| 释义 |
- Interactions
- References
- Further reading
{{Infobox_gene}}Nuclear inhibitor of protein phosphatase 1 is an enzyme that in humans is encoded by the PPP1R8 gene.[1][2][3]This gene, through alternative splicing, encodes three different isoforms. Two of the protein isoforms encoded by this gene are specific inhibitors of type 1 serine/threonine protein phosphatases and can bind but not cleave RNA. The third protein isoform lacks the phosphatase inhibitory function but is a single-strand endoribonuclease comparable to RNase E of E. coli. This isoform requires magnesium for its function and cleaves specific sites in A+U-rich regions of RNA.[3] InteractionsPPP1R8 has been shown to interact with PPP1CA,[4][5] Histone deacetylase 2,[4] SF3B1[6] EED [4] and the EZH2 domain of PRC2.[7] References1. ^{{cite journal |vauthors=Wang M, Cohen SN | title = ard-1: a human gene that reverses the effects of temperature-sensitive and deletion mutations in the Escherichia coli rne gene and encodes an activity producing RNase E-like cleavages | journal = Proc Natl Acad Sci USA | volume = 91 | issue = 22 | pages = 10591–5 |date=November 1994 | pmid = 7524097 | pmc = 45067 | doi =10.1073/pnas.91.22.10591 | bibcode =1994PNAS...9110591W }}
2. ^{{cite journal |vauthors=Mishima K, Tsuchiya M, Nightingale MS, Moss J, Vaughan M | title = ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain | journal = J Biol Chem | volume = 268 | issue = 12 | pages = 8801–7 |date=May 1993 | pmid = 8473324 | pmc = | doi = }}
3. ^1 {{cite web | title = Entrez Gene: PPP1R8 protein phosphatase 1, regulatory (inhibitor) subunit 8| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5511| accessdate = }}
4. ^1 2 {{cite journal |last=Jin |first=Qiming |authorlink= |author2=van Eynde Aleyde |author3=Beullens Monique |author4=Roy Nivedita |author5=Thiel Gerald |author6=Stalmans Willy |author7=Bollen Mathieu |date=August 2003 |title=The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor |journal=J. Biol. Chem. |volume=278 |issue=33 |pages=30677–85 | issn = 0021-9258| pmid = 12788942 |doi = 10.1074/jbc.M302273200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}
5. ^{{cite journal |doi=10.1093/nar/28.3.678 |last=Ajuh |first=P M |authorlink= |author2=Browne G J |author3=Hawkes N A |author4=Cohen P T |author5=Roberts S G |author6=Lamond A I |date=February 2000 |title=Association of a protein phosphatase 1 activity with the human factor C1 (HCF) complex |journal=Nucleic Acids Res. |volume=28 |issue=3 |pages=678–86 | issn = | pmid = 10637318 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=102561 }}
6. ^{{cite journal |last=Boudrez |first=An |authorlink= |author2=Beullens Monique |author3=Waelkens Etienne |author4=Stalmans Willy |author5=Bollen Mathieu |date=August 2002 |title=Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1 |journal=J. Biol. Chem. |volume=277 |issue=35 |pages=31834–41 | issn = 0021-9258| pmid = 12105215 |doi = 10.1074/jbc.M204427200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}
7. ^{{cite journal |vauthors=Ferreira M, Verbinnen I, Fardilha M, Van Eynde A, Bollen M |title=The deletion of the protein phosphatase 1 regulator NIPP1 in testis causes hyperphosphorylation and degradation of the histone methyltransferase EZH2 |journal=J. Biol. Chem. |volume=293 |issue=47 |pages=18031–18039 |date=November 2018 |pmid=30305391 |pmc=6254331 |doi=10.1074/jbc.AC118.005577 |url=}}
Further reading{{refbegin | 2}}- {{cite journal |vauthors=Van Eynde A, Wera S, Beullens M, etal |title=Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing. |journal=J. Biol. Chem. |volume=270 |issue= 47 |pages= 28068–74 |year= 1996 |pmid= 7499293 |doi=10.1074/jbc.270.47.28068 }}
- {{cite journal |vauthors=Claverie-Martin F, Wang M, Cohen SN |title=ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13823–8 |year= 1997 |pmid= 9153239 |doi=10.1074/jbc.272.21.13823 }}
