RBM8A_MOUSE
ID RBM8A_MOUSE Reviewed; 174 AA.
AC Q9CWZ3; A0A023T672; Q3UT38; Q6GTD4; Q9D6U5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=RNA-binding protein 8A;
DE AltName: Full=RNA-binding motif protein 8A;
DE AltName: Full=Ribonucleoprotein RBM8A;
GN Name=Rbm8a; Synonyms=Rbm8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=24416299; DOI=10.1371/journal.pone.0084842;
RA Gong P., Zhao M., He C.;
RT "Slow co-evolution of the MAGO and Y14 protein families is required for the
RT maintenance of their obligate heterodimerization mode.";
RL PLoS ONE 9:E84842-E84842(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Egg, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome (By similarity). Core component of the splicing-dependent
CC multiprotein exon junction complex (EJC) deposited at splice junctions
CC on mRNAs. The EJC is a dynamic structure consisting of core proteins
CC and several peripheral nuclear and cytoplasmic associated factors that
CC join the complex only transiently either during EJC assembly or during
CC subsequent mRNA metabolism. The EJC marks the position of the exon-exon
CC junction in the mature mRNA for the gene expression machinery and the
CC core components remain bound to spliced mRNAs throughout all stages of
CC mRNA metabolism thereby influencing downstream processes including
CC nuclear mRNA export, subcellular mRNA localization, translation
CC efficiency and nonsense-mediated mRNA decay (NMD). 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y5S9}.
CC -!- SUBUNIT: Heterodimer with either MAGOH or MAGOHB. Part of the mRNA
CC splicing-dependent exon junction complex (EJC) complex; the core
CC complex contains CASC3, EIF4A3, MAGOH or MAGOHB, and RBM8A. Interacts
CC with PYM1; the interaction is direct and dissociates the EJC from
CC spliced mRNAs. Part of a complex that contains the EJC core components
CC CASC3, EIF4A3, MAGOH and RBM8A plus proteins involved in nonsense-
CC mediated mRNA decay, such as UPF1, UPF2, UPF3A and UPF3B. Found in a
CC post-splicing complex with NXF1, MAGOH, UPF1, UPF2, UPF3A, UPF3B and
CC RNPS1. Interacts with DDX39B, MAGOH, DPH1, UPF3B, RNPS1, SRRM1 and
CC ALYREF/THOC4. Interacts with IPO13; the interaction mediates the
CC nuclear import of the MAGOH-RBM8A heterodimer. Identified in the
CC spliceosome C complex. Associates with polysomes.
CC {ECO:0000250|UniProtKB:Q9Y5S9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y5S9}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q9Y5S9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y5S9}. Note=Nucleocytoplasmic shuttling
CC protein. Travels to the cytoplasm as part of the exon junction complex
CC (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1
CC and UAP56 in the nucleus and nuclear speckles.
CC {ECO:0000250|UniProtKB:Q9Y5S9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CWZ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CWZ3-2; Sequence=VSP_010251;
CC -!- SIMILARITY: Belongs to the RBM8A family. {ECO:0000305}.
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DR EMBL; KF051021; AHX83807.1; -; mRNA.
DR EMBL; AK009953; BAB26605.1; -; mRNA.
DR EMBL; AK010284; BAB26820.1; -; mRNA.
DR EMBL; AK082925; BAC38693.1; -; mRNA.
DR EMBL; AK139805; BAE24142.1; -; mRNA.
DR EMBL; AC122037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466620; EDL38900.1; -; Genomic_DNA.
DR EMBL; BC020086; AAH20086.1; -; mRNA.
DR EMBL; BC058376; AAH58376.1; -; mRNA.
DR EMBL; BC132651; AAI32652.1; -; mRNA.
DR EMBL; BC132653; AAI32654.1; -; mRNA.
