RNPS1: Difference between revisions
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{{ | '''RNA-binding protein with serine-rich domain 1''' is a [[protein]] that in humans is encoded by the ''RNPS1'' [[gene]].<ref name="pmid9580558">{{cite journal | vauthors = Loyer P, Trembley JH, Lahti JM, Kidd VJ | title = The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo | journal = Journal of Cell Science | volume = 111 ( Pt 11) | issue = 11 | pages = 1495–506 | date = Jun 1998 | pmid = 9580558 | pmc = | doi = }}</ref><ref name="pmid8543184">{{cite journal | vauthors = Badolato J, Gardiner E, Morrison N, Eisman J | title = Identification and characterisation of a novel human RNA-binding protein | journal = Gene | volume = 166 | issue = 2 | pages = 323–7 | date = Dec 1995 | pmid = 8543184 | pmc = | doi = 10.1016/0378-1119(95)00571-4 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RNPS1 RNA binding protein S1, serine-rich domain| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10921| accessdate = }}</ref> | ||
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== 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.<ref name="entrez" /> | |||
== | == Interactions == | ||
{{protein- | RNPS1 has been shown to [[Protein-protein interaction|interact]] with [[SART3]]<ref name=pmid11477570>{{cite journal | vauthors = Harada K, Yamada A, Yang D, Itoh K, Shichijo S | title = Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation | journal = International Journal of Cancer | volume = 93 | issue = 5 | pages = 623–8 | date = Sep 2001 | pmid = 11477570 | doi = 10.1002/ijc.1391 }}</ref> and [[Pinin]].<ref name=pmid17353931>{{cite journal | vauthors = 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 | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}</ref><ref name=pmid14517304>{{cite journal | vauthors = Li C, Lin RI, Lai MC, Ouyang P, Tarn WY | title = Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1 | journal = Molecular and Cellular Biology | volume = 23 | issue = 20 | pages = 7363–76 | date = Oct 2003 | pmid = 14517304 | pmc = 230327 | doi = 10.1128/MCB.23.20.7363-7376.2003 }}</ref> | ||
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== References == | |||
{{Reflist}} | |||
== Further reading == | |||
{{Refbegin | 2}} | |||
* {{cite journal | vauthors = Burn TC, Connors TD, Van Raay TJ, Dackowski WR, Millholland JM, Klinger KW, Landes GM | title = 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 | journal = Genome Research | volume = 6 | issue = 6 | pages = 525–37 | date = Jun 1996 | pmid = 8828041 | doi = 10.1101/gr.6.6.525 }} | |||
* {{cite journal | vauthors = Wilson KF, Fortes P, Singh US, Ohno M, Mattaj IW, Cerione RA | title = The nuclear cap-binding complex is a novel target of growth factor receptor-coupled signal transduction | journal = The Journal of Biological Chemistry | volume = 274 | issue = 7 | pages = 4166–73 | date = Feb 1999 | pmid = 9933612 | doi = 10.1074/jbc.274.7.4166 }} | |||
* {{cite journal | vauthors = Mayeda A, Badolato J, Kobayashi R, Zhang MQ, Gardiner EM, Krainer AR | title = Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing | journal = The EMBO Journal | volume = 18 | issue = 16 | pages = 4560–70 | date = Aug 1999 | pmid = 10449421 | pmc = 1171530 | doi = 10.1093/emboj/18.16.4560 }} | |||
* {{cite journal | vauthors = Le Hir H, Izaurralde E, Maquat LE, Moore MJ | title = The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions | journal = The EMBO Journal | volume = 19 | issue = 24 | pages = 6860–9 | date = Dec 2000 | pmid = 11118221 | pmc = 305905 | doi = 10.1093/emboj/19.24.6860 }} | |||
* {{cite journal | vauthors = Harada K, Yamada A, Yang D, Itoh K, Shichijo S | title = Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation | journal = International Journal of Cancer | volume = 93 | issue = 5 | pages = 623–8 | date = Sep 2001 | pmid = 11477570 | doi = 10.1002/ijc.1391 }} | |||
