ID RBM8A_HUMAN Reviewed; 174 AA. AC Q9Y5S9; B3KQI9; Q6FHD1; Q6IQ40; Q9GZX8; Q9NZI4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 243. DE RecName: Full=RNA-binding protein 8A; DE AltName: Full=Binder of OVCA1-1; DE Short=BOV-1; DE AltName: Full=RNA-binding motif protein 8A; DE AltName: Full=RNA-binding protein Y14 {ECO:0000303|PubMed:11030346}; DE AltName: Full=Ribonucleoprotein RBM8A; GN Name=RBM8A; Synonyms=RBM8; ORFNames=HSPC114, MDS014; 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). RC TISSUE=Skeletal muscle; RX PubMed=11004516; DOI=10.1016/s0167-4781(00)00090-7; RA Conklin D.C., Rixon M.W., Kuestner R.E., Maurer M.F., Whitmore T.E., RA Millar R.P.; RT "Cloning and gene expression of a novel human ribonucleoprotein."; RL Biochim. Biophys. Acta 1492:465-469(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH MAGOH. 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH DPH1. RC TISSUE=Brain; RX PubMed=11013075; DOI=10.1006/geno.2000.6315; RA Salicioni A.M., Xi M., Vanderveer L.A., Balsara B., Testa J.R., RA Dunbrack R.L. Jr., Godwin A.K.; RT "Identification and structural analysis of human RBM8A and RBM8B: two RT highly conserved RNA-binding motif proteins that interact with OVCA1, a RT candidate tumor suppressor."; RL Genomics 69:54-62(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, AND SUBCELLULAR RP LOCATION. RX PubMed=11030346; DOI=10.1016/s1097-2765(00)00065-4; RA Kataoka N., Yong J., Kim V.N., Velazquez F., Perkinson R.A., Wang F., RA Dreyfuss G.; RT "Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding RT protein that persists in the cytoplasm."; RL Mol. Cell 6:673-682(2000). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11707068; DOI=10.1006/geno.2001.6650; RA Faurholm B., Millar R.P., Katz A.A.; RT "The genes encoding the type II gonadotropin-releasing hormone receptor and RT the ribonucleoprotein RBM8A in humans overlap in two genomic loci."; RL Genomics 78:15-18(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hematopoietic stem cell; RA Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.; RT "Novel genes expressed in hematopoietic stem/progenitor cells from RT myelodysplastic syndrome patients."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [10] 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 [11] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon; 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 [13] RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) RP WITH DEK; RNPS1; SRRM1 AND ALYREF/THOC4. RX PubMed=11118221; DOI=10.1093/emboj/19.24.6860; RA Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.; RT "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of RT mRNA exon-exon junctions."; RL EMBO J. 19:6860-6869(2000). RN [14] RP INTERACTION WITH IPO13. RX PubMed=11447110; DOI=10.1093/emboj/20.14.3685; RA Mingot J.-M., Kostka S., Kraft R., Hartmann E., Goerlich D.; RT "Importin 13: a novel mediator of nuclear import and export."; RL EMBO J. 20:3685-3694(2001). RN [15] RP INTERACTION WITH ALYREF/THOC4 AND THE EXON JUNCTION COMPLEX. RX PubMed=11707413; DOI=10.1093/emboj/20.22.6424; RA Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G.; RT "Magoh, a human homolog of Drosophila mago nashi protein, is a component of RT the splicing-dependent exon-exon junction complex."; RL EMBO J. 20:6424-6433(2001). RN [16] RP IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B. RX PubMed=11546873; DOI=10.1126/science.1062829; RA Kim V.N., Kataoka N., Dreyfuss G.; RT "Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent RT exon-exon junction complex."; RL Science 293:1832-1836(2001). RN [17] RP IDENTIFICATION IN A POST-SPLICING COMPLEX WITH NXF1; UPF1; UPF2; UPF3A; RP UPF3B AND RNPS1. RX PubMed=11546874; DOI=10.1126/science.1062786; RA Lykke-Andersen J., Shu M.