DR CCDS; CCDS51005.1; -. [Q9CWZ3-1]
DR CCDS; CCDS79983.1; -. [Q9CWZ3-2]
DR RefSeq; NP_001095877.1; NM_001102407.1. [Q9CWZ3-1]
DR RefSeq; NP_080151.2; NM_025875.2. [Q9CWZ3-2]
DR AlphaFoldDB; Q9CWZ3; -.
DR SMR; Q9CWZ3; -.
DR BioGRID; 208557; 83.
DR ComplexPortal; CPX-635; Exon junction core complex, Magoh variant.
DR ComplexPortal; CPX-638; Exon junction subcomplex magoh-y14.
DR ComplexPortal; CPX-681; Exon junction subcomplex Magohb-Y14.
DR ComplexPortal; CPX-683; Exon junction core complex, Magohb variant.
DR IntAct; Q9CWZ3; 39.
DR STRING; 10090.ENSMUSP00000044548; -.
DR iPTMnet; Q9CWZ3; -.
DR PhosphoSitePlus; Q9CWZ3; -.
DR SwissPalm; Q9CWZ3; -.
DR EPD; Q9CWZ3; -.
DR jPOST; Q9CWZ3; -.
DR MaxQB; Q9CWZ3; -.
DR PaxDb; Q9CWZ3; -.
DR PeptideAtlas; Q9CWZ3; -.
DR PRIDE; Q9CWZ3; -.
DR ProteomicsDB; 255041; -. [Q9CWZ3-1]
DR ProteomicsDB; 255042; -. [Q9CWZ3-2]
DR DNASU; 60365; -.
DR Ensembl; ENSMUST00000048915; ENSMUSP00000044548; ENSMUSG00000038374. [Q9CWZ3-2]
DR Ensembl; ENSMUST00000196456; ENSMUSP00000143190; ENSMUSG00000038374. [Q9CWZ3-1]
DR GeneID; 60365; -.
DR KEGG; mmu:60365; -.
DR UCSC; uc007dty.3; mouse. [Q9CWZ3-1]
DR UCSC; uc008qnk.2; mouse. [Q9CWZ3-2]
DR UCSC; uc008qnl.2; mouse.
DR CTD; 9939; -.
DR MGI; MGI:1913129; Rbm8a.
DR VEuPathDB; HostDB:ENSMUSG00000038374; -.
DR eggNOG; KOG0130; Eukaryota.
DR GeneTree; ENSGT00730000111185; -.
DR InParanoid; Q9CWZ3; -.
DR OMA; TIAVDWC; -.
DR OrthoDB; 1234149at2759; -.
DR PhylomeDB; Q9CWZ3; -.
DR TreeFam; TF314933; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 60365; 16 hits in 44 CRISPR screens.
DR ChiTaRS; Rbm8a; mouse.
DR PRO; PR:Q9CWZ3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CWZ3; protein.
DR Bgee; ENSMUSG00000038374; Expressed in dorsal pancreas and 226 other tissues.
DR ExpressionAtlas; Q9CWZ3; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:1990501; C:exon-exon junction subcomplex mago-y14; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; ISO:MGI.
DR GO; GO:2000622; P:regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
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 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 Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond;
KW 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:0000250|UniProtKB:Q9Y5S9"
FT CHAIN 2..174
FT /note="RNA-binding protein 8A"
FT /id="PRO_0000081764"
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:0000250|UniProtKB:Q9Y5S9"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S9"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S9"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S9"
FT VAR_SEQ 43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010251"
FT CONFLICT 14
FT /note="D -> N (in Ref. 2; BAB26605)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="E -> K (in Ref. 2; BAE24142 and 5; AAI32652)"
FT CONFLICT 51
FT /note="R -> Q (in Ref. 2; BAE24142 and 5; AAI32652/
FT AAI32654)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="E -> K (in Ref. 2; BAE24142 and 5; AAI32652/
FT AAI32654)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="G -> S (in Ref. 2; BAE24142 and 5; AAI32652/
FT AAI32654)"
FT /evidence="ECO:0000305"
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
