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Q9Y5S9 (RBM8A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein 8A
Alternative name(s):
Binder of OVCA1-1
Short name=BOV-1
RNA-binding motif protein 8A
RNA-binding protein Y14
Ribonucleoprotein RBM8A
Gene names
Name:RBM8A
Synonyms:RBM8
ORF Names:HSPC114, MDS014
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length174 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator WIBG/PYM leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Its removal from cytoplasmic mRNAs requires translation initiation from EJC-bearing spliced mRNAs. Associates preferentially with mRNAs produced by splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. The MAGOH-RBM8A heterodimer is a component of the nonsense mediated decay (NMD) pathway. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. Ref.18 Ref.21 Ref.22 Ref.25 Ref.32 Ref.39

Subunit structure

Heterodimer with RBM8A. Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with WIBG/PYM; the interaction is direct and dissociates the EJC from spliced mRNAs. Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Interacts with BAT1, MAGOH, OVCA1, UPF3B, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with IPO13; the interaction mediates the nuclear import of the MAGOH-RBM8A heterodimer. Identified in the spliceosome C complex. Associates with polysomes. Ref.2 Ref.3 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29 Ref.33

Subcellular location

Nucleus. Nucleus speckle. Cytoplasm. Note: Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles. Ref.34

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the RBM8A family.

Contains 1 RRM (RNA recognition motif) domain.

Sequence caution

The sequence AAG14951.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG16782.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG16782.1 differs from that shown. Reason: Chimeric cDNA. A chimeric cDNA originating from chromosomes 1 and 5.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
mRNA transport
Nonsense-mediated mRNA decay
Translation regulation
Transport
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.19. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from mutant phenotype Ref.25. Source: UniProtKB

regulation of alternative mRNA splicing, via spliceosome

Inferred from mutant phenotype Ref.39. Source: UniProtKB

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.19. Source: UniProtKB

cytoplasm

Non-traceable author statement Ref.4. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

exon-exon junction complex

Inferred from direct assay PubMed 16601204Ref.29Ref.33. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.3Ref.4. Source: UniProtKB

   Molecular_functionRNA binding

Non-traceable author statement Ref.3. Source: UniProtKB

mRNA binding

Non-traceable author statement Ref.4. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5S9-1)

Also known as: BOV-1a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Y5S9-2)

Also known as: BOV-1b;

The sequence of this isoform differs from the canonical sequence as follows:
     44-44: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.31
Chain2 – 174173RNA-binding protein 8A
PRO_0000081763

Regions

Domain73 – 15179RRM

Amino acid modifications

Modified residue21N-acetylalanine Ref.31 Ref.36 Ref.38
Modified residue241Phosphoserine Ref.36 Ref.38
Modified residue421Phosphoserine Ref.28 Ref.30 Ref.36 Ref.38
Modified residue561Phosphoserine Ref.30 Ref.35 Ref.38

Natural variations

Alternative sequence441Missing in isoform 2.
VSP_005810

Experimental info

Mutagenesis82 – 832EE → RR: Impaired nonsense-mediated decay activity.
Mutagenesis106 – 1083LDR → RDE: Complete loss of nonsense-mediated decay activity. Ref.25
Mutagenesis1181L → R: Complete loss of nonsense-mediated decay activity. Ref.25
Mutagenesis149 – 1502CF → KA: Complete loss of nonsense-mediated decay activity.
Sequence conflict1301A → V in CAG46622. Ref.8

Secondary structure

................. 174
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (BOV-1a) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 70BBD03CDDFEECFE

FASTA17419,889
        10         20         30         40         50         60 
MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEEGSRARM REDYDSVEQD 

        70         80         90        100        110        120 
GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK NIHLNLDRRT GYLKGYTLVE 

       130        140        150        160        170 
YETYKEAQAA MEGLNGQDLM GQPISVDWCF VRGPPKGKRR GGRRRSRSPD RRRR 

« Hide

Isoform 2 (BOV-1b) [UniParc].