-D., Steitz J.A.; RT "Communication of the position of exon-exon junctions to the mRNA RT surveillance machinery by the protein RNPS1."; RL Science 293:1836-1839(2001). RN [18] RP FUNCTION IN TRANSLATION, ASSOCIATION WITH POLYSOMES, AND RNA-BINDING. RX PubMed=12121612; DOI=10.1016/s0960-9822(02)00902-8; RA Dostie J., Dreyfuss G.; RT "Translation is required to remove Y14 from mRNAs in the cytoplasm."; RL Curr. Biol. 12:1060-1067(2002). RN [19] 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 [20] RP INTERACTION WITH DDX39B; RNPS1; SRRM1 AND ALYREF/THOC4. RX PubMed=12944400; DOI=10.1074/jbc.m306856200; RA McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.; RT "An evolutionarily conserved role for SRm160 in 3'-end processing that RT functions independently of exon junction complex formation."; RL J. Biol. Chem. 278:44153-44160(2003). RN [21] RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, AND INTERACTION WITH UPF3B. RX PubMed=12718880; DOI=10.1016/s1097-2765(03)00142-4; RA Gehring N.H., Neu-Yilik G., Schell T., Hentze M.W., Kulozik A.E.; RT "Y14 and hUpf3b form an NMD-activating complex."; RL Mol. Cell 11:939-949(2003). RN [22] RP FUNCTION, AND INTERACTION WITH MAGOH. 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 [23] 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 [24] RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) RP WITH RNPS1 AND SRRM1. RX PubMed=14625303; DOI=10.1074/jbc.m307692200; RA Kataoka N., Dreyfuss G.; RT "A simple whole cell lysate system for in vitro splicing reveals a stepwise RT assembly of the exon-exon junction complex."; RL J. Biol. Chem. 279:7009-7013(2004). RN [25] RP FUNCTION, AND MUTAGENESIS OF 82-GLU-GLU-83; 106-LEU--ARG-108; LEU-118 AND RP 149-CYS-PHE-150. 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 [26] 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 [27] 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 [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [29] 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 [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-56, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [31] 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 [32] RP FUNCTION IN MRNA TRANSLATION. RX PubMed=19409878; DOI=10.1016/j.bbrc.2009.04.123; RA Lee H.C., Choe J., Chi S.G., Kim Y.K.; RT "Exon junction complex enhances translation of spliced mRNAs at multiple RT steps."; RL Biochem. Biophys. Res. Commun. 384:334-340(2009). RN [33] RP INTERACTION WITH PYM1. 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 [34] 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 [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [36] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-24 AND SER-42, CLEAVAGE OF INITIATOR METHIONINE [LARGE RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [37] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [38] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-24; SER-42 AND SER-56, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [39] 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 [40] RP INVOLVEMENT IN TAR. RX PubMed=22366785; DOI=10.1038/ng.1083; RA Albers C.A., Paul D.S., Schulze H., Freson K., Stephens J.C., RA Smethurst P.A., Jolley J.D., Cvejic A., Kostadima M., Bertone P., RA Breuning M.H., Debili N., Deloukas P., Favier R., Fiedler J., Hobbs C.M., RA Huang N., Hurles M.E., Kiddle G., Krapels I., Nurden P., Ruivenkamp C.A., RA Sambrook J.G., Smith K., Stemple D.L., Strauss G., Thys C., van Geet C., RA Newbury-Ecob R., Ouwehand W.H., Ghevaert C.; RT "Compound inheritance of a low-frequency regulatory SNP and a rare null RT mutation in exon-junction complex subunit RBM8A causes TAR syndrome."; RL Nat. Genet. 