* {{cite journal | vauthors = Kim VN, Kataoka N, Dreyfuss G | title = Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex | journal = Science | volume = 293 | issue = 5536 | pages = 1832–6 | date = Sep 2001 | pmid = 11546873 | doi = 10.1126/science.1062829 }} | |||
* {{cite journal | vauthors = Lykke-Andersen J, Shu MD, Steitz JA | title = Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1 | journal = Science | volume = 293 | issue = 5536 | pages = 1836–9 | date = Sep 2001 | pmid = 11546874 | doi = 10.1126/science.1062786 }} | |||
* {{cite journal | vauthors = Lejeune F, Ishigaki Y, Li X, Maquat LE | title = The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling | journal = The EMBO Journal | volume = 21 | issue = 13 | pages = 3536–45 | date = Jul 2002 | pmid = 12093754 | pmc = 126094 | doi = 10.1093/emboj/cdf345 }} | |||
* {{cite journal | vauthors = McCracken S, Longman D, Johnstone IL, Cáceres JF, Blencowe BJ | title = An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation | journal = The Journal of Biological Chemistry | volume = 278 | issue = 45 | pages = 44153–60 | date = Nov 2003 | pmid = 12944400 | doi = 10.1074/jbc.M306856200 }} | |||
* {{cite journal | vauthors = Li C, Lin RI, Lai MC, Ouyang P, Tarn WY | title = Nuclear Pnn/DRS protein binds to spliced mRNPs and participates in mRNA processing and export via interaction with RNPS1 | journal = Molecular and Cellular Biology | volume = 23 | issue = 20 | pages = 7363–76 | date = Oct 2003 | pmid = 14517304 | pmc = 230327 | doi = 10.1128/MCB.23.20.7363-7376.2003 }} | |||
* {{cite journal | vauthors = Kataoka N, Dreyfuss G | title = A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex | journal = The Journal of Biological Chemistry | volume = 279 | issue = 8 | pages = 7009–13 | date = Feb 2004 | pmid = 14625303 | doi = 10.1074/jbc.M307692200 }} | |||
* {{cite journal | vauthors = Sakashita E, Tatsumi S, Werner D, Endo H, Mayeda A | title = Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo | journal = Molecular and Cellular Biology | volume = 24 | issue = 3 | pages = 1174–87 | date = Feb 2004 | pmid = 14729963 | pmc = 321435 | doi = 10.1128/MCB.24.3.1174-1187.2004 }} | |||
* {{cite journal | vauthors = Nott A, Le Hir H, Moore MJ | title = Splicing enhances translation in mammalian cells: an additional function of the exon junction complex | journal = Genes & Development | volume = 18 | issue = 2 | pages = 210–22 | date = Jan 2004 | pmid = 14752011 | pmc = 324426 | doi = 10.1101/gad.1163204 }} | |||
* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }} | |||
* {{cite journal | vauthors = 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 | title = Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization | journal = Current Biology | volume = 14 | issue = 16 | pages = 1436–50 | date = Aug 2004 | pmid = 15324660 | doi = 10.1016/j.cub.2004.07.051 }} | |||
{{Refend}} | |||
{{Protein-stub}} |
Latest revision as of 22:04, 25 November 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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RNA-binding protein with serine-rich domain 1 is a protein that in humans is encoded by the RNPS1 gene.[1][2][3]
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.[3]
Interactions
RNPS1 has been shown to interact with SART3[4] and Pinin.[5][6]
References
- ↑ 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.
- ↑ 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.
- ↑ 3.0 3.1 "Entrez Gene: RNPS1 RNA binding protein S1, serine-rich domain".
- ↑ 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.
- ↑ 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.
- ↑ 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.
- 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.
- 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.
- 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.
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