| |
|---|---|
| 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 | messenger RNA |
Cross database links:
| 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 | |
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1: MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEEGSRARM REDYDSVEQD 61: GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK NIHLNLDRRT GYLKGYTLVE 121: YETYKEAQAA MEGLNGQDLM GQPISVDWCF VRGPPKGKRR GGRRRSRSPD RRRR