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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:Q15287
Protein Name:RNA-binding protein with serine-rich domain 1 aka RNPS1 aka LDC2
Length:305
Molecular Weight:34208.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Nucleus1
Substrate mRNA

Cross database links:

Genevestigator: Q15287
eggNOG: prNOG20034
RefSeq: NP_006702.1    NP_542161.1   
Entrez Gene ID: 10921   
Pfam: PF00076   
OMIM: 606447  gene
KEGG: hsa:10921   

Gene Ontology

GO:0005737 C:cytoplasm
GO:0016607 C:nuclear speck
GO:0000166 F:nucleotide binding
GO:0005515 F:protein binding
GO:0003723 F:RNA binding
GO:0006397 P:mRNA processing
GO:0000184 P:nuclear-transcribed mRNA catabolic process,...
GO:0008380 P:RNA splicing
GO:0006350 P:transcription

References (25)

[1] “Identification and characterisation of a novel human RNA-binding protein.”  Badolato J.et.al.   8543184
[2] “The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinases in vivo.”  Loyer P.et.al.   9580558
[3] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[4] “The sequence and analysis of duplication-rich human chromosome 16.”  Martin J.et.al.   15616553
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing.”  Mayeda A.et.al.   10449421
[7] “The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions.”  Le Hir H.et.al.   11118221
[8] “Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation.”  Harada K.et.al.   11477570
[9] “Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1.”  Lykke-Andersen J.et.al.   11546874
[10] “An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation.”  McCracken S.et.al.   12944400
[11] “Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1.”  Li C.et.al.   14517304
[12] “Splicing enhances translation in mammalian cells: an additional function of the exon junction complex.”  Nott A.et.al.   14752011
[13] “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
[14] “Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo.”  Sakashita E.et.al.   14729963
[15] “Large-scale characterization of HeLa cell nuclear phosphoproteins.”  Beausoleil S.A.et.al.   15302935
[16] “Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation.”  Trembley J.H.et.al.   15684395
[17] “Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements.”  Gehring N.H.et.al.   16209946
[18] “Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.”  Rush J.et.al.   15592455
[19] “Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core.”  Tange T.O.et.al.   16314458
[20] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[21] “The abundance of RNPS1, a protein component of the exon junction complex, can determine the variability in efficiency of the nonsense mediated decay pathway.”  Viegas M.H.et.al.   17586820
[22] “Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.”  Molina H.et.al.   17287340
[23] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[24] “Assembly and mobility of exon-exon junction complexes in living cells.”  Schmidt U.et.al.   19324961
[25] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
Structure:
4A8X     

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FASTA formatted sequence
1:	MDLSGVKKKS LLGVKENNKK SSTRAPSPTK RKDRSDEKSK DRSKDKGATK ESSEKDRGRD 
61:	KTRKRRSASS GSSSTRSRSS STSSSGSSTS TGSSSGSSSS SASSRSGSSS TSRSSSSSSS 
121:	SGSPSPSRRR HDNRRRSRSK SKPPKRDEKE RKRRSPSPKP TKVHIGRLTR NVTKDHIMEI 
181:	FSTYGKIKMI DMPVERMHPH LSKGYAYVEF ENPDEAEKAL KHMDGGQIDG QEITATAVLA 
241:	PWPRPPPRRF SPPRRMLPPP PMWRRSPPRM RRRSRSPRRR SPVRRRSRSP GRRRHRSRSS 
301:	SNSSR