Checksum: 6710C1BD9CFAF92E
Show »

FASTA17319,760

References

« Hide 'large scale' references
[1]"Cloning and gene expression of a novel human ribonucleoprotein."
Conklin D.C., Rixon M.W., Kuestner R.E., Maurer M.F., Whitmore T.E., Millar R.P.
Biochim. Biophys. Acta 1492:465-469(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Skeletal muscle.
[2]"MAGOH interacts with a novel RNA-binding protein."
Zhao X.F., Nowak N.J., Shows T.B., Aplan P.D.
Genomics 63:145-148(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH MAGOH.
[3]"Identification and structural analysis of human RBM8A and RBM8B: two highly conserved RNA-binding motif proteins that interact with OVCA1, a candidate tumor suppressor."
Salicioni A.M., Xi M., Vanderveer L.A., Balsara B., Testa J.R., Dunbrack R.L. Jr., Godwin A.K.
Genomics 69:54-62(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH OVCA1.
Tissue: Brain.
[4]"Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm."
Kataoka N., Yong J., Kim V.N., Velazquez F., Perkinson R.A., Wang F., Dreyfuss G.
Mol. Cell 6:673-682(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
[5]"The genes encoding the type II gonadotropin-releasing hormone receptor and the ribonucleoprotein RBM8A in humans overlap in two genomic loci."
Faurholm B., Millar R.P., Katz A.A.
Genomics 78:15-18(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hematopoietic stem cell.
[7]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Umbilical cord blood.
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[9]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Teratocarcinoma.
[10]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon.
[13]"The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions."
Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.
EMBO J. 19:6860-6869(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RNPS1; SRRM1 AND ALYREF/THOC4.
[14]"Importin 13: a novel mediator of nuclear import and export."
Mingot J.-M., Kostka S., Kraft R., Hartmann E., Goerlich D.
EMBO J. 20:3685-3694(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IPO13.
[15]"Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex."
Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G.
EMBO J. 20:6424-6433(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALYREF/THOC4 AND THE EXON JUNCTION COMPLEX.
[16]"Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex."
Kim V.N., Kataoka N., Dreyfuss G.
Science 293:1832-1836(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B.
[17]"Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1."
Lykke-Andersen J., Shu M.-D., Steitz J.A.
Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A POST-SPLICING COMPLEX WITH NXF1; UPF1; UPF2; UPF3A; UPF3B AND RNPS1.
[18]"Translation is required to remove Y14 from mRNAs in the cytoplasm."
Dostie J., Dreyfuss G.
Curr. Biol. 12:1060-1067(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSLATION, ASSOCIATION WITH POLYSOMES, RNA-BINDING.
[19]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[20]"An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation."
McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.
J. Biol. Chem. 278:44153-44160(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAT1; RNPS1; SRRM1 AND ALYREF/THOC4.
[21]"Y14 and hUpf3b form an NMD-activating complex."
Gehring N.H., Neu-Yilik G., Schell T., Hentze M.W., Kulozik A.E.
Mol. Cell 11:939-949(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH RENT3B.
[22]"A novel mode of RBD-protein recognition in the Y14-Mago complex."
Fribourg S., Gatfield D., Izaurralde E., Conti E.
Nat. Struct. Biol. 10:433-439(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAGOH.
[23]"Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex."
Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E., Conti E.
EMBO Rep. 5:304-310(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WIBG.
[24]"A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex."
Kataoka N., Dreyfuss G.
J. Biol. Chem. 279:7009-7013(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH RNPS1 AND SRRM1.
[25]"Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements."
Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E.
Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 82-GLU-GLU-83; 106-LEU--ARG-108; LEU-118 AND 149-CYS-PHE-150.
[26]"The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity."
Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H.
Nat. Struct. Mol. Biol. 12:861-869(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX.
[27]"Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[28]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs."
Diem M.D., Chan C.C., Younis I., Dreyfuss G.
Nat. Struct. Mol. Biol. 14:1173-1179(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WIBG.
[30]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[32]"Exon junction complex enhances translation of spliced mRNAs at multiple steps."
Lee H.C., Choe J., Chi S.G., Kim Y.K.
Biochem. Biophys. Res. Commun. 384:334-340(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA TRANSLATION.
[33]"Disassembly of exon junction complexes by PYM."
Gehring N.H., Lamprinaki S., Kulozik A.E., Hentze M.W.
Cell 137:536-548(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WIBG.
[34]"Assembly and mobility of exon-exon junction complexes in living cells."
Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[35]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[36]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-42 AND SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[40]"Structure of the Y14-Magoh core of the exon junction complex."
Lau C.K., Diem M.D., Dreyfuss G., Van Duyne G.D.
Curr. Biol. 13:933-941(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 50-155 IN COMPLEX WITH MAGOH.
[41]"The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA."
Bono F., Ebert J., Lorentzen E., Conti E.
Cell 126:713-725(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 66-154 IN THE EJC COMPLEX WITH CASC3; EIF4A3; MAGOH AND AMP-PNP.
[42]"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA."
Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H., Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R.
Science 313:1968-1972(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 64-154 IN THE EJC COMPLEX WITH CASC3; EIF4A3; MAGOH AND ADP-NP.
[43]"Mechanism of ATP turnover inhibition in the EJC."
Nielsen K.H., Chamieh H., Andersen C.B., Fredslund F., Hamborg K., Le Hir H., Andersen G.R.
RNA 15:67-75(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 51-174 IN THE EJC COMPLEX WITH CASC3; EIF4A3; MAGOH AND TRANSITION STATE ANALOG ADP-ALF3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF127761 mRNA. Translation: AAD21089.1.
AF198620 mRNA. Translation: AAF37551.1.
AF231511 mRNA. Translation: AAG16781.1.
AF231512 mRNA. Translation: AAG16782.1. Different initiation.
AF299118 mRNA. Translation: AAG27091.1.
AF403012 Genomic DNA. Translation: AAL26999.1.
AF182415 mRNA. Translation: AAG14951.1. Different initiation.
AF161463 mRNA. Translation: AAF29078.1.
CR541823 mRNA. Translation: CAG46622.1.
CR541805 mRNA. Translation: CAG46604.1.
AK075009 mRNA. Translation: BAG52051.1.
AL160282 Genomic DNA. No translation available.
CH471244 Genomic DNA. Translation: EAW71419.1.
BC017088 mRNA. Translation: AAH17088.1.
RefSeqNP_005096.1. NM_005105.4.
UniGeneHs.591455.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P27X-ray2.00B/D50-155[»]
2HYIX-ray2.30B/H64-154[»]
2J0QX-ray3.20D/G66-174[»]
2J0SX-ray2.21D66-154[»]
2XB2X-ray3.40D/Z66-155[»]
3EX7X-ray2.30B/G51-174[»]
ProteinModelPortalQ9Y5S9.
SMRQ9Y5S9. Positions 12-155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115265. 61 interactions.
DIPDIP-33070N.
IntActQ9Y5S9. 36 interactions.
MINTMINT-265248.
STRING9606.ENSP00000333001.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteQ9Y5S9.