- {{cite journal |vauthors=Vulsteke V, Beullens M, Waelkens E, etal |title=Properties and phosphorylation sites of baculovirus-expressed nuclear inhibitor of protein phosphatase-1 (NIPP-1). |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 32972–8 |year= 1998 |pmid= 9407077 |doi=10.1074/jbc.272.52.32972 }}
- {{cite journal |vauthors=Van Eynde A, Pérez-Callejón E, Schoenmakers E, etal |title=Organization and alternate splice products of the gene encoding nuclear inhibitor of protein phosphatase-1 (NIPP-1). |journal=Eur. J. Biochem. |volume=261 |issue= 1 |pages= 291–300 |year= 1999 |pmid= 10103062 |doi=10.1046/j.1432-1327.1999.00272.x }}
- {{cite journal |vauthors=Jin Q, Beullens M, Jagiello I, etal |title=Mapping of the RNA-binding and endoribonuclease domains of NIPP1, a nuclear targeting subunit of protein phosphatase 1. | series=342 |journal=Biochem. J. |volume=( Pt 1) |issue= 1|pages= 13–9 |year= 1999 |pmid= 10432294 |doi=10.1042/0264-6021:3420013 | pmc=1220430 }}
- {{cite journal |vauthors=Chang AC, Sohlberg B, Trinkle-Mulcahy L, etal |title=Alternative splicing regulates the production of ARD-1 endoribonuclease and NIPP-1, an inhibitor of protein phosphatase-1, as isoforms encoded by the same gene. |journal=Gene |volume=240 |issue= 1 |pages= 45–55 |year= 2000 |pmid= 10564811 |doi=10.1016/S0378-1119(99)00435-7 }}
- {{cite journal |vauthors=Boudrez A, Beullens M, Groenen P, etal |title=NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25411–7 |year= 2000 |pmid= 10827081 |doi= 10.1074/jbc.M001676200 }}
- {{cite journal |vauthors=Jagiello I, Van Eynde A, Vulsteke V, etal |title=Nuclear and subnuclear targeting sequences of the protein phosphatase-1 regulator NIPP1. | series=113 |journal=J. Cell Sci. |volume=Pt 21 |issue= |pages= 3761–8 |year= 2001 |pmid= 11034904 |doi= }}
- {{cite journal |vauthors=Beullens M, Vulsteke V, Van Eynde A, etal |title=The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding. | series=352 |journal=Biochem. J. |volume=Pt 3 |issue= |pages= 651–8 |year= 2001 |pmid= 11104670 |doi= | pmc=1221501 }}
- {{cite journal |vauthors=Trinkle-Mulcahy L, Sleeman JE, Lamond AI |title=Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells. |journal=J. Cell Sci. |volume=114 |issue= Pt 23 |pages= 4219–28 |year= 2002 |pmid= 11739654 |doi= }}
- {{cite journal |vauthors=Beullens M, Bollen M |title=The protein phosphatase-1 regulator NIPP1 is also a splicing factor involved in a late step of spliceosome assembly. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19855–60 |year= 2002 |pmid= 11909864 |doi= 10.1074/jbc.M200847200 }}
- {{cite journal |vauthors=Boudrez A, Beullens M, Waelkens E, etal |title=Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1. |journal=J. Biol. Chem. |volume=277 |issue= 35 |pages= 31834–41 |year= 2002 |pmid= 12105215 |doi= 10.1074/jbc.M204427200 }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M }}
- {{cite journal |vauthors=Ammosova T, Jerebtsova M, Beullens M, etal |title=Nuclear protein phosphatase-1 regulates HIV-1 transcription. |journal=J. Biol. Chem. |volume=278 |issue= 34 |pages= 32189–94 |year= 2003 |pmid= 12788939 |doi= 10.1074/jbc.M300521200 }}
- {{cite journal |vauthors=Jin Q, van Eynde A, Beullens M, etal |title=The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor. |journal=J. Biol. Chem. |volume=278 |issue= 33 |pages= 30677–85 |year= 2003 |pmid= 12788942 |doi= 10.1074/jbc.M302273200 }}
- {{cite journal |vauthors=Vulsteke V, Beullens M, Boudrez A, etal |title=Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1. |journal=J. Biol. Chem. |volume=279 |issue= 10 |pages= 8642–7 |year= 2004 |pmid= 14699119 |doi= 10.1074/jbc.M311466200 }}
- {{cite journal |vauthors=Colland F, Jacq X, Trouplin V, etal |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 | pmc=442148 }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
{{refend}}{{PDB Gallery|geneid=5511}}{{gene-1-stub}} |