RNPS1

RNA-binding protein with serine-rich domain 1 is a protein that in humans is encoded by the RNPS1 gene.[5][6][7]

RNPS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4A8X
Identifiers
Aliases	RNPS1, E5.1, RNA binding protein with serine rich domain 1
External IDs	OMIM: 606447 MGI: 97960 HomoloGene: 40648 GeneCards: RNPS1
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 2,253,116 bp[1] End 2,268,397 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 A3.3 Start 24,414,565 bp[2] End 24,425,901 bp[2]
Gene ontology Molecular function • mRNA 3'-UTR binding • GO:0001948 protein binding • RNA binding • nucleic acid binding Cellular component • cytoplasm • cytosol • nuclear speck • exon-exon junction complex • nucleoplasm • ASAP complex • cell nucleus Biological process • mRNA splicing, via spliceosome • termination of RNA polymerase II transcription • mRNA processing • regulation of alternative mRNA splicing, via spliceosome • mRNA export from nucleus • transcription, DNA-templated • negative regulation of mRNA splicing, via spliceosome • RNA splicing • positive regulation of apoptotic process • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • mRNA 3'-end processing • RNA export from nucleus Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10921	19826
Ensembl	ENSG00000205937	ENSMUSG00000034681
UniProt	Q15287	Q99M28
RefSeq (mRNA)	NM_001286625 NM_001286626 NM_001286627 NM_006711 NM_080594	NM_001080127 NM_001080128 NM_009070 NM_001357626
RefSeq (protein)	NP_001273554 NP_001273555 NP_001273556 NP_006702 NP_542161	NP_001073596 NP_001073597 NP_033096 NP_001344555
Location (UCSC)	Chr 16: 2.25 – 2.27 Mb	Chr 17: 24.41 – 24.43 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[7]

Interactions

RNPS1 has been shown to interact with SART3[8] and Pinin.[9][10]

References

1. GRCh38: Ensembl release 89: ENSG00000205937 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000034681 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. PMID 9580558.
6. 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. PMID 8543184.
7. "Entrez Gene: RNPS1 RNA binding protein S1, serine-rich domain".
8. 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. PMID 11477570. S2CID 24724555.
9. 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. PMC 1847948. PMID 17353931.
10. Li C, Lin RI, Lai MC, Ouyang P, Tarn WY (Oct 2003). "Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1". Molecular and Cellular Biology. 23 (20): 7363–76. doi:10.1128/MCB.23.20.7363-7376.2003. PMC 230327. PMID 14517304.

Further reading

• 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. PMID 8828041.
• 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. PMID 9933612.
• Mayeda A, Badolato J, Kobayashi R, Zhang MQ, Gardiner EM, Krainer AR (Aug 1999). "Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing". The EMBO Journal. 18 (16): 4560–70. doi:10.1093/emboj/18.16.4560. PMC 1171530. PMID 10449421.
• Le Hir H, Izaurralde E, Maquat LE, Moore MJ (Dec 2000). "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions". The EMBO Journal. 19 (24): 6860–9. doi:10.1093/emboj/19.24.6860. PMC 305905. PMID 11118221.
• 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. PMID 11477570. S2CID 24724555.
• 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. PMID 11546873. S2CID 12018200.
• 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. PMID 11546874. S2CID 389385.
• Lejeune F, Ishigaki Y, Li X, Maquat LE (Jul 2002). "The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling". The EMBO Journal. 21 (13): 3536–45. doi:10.1093/emboj/cdf345. PMC 126094. PMID 12093754.
• 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. PMID 12944400.
• Li C, Lin RI, Lai MC, Ouyang P, Tarn WY (Oct 2003). "Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1". Molecular and Cellular Biology. 23 (20): 7363–76. doi:10.1128/MCB.23.20.7363-7376.2003. PMC 230327. PMID 14517304.
• 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. PMID 14625303.
• Sakashita E, Tatsumi S, Werner D, Endo H, Mayeda A (Feb 2004). "Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo". Molecular and Cellular Biology. 24 (3): 1174–87. doi:10.1128/MCB.24.3.1174-1187.2004. PMC 321435. PMID 14729963.
• Nott A, Le Hir H, Moore MJ (Jan 2004). "Splicing enhances translation in mammalian cells: an additional function of the exon junction complex". Genes & Development. 18 (2): 210–22. doi:10.1101/gad.1163204. PMC 324426. PMID 14752011.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• 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. PMID 15324660. S2CID 2371325.

External links

• Overview of all the structural information available in the PDB for UniProt: Q15287 (RNA-binding protein with serine-rich domain 1) at the PDBe-KB.