RNPS1

From Wikipedia, the free encyclopedia


RNA binding protein S1, serine-rich domain
Identifiers
Symbol(s) RNPS1; E5.1; MGC117332
External IDs OMIM: 606447 HomoloGene40648
Orthologs
Human Mouse
Entrez 10921 n/a


Refseq NM_006711 (mRNA)
NP_006702 (protein)
n/a (mRNA)
n/a (protein)
Pubmed search [1] n/a

RNA binding protein S1, serine-rich domain, also known as RNPS1, is a human gene.[1]

This gene encodes a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA surveillance. mRNA surveillance detects exported mRNAs with truncated open reading frames and initiates nonsense-mediated mRNA decay (NMD). When translation ends upstream from the last exon-exon junction, this triggers NMD to degrade mRNAs containing premature stop codons. This protein binds to the mRNA and remains bound after nuclear export, acting as a nucleocytoplasmic shuttling protein. This protein contains many serine residues. Two splice variants have been found for this gene; both variants encode the same protein.[1]

[edit] References

[edit] Further reading

  • Badolato J, Gardiner E, Morrison N, Eisman J (1996). "Identification and characterisation of a novel human RNA-binding protein.". Gene 166 (2): 323–7. PMID 8543184. 
  • Burn TC, Connors TD, Van Raay TJ, et al. (1996). "Generation of a transcriptional map for a 700-kb region surrounding the polycystic kidney disease type 1 (PKD1) and tuberous sclerosis type 2 (TSC2) disease genes on human chromosome 16p3.3.". Genome Res. 6 (6): 525–37. PMID 8828041. 
  • Loyer P, Trembley JH, Lahti JM, Kidd VJ (1998). "The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo.". J. Cell. Sci. 111 ( Pt 11): 1495–506. PMID 9580558. 
  • Wilson KF, Fortes P, Singh US, et al. (1999). "The nuclear cap-binding complex is a novel target of growth factor receptor-coupled signal transduction.". J. Biol. Chem. 274 (7): 4166–73. PMID 9933612. 
  • Mayeda A, Badolato J, Kobayashi R, et al. (1999). "Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing.". EMBO J. 18 (16): 4560–70. doi:10.1093/emboj/18.16.4560. PMID 10449421. 
  • Le Hir H, Izaurralde E, Maquat LE, Moore MJ (2001). "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions.". EMBO J. 19 (24): 6860–9. doi:10.1093/emboj/19.24.6860. PMID 11118221. 
  • Harada K, Yamada A, Yang D, et al. (2001). "Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation.". Int. J. Cancer 93 (5): 623–8. PMID 11477570. 
  • Kim VN, Kataoka N, Dreyfuss G (2001). "Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex.". Science 293 (5536): 1832–6. doi:10.1126/science.1062829. PMID 11546873. 
  • Lykke-Andersen J, Shu MD, Steitz JA (2001). "Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1.". Science 293 (5536): 1836–9. doi:10.1126/science.1062786. PMID 11546874. 
  • Lejeune F, Ishigaki Y, Li X, Maquat LE (2002). "The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling.". EMBO J. 21 (13): 3536–45. doi:10.1093/emboj/cdf345. PMID 12093754. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • McCracken S, Longman D, Johnstone IL, et al. (2004). "An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation.". J. Biol. Chem. 278 (45): 44153–60. doi:10.1074/jbc.M306856200. PMID 12944400. 
  • Li C, Lin RI, Lai MC, et al. (2003). "Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1.". Mol. Cell. Biol. 23 (20): 7363–76. PMID 14517304. 
  • Kataoka N, Dreyfuss G (2004). "A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex.". J. Biol. Chem. 279 (8): 7009–13. doi:10.1074/jbc.M307692200. PMID 14625303. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Sakashita E, Tatsumi S, Werner D, et al. (2004). "Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo.". Mol. Cell. Biol. 24 (3): 1174–87. PMID 14729963. 
  • Nott A, Le Hir H, Moore MJ (2004). "Splicing enhances translation in mammalian cells: an additional function of the exon junction complex.". Genes Dev. 18 (2): 210–22. doi:10.1101/gad.1163204. PMID 14752011. 
  • Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935. 
  • Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.