DR Genevisible; Q96A72; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0035145; C:exon-exon junction complex; IDA:HGNC.
DR GO; GO:1990501; C:exon-exon junction subcomplex mago-y14; IPI:ComplexPortal.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; 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; IDA:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IGI:HGNC.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR CDD; cd11295; Mago_nashi; 1.
DR Gene3D; 3.30.1560.10; -; 1.
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; Direct protein sequencing; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Reference proteome; RNA-binding;
KW Spliceosome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..148
FT /note="Protein mago nashi homolog 2"
FT /id="PRO_0000174146"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VARIANT 119
FT /note="E -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036431"
FT STRAND 7..17
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 118..143
FT /evidence="ECO:0007829|PDB:6ICZ"
SQ SEQUENCE 148 AA; 17276 MW; 0C7D8F79ACC09E39 CRC64;
MAVASDFYLR YYVGHKGKFG HEFLEFEFRP DGKLRYANNS NYKNDVMIRK EAYVHKSVME
ELKRIIDDSE ITKEDDALWP PPDRVGRQEL EIVIGDEHIS FTTSKIGSLI DVNQSKDPEG
LRVFYYLVQD LKCLVFSLIG LHFKIKPI