Polymorphism databases

DMDM10720244.

Proteomic databases

PaxDbQ9Y5S9.
PRIDEQ9Y5S9.

Protocols and materials databases

DNASU9939.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330165; ENSP00000333001; ENSG00000131795. [Q9Y5S9-1]
ENST00000369307; ENSP00000358313; ENSG00000131795. [Q9Y5S9-2]
GeneID9939.
KEGGhsa:9939.
UCSCuc001ent.2. human. [Q9Y5S9-1]
uc001enu.2. human. [Q9Y5S9-2]

Organism-specific databases

CTD9939.
GeneCardsGC01P145507.
HGNCHGNC:9905. RBM8A.
HPACAB012803.
HPA018403.
MIM605313. gene.
neXtProtNX_Q9Y5S9.
Orphanet3320. Thrombocytopenia - absent radius.
PharmGKBPA34270.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000183826.
HOVERGENHBG055173.
InParanoidQ9Y5S9.
KOK12876.
OMAWILFVTS.
OrthoDBEOG7C5MB6.
PhylomeDBQ9Y5S9.
TreeFamTF314933.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

BgeeQ9Y5S9.
CleanExHS_RBM8A.
GenevestigatorQ9Y5S9.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR008111. RNA-bd_8.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
PRINTSPR01738. RNABINDINGM8.
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBM8A. human.
EvolutionaryTraceQ9Y5S9.
GeneWikiRBM8A.
GenomeRNAi9939.
NextBio37498.
PMAP-CutDBQ9Y5S9.
PROQ9Y5S9.
SOURCESearch...

Entry information

Entry nameRBM8A_HUMAN
AccessionPrimary (citable) accession number: Q9Y5S9
Secondary accession number(s): B3KQI9 expand/collapse secondary AC list , Q6FHD1, Q6IQ40, Q9GZX8, Q9NZI4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM