This gene encodes a protein that is part of a post-splicing multiprotein complex, the exon junction 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.[3]
↑Loyer P, Trembley JH, Lahti JM, Kidd VJ (Jun 1998). "The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo". Journal of Cell Science. 111 ( Pt 11) (11): 1495–506. PMID9580558.
↑Badolato J, Gardiner E, Morrison N, Eisman J (Dec 1995). "Identification and characterisation of a novel human RNA-binding protein". Gene. 166 (2): 323–7. doi:10.1016/0378-1119(95)00571-4. PMID8543184.
↑Harada K, Yamada A, Yang D, Itoh K, Shichijo S (Sep 2001). "Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation". International Journal of Cancer. 93 (5): 623–8. doi:10.1002/ijc.1391. PMID11477570.
↑Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC1847948. PMID17353931.
Burn TC, Connors TD, Van Raay TJ, Dackowski WR, Millholland JM, Klinger KW, Landes GM (Jun 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 Research. 6 (6): 525–37. doi:10.1101/gr.6.6.525. PMID8828041.
Wilson KF, Fortes P, Singh US, Ohno M, Mattaj IW, Cerione RA (Feb 1999). "The nuclear cap-binding complex is a novel target of growth factor receptor-coupled signal transduction". The Journal of Biological Chemistry. 274 (7): 4166–73. doi:10.1074/jbc.274.7.4166. PMID9933612.
Harada K, Yamada A, Yang D, Itoh K, Shichijo S (Sep 2001). "Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation". International Journal of Cancer. 93 (5): 623–8. doi:10.1002/ijc.1391. PMID11477570.
Kim VN, Kataoka N, Dreyfuss G (Sep 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. PMID11546873.
Lykke-Andersen J, Shu MD, Steitz JA (Sep 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. PMID11546874.
McCracken S, Longman D, Johnstone IL, Cáceres JF, Blencowe BJ (Nov 2003). "An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation". The Journal of Biological Chemistry. 278 (45): 44153–60. doi:10.1074/jbc.M306856200. PMID12944400.
Kataoka N, Dreyfuss G (Feb 2004). "A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex". The Journal of Biological Chemistry. 279 (8): 7009–13. doi:10.1074/jbc.M307692200. PMID14625303.
Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID15324660.