44:435-439(2012). RN [41] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-42 AND SER-56, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [42] RP INTERACTION WITH MAGOHB AND MAGOH, AND IDENTIFICATION IN THE EXON JUNCTION RP 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 [43] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [44] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [45] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 50-155 IN COMPLEX WITH MAGOH. 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 [47] RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 66-154 IN THE EJC COMPLEX WITH RP CASC3; EIF4A3; MAGOH 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 [48] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 64-154 IN THE EJC COMPLEX WITH RP CASC3; EIF4A3; MAGOH 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 [49] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 51-174 IN THE EJC COMPLEX WITH RP CASC3; EIF4A3; MAGOH 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 [50] {ECO:0007744|PDB:2XB2} RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 66-155 IN THE EJC COMPLEX WITH RP CASC3; EIF4A3; MAGOH; UPF3B; UPF2 AND RNA. 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). RN [51] {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 [52] {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). CC -!- FUNCTION: Required for pre-mRNA splicing as component of the CC spliceosome (PubMed:28502770, PubMed:29301961). Core component of the CC splicing-dependent multiprotein exon junction complex (EJC) deposited CC at splice junctions on mRNAs. The EJC is a dynamic structure consisting CC of core proteins and several peripheral nuclear and cytoplasmic CC associated factors that join the complex only transiently either during CC EJC assembly or during subsequent mRNA metabolism. The EJC marks the CC position of the exon-exon junction in the mature mRNA for the gene CC expression machinery and the core components remain bound to spliced CC mRNAs throughout all stages of mRNA metabolism thereby influencing CC downstream processes including nuclear mRNA export, subcellular mRNA CC localization, translation efficiency and nonsense-mediated mRNA decay CC (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of CC EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a CC stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC CC key regulator PYM1 leading to EJC disassembly in the cytoplasm and CC translation enhancement of EJC-bearing spliced mRNAs by recruiting them CC to the ribosomal 48S preinitiation complex. Its removal from CC cytoplasmic mRNAs requires translation initiation from EJC-bearing CC spliced mRNAs. Associates preferentially with mRNAs produced by CC splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced CC from intronless cDNAs. Associates with both nuclear mRNAs and newly CC exported cytoplasmic mRNAs. The MAGOH-RBM8A heterodimer is a component CC of the nonsense mediated decay (NMD) pathway. Involved in the splicing CC modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); CC specifically inhibits formation of proapoptotic isoforms such as Bcl- CC X(S); the function is different from the established EJC assembly. CC {ECO:0000269|PubMed:12121612, ECO:0000269|PubMed:12718880, CC ECO:0000269|PubMed:12730685, ECO:0000269|PubMed:16209946, CC ECO:0000269|PubMed:19409878, ECO:0000269|PubMed:22203037, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. CC -!- SUBUNIT: Heterodimer with either MAGOH or MAGOHB (PubMed:10662555, CC PubMed:12730685, PubMed:23917022, PubMed:12781131). Part of the mRNA CC splicing-dependent exon junction complex (EJC) complex; the core CC complex contains CASC3, EIF4A3, MAGOH or MAGOHB, and RBM8A CC (PubMed:11707413, PubMed:16170325, PubMed:16314458, PubMed:23917022, CC PubMed:16923391, PubMed:16931718, PubMed:19033377, PubMed:20479275). CC Interacts with PYM1; the interaction is direct and dissociates the EJC CC from spliced mRNAs (PubMed:14968132, PubMed:18026120, PubMed:19410547). CC Part of a complex that contains the EJC core components