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| 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 | messenger RNA |
Cross database links:
| 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
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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 | |
| Structure: | |
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| FASTA formatted sequence |
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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