RBM8A_HUMAN
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 03-AUG-2022, entry version 234.
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};
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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 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 AlphaFoldDB; Q9Y5S9; -.
DR SMR; Q9Y5S9; -.
DR BioGRID; 115265; 172.
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; 76.
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; Q9Y5S9; -.
DR PeptideAtlas; Q9Y5S9; -.
DR PRIDE; Q9Y5S9; -.
DR ProteomicsDB; 86494; -. [Q9Y5S9-1]
DR ProteomicsDB; 86495; -. [Q9Y5S9-2]
DR Antibodypedia; 74773; 142 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 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; TIAVDWC; -.
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; 652 hits in 1038 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 208 other tissues.
DR ExpressionAtlas; Q9Y5S9; baseline and differential.
DR Genevisible; Q9Y5S9; HS.
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; 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; 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; PTHR45894; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR01738; RNABINDINGM8.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
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
