PPP1R8

PPP1R8
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3V4Y
Identifiers
Aliases	PPP1R8 , ARD-1, ARD1, NIPP-1, NIPP1, PRO2047, protein phosphatase 1 regulatory subunit 8
External IDs	OMIM: 602636; MGI: 2140494; HomoloGene: 8555; GeneCards: PPP1R8; OMA:PPP1R8 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p35.3 Start 27,830,782 bp [1] End 27,851,676 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4|4 D2.3 Start 132,554,240 bp [2] End 132,570,480 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon ventricular zone islet of Langerhans ganglionic eminence stromal cell of endometrium smooth muscle tissue lymph node C1 segment granulocyte mucosa of sigmoid colon Top expressed in somite mandibular prominence maxillary prominence epiblast medial ganglionic eminence abdominal wall hand otic vesicle condyle human fetus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein serine/threonine phosphatase inhibitor activity DNA binding protein binding RNA binding protein phosphatase inhibitor activity nuclease activity endonuclease activity ribonuclease E activity hydrolase activity mRNA binding protein phosphatase regulator activity Cellular component cytoplasm nuclear speck nucleoplasm spliceosomal complex nucleus Biological process regulation of transcription, DNA-templated nucleic acid phosphodiester bond hydrolysis mRNA processing RNA catabolic process transcription, DNA-templated RNA splicing cell population proliferation RNA phosphodiester bond hydrolysis negative regulation of protein dephosphorylation negative regulation of phosphoprotein phosphatase activity regulation of phosphoprotein phosphatase activity production of miRNAs involved in gene silencing by miRNA Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5511 100336 Ensembl ENSG00000117751 ENSMUSG00000028882 UniProt Q12972 Q8R3G1 RefSeq (mRNA) NM_138558 NM_002713 NM_014110 NM_001290725 NM_146154 NM_001355198 NM_001355199 RefSeq (protein) NP_002704 NP_054829 NP_612568 NP_001277654 NP_666266 NP_001342127 NP_001342128 Location (UCSC) Chr 1: 27.83 – 27.85 Mb Chr 4: 132.55 – 132.57 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Nuclear inhibitor of protein phosphatase 1 is an enzyme that in humans is encoded by the PPP1R8 gene. ^{[5] [6] [7]}

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. ^[7]

Interactions

PPP1R8 has been shown to interact with PPP1CA, ^{[8] [9]} Histone deacetylase 2, ^[8] SF3B1 ^[10] EED ^[8] and the EZH2 domain of PRC2. ^[11]

References

1. GRCh38: Ensembl release 89: ENSG00000117751 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028882 – 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. Wang M, Cohen SN (November 1994). "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". Proc Natl Acad Sci USA. 91 (22): 10591–5. Bibcode:1994PNAS...9110591W. doi: 10.1073/pnas.91.22.10591 . PMC   45067 . PMID   7524097.
6. Mishima K, Tsuchiya M, Nightingale MS, Moss J, Vaughan M (May 1993). "ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain". J Biol Chem. 268 (12): 8801–7. doi: 10.1016/S0021-9258(18)52945-8 . PMID   8473324.
7. "Entrez Gene: PPP1R8 protein phosphatase 1, regulatory (inhibitor) subunit 8".
8. Jin Q, van Eynde Aleyde, Beullens Monique, Roy Nivedita, Thiel Gerald, Stalmans Willy, Bollen Mathieu (August 2003). "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". J. Biol. Chem. 278 (33): 30677–85. doi: 10.1074/jbc.M302273200 . ISSN   0021-9258. PMID   12788942.
9. Ajuh PM, Browne G J, Hawkes N A, Cohen P T, Roberts S G, Lamond A I (February 2000). "Association of a protein phosphatase 1 activity with the human factor C1 (HCF) complex". Nucleic Acids Res. 28 (3): 678–86. doi:10.1093/nar/28.3.678. PMC   102561 . PMID   10637318.
10. Boudrez A, Beullens Monique, Waelkens Etienne, Stalmans Willy, Bollen Mathieu (August 2002). "Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1". J. Biol. Chem. 277 (35): 31834–41. doi: 10.1074/jbc.M204427200 . ISSN   0021-9258. PMID   12105215.
11. Ferreira M, Verbinnen I, Fardilha M, Van Eynde A, Bollen M (November 2018). "The deletion of the protein phosphatase 1 regulator NIPP1 in testis causes hyperphosphorylation and degradation of the histone methyltransferase EZH2". J. Biol. Chem. 293 (47): 18031–18039. doi: 10.1074/jbc.AC118.005577 . PMC   6254331 . PMID   30305391.

Further reading

• Van Eynde A, Wera S, Beullens M, et al. (1996). "Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing". J. Biol. Chem. 270 (47): 28068–74. doi: 10.1074/jbc.270.47.28068 . PMID   7499293.
• Claverie-Martin F, Wang M, Cohen SN (1997). "ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E." J. Biol. Chem. 272 (21): 13823–8. doi: 10.1074/jbc.272.21.13823 . PMID   9153239.
• Vulsteke V, Beullens M, Waelkens E, et al. (1998). "Properties and phosphorylation sites of baculovirus-expressed nuclear inhibitor of protein phosphatase-1 (NIPP-1)". J. Biol. Chem. 272 (52): 32972–8. doi: 10.1074/jbc.272.52.32972 . PMID   9407077.
• Van Eynde A, Pérez-Callejón E, Schoenmakers E, et al. (1999). "Organization and alternate splice products of the gene encoding nuclear inhibitor of protein phosphatase-1 (NIPP-1)". Eur. J. Biochem. 261 (1): 291–300. doi: 10.1046/j.1432-1327.1999.00272.x . PMID   10103062.
• Jin Q, Beullens M, Jagiello I, et al. (1999). "Mapping of the RNA-binding and endoribonuclease domains of NIPP1, a nuclear targeting subunit of protein phosphatase 1". Biochem. J. 342. ( Pt 1) (1): 13–9. doi:10.1042/0264-6021:3420013. PMC   1220430 . PMID   10432294.
• Chang AC, Sohlberg B, Trinkle-Mulcahy L, et al. (2000). "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". Gene. 240 (1): 45–55. doi: 10.1016/S0378-1119(99)00435-7 . PMID   10564811.
• Boudrez A, Beullens M, Groenen P, et al. (2000). "NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry". J. Biol. Chem. 275 (33): 25411–7. doi: 10.1074/jbc.M001676200 . PMID   10827081.
• Jagiello I, Van Eynde A, Vulsteke V, et al. (2001). "Nuclear and subnuclear targeting sequences of the protein phosphatase-1 regulator NIPP1". J. Cell Sci. 113. Pt 21 (21): 3761–8. doi:10.1242/jcs.113.21.3761. PMID   11034904.
• Beullens M, Vulsteke V, Van Eynde A, et al. (2001). "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". Biochem. J. 352. Pt 3 (Pt 3): 651–8. PMC   1221501 . PMID   11104670.
• Trinkle-Mulcahy L, Sleeman JE, Lamond AI (2002). "Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells" . J. Cell Sci. 114 (Pt 23): 4219–28. doi:10.1242/jcs.114.23.4219. PMID   11739654.
• Beullens M, Bollen M (2002). "The protein phosphatase-1 regulator NIPP1 is also a splicing factor involved in a late step of spliceosome assembly". J. Biol. Chem. 277 (22): 19855–60. doi: 10.1074/jbc.M200847200 . PMID   11909864.
• Boudrez A, Beullens M, Waelkens E, et al. (2002). "Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1". J. Biol. Chem. 277 (35): 31834–41. doi: 10.1074/jbc.M204427200 . PMID   12105215.
• 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Ammosova T, Jerebtsova M, Beullens M, et al. (2003). "Nuclear protein phosphatase-1 regulates HIV-1 transcription". J. Biol. Chem. 278 (34): 32189–94. doi: 10.1074/jbc.M300521200 . PMID   12788939.
• Jin Q, van Eynde A, Beullens M, et al. (2003). "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". J. Biol. Chem. 278 (33): 30677–85. doi: 10.1074/jbc.M302273200 . PMID   12788942.
• Vulsteke V, Beullens M, Boudrez A, et al. (2004). "Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1". J. Biol. Chem. 279 (10): 8642–7. doi: 10.1074/jbc.M311466200 . PMID   14699119.
• Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC   442148 . PMID   15231748.
• 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. PMC   528928 . PMID   15489334.