CASC3, EIF4A3, CC MAGOH and RBM8A plus proteins involved in nonsense-mediated mRNA decay, CC such as UPF1, UPF2, UPF3A and UPF3B (PubMed:11546873, PubMed:12718880, CC PubMed:20479275). Found in a post-splicing complex with NXF1, MAGOH, CC UPF1, UPF2, UPF3A, UPF3B and RNPS1 (PubMed:11546874). Interacts with CC DDX39B, MAGOH, DPH1, UPF3B, RNPS1, SRRM1 and ALYREF/THOC4 CC (PubMed:11013075, PubMed:11118221, PubMed:11707413, PubMed:12944400). CC Interacts with IPO13; the interaction mediates the nuclear import of CC the MAGOH-RBM8A heterodimer (PubMed:11447110). Identified in the CC spliceosome C complex (PubMed:11991638, PubMed:28502770, CC PubMed:29301961). Associates with polysomes (PubMed:12121612). CC {ECO:0000269|PubMed:10662555, ECO:0000269|PubMed:11013075, CC ECO:0000269|PubMed:11118221, ECO:0000269|PubMed:11447110, CC ECO:0000269|PubMed:11546873, ECO:0000269|PubMed:11546874, CC ECO:0000269|PubMed:11707413, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:12121612, ECO:0000269|PubMed:12718880, CC ECO:0000269|PubMed:12730685, ECO:0000269|PubMed:12781131, CC ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:14625303, CC ECO:0000269|PubMed:14968132, ECO:0000269|PubMed:16170325, CC ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:16923391, CC ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:18026120, CC ECO:0000269|PubMed:19033377, ECO:0000269|PubMed:19410547, CC ECO:0000269|PubMed:20479275, ECO:0000269|PubMed:23917022, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. CC -!- INTERACTION: CC Q9Y5S9; P38919: EIF4A3; NbExp=21; IntAct=EBI-447231, EBI-299104; CC Q9Y5S9; P61326: MAGOH; NbExp=40; IntAct=EBI-447231, EBI-299134; CC Q9Y5S9; Q96A72: MAGOHB; NbExp=12; IntAct=EBI-447231, EBI-746778; CC Q9Y5S9; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-447231, EBI-539478; CC Q9Y5S9; P78362: SRPK2; NbExp=2; IntAct=EBI-447231, EBI-593303; CC Q9Y5S9; Q99081-3: TCF12; NbExp=3; IntAct=EBI-447231, EBI-11952764; CC Q9Y5S9; Q9H1J1: UPF3A; NbExp=4; IntAct=EBI-447231, EBI-521530; CC Q9Y5S9; Q9BZI7: UPF3B; NbExp=9; IntAct=EBI-447231, EBI-372780; CC Q9Y5S9-1; P61326: MAGOH; NbExp=7; IntAct=EBI-5773674, EBI-299134; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11030346, CC ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:29301961}. Nucleus speckle CC {ECO:0000269|PubMed:11030346, ECO:0000269|PubMed:19324961}. Cytoplasm CC {ECO:0000269|PubMed:11030346, ECO:0000269|PubMed:19324961}. CC Note=Nucleocytoplasmic shuttling protein (PubMed:11030346). Travels to CC the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. CC Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the CC nucleus and nuclear speckles (PubMed:19324961). CC {ECO:0000269|PubMed:11030346, ECO:0000269|PubMed:19324961}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=BOV-1a; CC IsoId=Q9Y5S9-1; Sequence=Displayed; CC Name=2; Synonyms=BOV-1b; CC IsoId=Q9Y5S9-2; Sequence=VSP_005810; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DISEASE: Thrombocytopenia-absent radius syndrome (TAR) [MIM:274000]: An CC autosomal recessive disorder characterized by bilateral absence of the CC radii with the presence of both thumbs, thrombocytopenia, low numbers CC of megakaryocytes, and bleeding episodes in the first year of life. CC Thrombocytopenic episodes decrease with age. Skeletal anomalies range CC from absence of radii to virtual absence of upper limbs, with or CC without lower limb defects such as malformations of the hip and knee. CC {ECO:0000269|PubMed:22366785}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the RBM8A family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG14951.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAG16782.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAG16782.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. A chimeric cDNA originating from chromosomes 1 and 5.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF127761; AAD21089.1; -; mRNA. DR EMBL; AF198620; AAF37551.1; -; mRNA. DR EMBL; AF231511; AAG16781.1; -; mRNA. DR EMBL; AF231512; AAG16782.1; ALT_INIT; mRNA. DR EMBL; AF299118; AAG27091.1; -; mRNA. DR EMBL; AF403012; AAL26999.1; -; Genomic_DNA. DR EMBL; AF182415; AAG14951.1; ALT_INIT; mRNA. DR EMBL; AF161463; AAF29078.1; -; mRNA. DR EMBL; CR541823; CAG46622.1; -; mRNA. DR EMBL; CR541805; CAG46604.1; -; mRNA. DR EMBL; AK075009; BAG52051.1; -; mRNA. DR EMBL; AL160282; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471244; EAW71419.1; -; Genomic_DNA. DR EMBL; BC017088; AAH17088.1; -; mRNA. DR CCDS; CCDS72872.1; -. [Q9Y5S9-1] DR RefSeq; NP_005096.1; NM_005105.4. [Q9Y5S9-1] DR PDB; 1P27; X-ray; 2.00 A; B/D=50-155. DR PDB; 2HYI; X-ray; 2.30 A; B/H=64-154. DR PDB; 2J0Q; X-ray; 3.20 A; D/G=66-174. DR PDB; 2J0S; X-ray; 2.21 A; D=66-154. DR PDB; 2XB2; X-ray; 3.40 A; D/Z=66-155. DR PDB; 3EX7; X-ray; 2.30 A; B/G=51-174. DR PDB; 5XJC; EM; 3.60 A; w=1-174. DR PDB; 5YZG; EM; 4.10 A; w=1-174. DR PDB; 6ICZ; EM; 3.00 A; w=1-174. DR PDB; 6QDV; EM; 3.30 A; 8=64-150. DR PDB; 7A5P; EM; 5.00 A; w=1-174. DR PDB; 7W59; EM; 3.60 A; w=1-174. DR PDB; 7W5A; EM; 3.60 A; w=1-174. DR PDB; 7W5B; EM; 4.30 A; w=1-174. DR PDB; 7ZNJ; EM; 2.40 A; C/H/M/c/h/m=65-155. DR PDB; 8C6J; EM; 2.80 A; 8=1-174. DR PDBsum; 1P27; -. DR PDBsum; 2HYI; -. DR PDBsum; 2J0Q; -. DR PDBsum; 2J0S; -. DR PDBsum; 2XB2; -. DR PDBsum; 3EX7; -. DR PDBsum; 5XJC; -. DR PDBsum; 5YZG; -. DR PDBsum; 6ICZ; -. DR PDBsum; 6QDV; -. DR PDBsum; 7A5P; -. DR PDBsum; 7W59; -. DR PDBsum; 7W5A; -. DR PDBsum; 7W5B; -. DR PDBsum; 7ZNJ; -. DR PDBsum; 8C6J; -. DR AlphaFoldDB; Q9Y5S9; -. DR EMDB; EMD-14803; -. DR EMDB; EMD-16452; -. DR EMDB; EMD-32317; -. DR EMDB; EMD-32319; -. DR EMDB; EMD-32321; -. DR EMDB; EMD-4525; -. DR EMDB; EMD-6721; -. DR EMDB; EMD-6864; -. DR EMDB; EMD-9645; -. DR SMR; Q9Y5S9; -. DR BioGRID; 115265; 439. DR ComplexPortal; CPX-1941; Exon junction core complex, MAGOH variant. DR ComplexPortal; CPX-1942; Exon junction subcomplex MAGOH-Y14. DR ComplexPortal; CPX-680; Exon junction subcomplex MAGOHB-Y14. DR ComplexPortal; CPX-682; Exon junction core complex, MAGOHB variant. DR CORUM; Q9Y5S9; -. DR DIP; DIP-33070N; -. DR IntAct; Q9Y5S9; 84. DR MINT; Q9Y5S9; -. DR STRING; 9606.ENSP00000463058; -. DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family. DR GlyGen; Q9Y5S9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y5S9; -. DR MetOSite; Q9Y5S9; -. DR PhosphoSitePlus; Q9Y5S9; -. DR SwissPalm; Q9Y5S9; -. DR BioMuta; RBM8A; -. DR DMDM; 10720244; -. DR EPD; Q9Y5S9; -. DR jPOST; Q9Y5S9; -. DR MassIVE; Q9Y5S9; -. DR MaxQB; Q9Y5S9; -. DR PaxDb; 9606-ENSP00000463058; -. DR PeptideAtlas; Q9Y5S9; -. DR ProteomicsDB; 86494; -. [Q9Y5S9-1] DR ProteomicsDB; 86495; -. [Q9Y5S9-2] DR Pumba; Q9Y5S9; -. DR Antibodypedia; 74773; 175 antibodies from 29 providers. DR DNASU; 9939; -. DR Ensembl; ENST00000369307.4; ENSP00000358313.3; ENSG00000265241.8. [Q9Y5S9-2] DR Ensembl; ENST00000583313.7; ENSP00000463058.2; ENSG00000265241.8. [Q9Y5S9-1] DR Ensembl; ENST00000632555.1; ENSP00000488265.1; ENSG00000265241.8. [Q9Y5S9-1] DR Ensembl; ENST00000691760.1; ENSP00000510519.1; ENSG00000265241.8. [Q9Y5S9-1] DR GeneID; 9939; -. DR KEGG; hsa:9939; -. DR MANE-Select; ENST00000583313.7; ENSP00000463058.2; NM_005105.5; NP_005096.1. DR UCSC; uc031uto.2; human. [Q9Y5S9-1] DR AGR; HGNC:9905; -. DR CTD; 9939; -. DR DisGeNET; 9939; -. DR GeneCards; RBM8A; -. DR GeneReviews; RBM8A; -. DR HGNC; HGNC:9905; RBM8A. DR HPA; ENSG00000265241; Low tissue specificity. DR MalaCards; RBM8A; -. DR MIM; 274000; phenotype. DR MIM; 605313; gene. DR neXtProt; NX_Q9Y5S9; -. DR OpenTargets; ENSG00000265241; -. DR Orphanet; 3320; Thrombocytopenia-absent radius syndrome. DR PharmGKB; PA34270; -. DR VEuPathDB; HostDB:ENSG00000265241; -. DR eggNOG; KOG0130; Eukaryota. DR GeneTree; ENSGT00730000111185; -. DR InParanoid; Q9Y5S9; -. DR OMA; CEFGDIK; -. DR OrthoDB; 36315at2759; -. DR PhylomeDB; Q9Y5S9; -. DR TreeFam; TF314933; -. DR PathwayCommons; Q9Y5S9; -. 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; Q9Y5S9; -. DR SIGNOR; Q9Y5S9; -. DR BioGRID-ORCS; 9939; 680 hits in 1116 CRISPR screens. DR ChiTaRS; RBM8A; human. DR EvolutionaryTrace; Q9Y5S9; -. DR GeneWiki; RBM8A; -. DR GenomeRNAi; 9939; -. DR Pharos; Q9Y5S9; Tbio. DR PRO; PR:Q9Y5S9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y5S9; Protein. DR Bgee; ENSG00000265241; Expressed in ganglionic eminence and 210 other cell types or tissues. DR ExpressionAtlas; Q9Y5S9; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. 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:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. 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:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006406; P:mRNA export from nucleus; NAS: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; 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; cd12324; RRM_RBM8; 1. DR DisProt; DP02868; -. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR008111; RNA-bd_8. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR033744; RRM_RBM8. DR PANTHER; PTHR45894; RNA-BINDING PROTEIN 8A; 1. DR PANTHER; PTHR45894:SF1; RNA-BINDING PROTEIN 8A; 1. DR Pfam; PF00076; RRM_1; 1. DR PRINTS; PR01738; RNABINDINGM8. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. DR Genevisible; Q9Y5S9; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Isopeptide bond; mRNA processing; mRNA splicing; mRNA transport; KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome; KW RNA-binding; Spliceosome; Translation regulation; Transport; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT CHAIN 2..174 FT /note="RNA-binding protein 8A" FT /id="PRO_0000081763" FT DOMAIN 73..151 FT /note="RRM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 1..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 151..174 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..29 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..65 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 156..174 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 42 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 56 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 27 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 44 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10662555, FT ECO:0000303|PubMed:11013075" FT /id="VSP_005810" FT MUTAGEN 82..83 FT /note="EE->RR: Impaired nonsense-mediated decay activity." FT /evidence="ECO:0000269|PubMed:16209946" FT MUTAGEN 106..108 FT /note="LDR->RDE: Complete loss of nonsense-mediated decay FT activity." FT /evidence="ECO:0000269|PubMed:16209946" FT MUTAGEN 118 FT /note="L->R: Complete loss of nonsense-mediated decay FT activity." FT /evidence="ECO:0000269|PubMed:16209946" FT MUTAGEN 149..150 FT /note="CF->KA: Complete loss of nonsense-mediated decay FT activity." FT /evidence="ECO:0000269|PubMed:16209946" FT CONFLICT 130 FT /note="A -> V (in Ref. 8; CAG46622)" FT /evidence="ECO:0000305" FT STRAND 72..78 FT /evidence="ECO:0007829|PDB:1P27" FT HELIX 86..93 FT /evidence="ECO:0007829|PDB:1P27" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1P27" FT STRAND 99..106 FT /evidence="ECO:0007829|PDB:1P27" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:1P27" FT STRAND 111..122 FT /evidence="ECO:0007829|PDB:1P27" FT HELIX 124..134 FT /evidence="ECO:0007829|PDB:1P27" FT STRAND 138..143 FT /evidence="ECO:0007829|PDB:1P27" FT STRAND 145..153 FT /evidence="ECO:0007829|PDB:1P27" SQ SEQUENCE 174 AA; 19889 MW; 70BBD03CDDFEECFE CRC64; MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEEGSRARM REDYDSVEQD GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK NIHLNLDRRT GYLKGYTLVE YETYKEAQAA MEGLNGQDLM GQPISVDWCF VRGPPKGKRR GGRRRSRSPD RRRR //