PPP1R8

Protein phosphatase 1, regulatory subunit 8

PDB rendering based on 2jpe.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
3V4Y

Identifiers

Symbols

PPP1R8 ; ARD-1; ARD1; NIPP-1; NIPP1; PRO2047

External IDs

OMIM: 602636 MGI: 2140494 HomoloGene: 8555 GeneCards: PPP1R8 Gene

Gene ontology
Molecular function	• DNA binding • RNA binding • endonuclease activity • protein serine/threonine phosphatase inhibitor activity • protein binding • protein phosphatase type 1 regulator activity • ribonuclease E activity
Cellular component	• nucleus • spliceosomal complex • nucleolus • cytoplasm • nuclear speck
Biological process	• transcription, DNA-templated • regulation of transcription, DNA-templated • mRNA processing • RNA catabolic process • cell proliferation • RNA splicing • negative regulation of catalytic activity • RNA phosphodiester bond hydrolysis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
28.16 – 28.18 Mb

Chr 4:
132.83 – 132.84 Mb

PubMed search

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]

Interactions

PPP1R8 has been shown to interact with PPP1CA,^[4]^[5] Histone deacetylase 2,^[4] SF3B1^[6] and EED.^[4]

References

↑ 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. doi:10.1073/pnas.91.22.10591. PMC 45067. PMID 7524097.
↑ 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. PMID 8473324.
↑ 3.0 3.1 "Entrez Gene: PPP1R8 protein phosphatase 1, regulatory (inhibitor) subunit 8".
↑ 4.0 4.1 4.2 Jin, Qiming; 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. (United States) 278 (33): 30677–85. doi:10.1074/jbc.M302273200. ISSN 0021-9258. PMID 12788942.
↑ Ajuh, P M; 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. (ENGLAND) 28 (3): 678–86. doi:10.1093/nar/28.3.678. PMC 102561. PMID 10637318.
↑ Boudrez, An; Beullens Monique; Waelkens Etienne; Stalmans Willy; Bollen Mathieu (August 2002). "Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1". J. Biol. Chem. (United States) 277 (35): 31834–41. doi:10.1074/jbc.M204427200. ISSN 0021-9258. PMID 12105215.

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: 3761–8. 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: 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. 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. 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.

PDB gallery

2jpe: FHA domain of NIPP1

PPP1R8

Interactions

References

Further reading