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3.A.18.1.1
The nuclear mRNA Export Complex (mRNA-E also called TREX) (including the exon junction complex) [TAP+p15 interact as a complex with the nuclear pore to facilitate mRNA transport to the cytoplasm] (Nojimma et al. 2007; Cheng et al., 2006)

Accession Number:Q9Y5S9
Protein Name:RNA-binding protein 8A aka Y14
Length:174
Molecular Weight:19889.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Nucleus1
Substrate mRNA

Cross database links:

Genevestigator: Q9Y5S9
eggNOG: prNOG19287
HEGENOM: HBG756718
RefSeq: NP_005096.1   
Entrez Gene ID: 9939   
Pfam: PF00076   
OMIM: 605313  gene
KEGG: hsa:9939   

Gene Ontology

GO:0005737 C:cytoplasm
GO:0035145 C:exon-exon junction complex
GO:0016607 C:nuclear speck
GO:0005681 C:spliceosomal complex
GO:0003729 F:mRNA binding
GO:0000166 F:nucleotide binding
GO:0005515 F:protein binding
GO:0006397 P:mRNA processing
GO:0051028 P:mRNA transport
GO:0000184 P:nuclear-transcribed mRNA catabolic process,...
GO:0006417 P:regulation of translation
GO:0008380 P:RNA splicing

References (38)

[1] “Cloning and gene expression of a novel human ribonucleoprotein.”  Conklin D.C.et.al.   11004516
[2] “MAGOH interacts with a novel RNA-binding protein.”  Zhao X.F.et.al.   10662555
[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.et.al.   11013075
[4] “Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm.”  Kataoka N.et.al.   11030346
[5] “The genes encoding the type II gonadotropin-releasing hormone receptor and the ribonucleoprotein RBM8A in humans overlap in two genomic loci.”  Faurholm B.et.al.   11707068
[6] “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.et.al.   11042152
[7] “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.et.al.   16303743
[8] “The DNA sequence and biological annotation of human chromosome 1.”  Gregory S.G.et.al.   16710414
[9] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[10] “The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions.”  Le Hir H.et.al.   11118221
[11] “Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex.”  Kataoka N.et.al.   11707413
[12] “Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex.”  Kim V.N.et.al.   11546873
[13] “Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1.”  Lykke-Andersen J.et.al.   11546874
[14] “Translation is required to remove Y14 from mRNAs in the cytoplasm.”  Dostie J.et.al.   12121612
[15] “Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.”  Jurica M.S.et.al.   11991638
[16] “An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation.”  McCracken S.et.al.   12944400
[17] “Y14 and hUpf3b form an NMD-activating complex.”  Gehring N.H.et.al.   12718880
[18] “A novel mode of RBD-protein recognition in the Y14-Mago complex.”  Fribourg S.et.al.   12730685
[19] “Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex.”  Bono F.et.al.   14968132
[20] “A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex.”  Kataoka N.et.al.   14625303
[21] “Large-scale characterization of HeLa cell nuclear phosphoproteins.”  Beausoleil S.A.et.al.   15302935
[22] “Global phosphoproteome of HT-29 human colon adenocarcinoma cells.”  Kim J.-E.et.al.   16083285
[23] “Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements.”  Gehring N.H.et.al.   16209946
[24] “The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity.”  Ballut L.et.al.   16170325
[25] “Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core.”  Tange T.O.et.al.   16314458
[26] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[27] “A probability-based approach for high-throughput protein phosphorylation analysis and site localization.”  Beausoleil S.A.et.al.   16964243
[28] “PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs.”  Diem M.D.et.al.   18026120
[29] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[30] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[31] “Exon junction complex enhances translation of spliced mRNAs at multiple steps.”  Lee H.C.et.al.   19409878
[32] “Disassembly of exon junction complexes by PYM.”  Gehring N.H.et.al.   19410547
[33] “Assembly and mobility of exon-exon junction complexes in living cells.”  Schmidt U.et.al.   19324961
[34] “Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.”  Mayya V.et.al.   19690332
[35] “Structure of the Y14-Magoh core of the exon junction complex.”  Lau C.K.et.al.   12781131
[36] “The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA.”  Bono F.et.al.   16923391
[37] “Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA.”  Andersen C.B.et.al.   16931718
[38] “Mechanism of ATP turnover inhibition in the EJC.”  Nielsen K.H.et.al.   19033377
Structure:
1P27   2HYI   2J0Q   2J0S   3EX7   2XB2     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEEGSRARM REDYDSVEQD 
61:	GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK NIHLNLDRRT GYLKGYTLVE 
121:	YETYKEAQAA MEGLNGQDLM GQPISVDWCF VRGPPKGKRR GGRRRSRSPD RRRR