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PPP1R8 (protein phosphatase 1, regulatory (inhibitor) subunit 8)

Written2011-05Nikki Minnebo, Nele Van Dessel, Monique Beullens, Aleyde van Eynde, Mathieu Bollen
Laboratory of Biosignaling & Therapeutics, Dept Molecular Cell Biology, University of Leuven, Herestraat 49 box 901, 3000 Leuven, Belgium

(Note : for Links provided by Atlas : click)

Identity

Alias_namesprotein phosphatase 1, regulatory (inhibitor) subunit 8
protein phosphatase 1, regulatory subunit 8
Alias_symbol (synonym)ard-1
NIPP-1
PRO2047
ARD1
NIPP1
Other aliasARD-1
HGNC (Hugo) PPP1R8
LocusID (NCBI) 5511
Atlas_Id 41811
Location 1p35.3  [Link to chromosome band 1p35]
Location_base_pair Starts at 27830814 and ends at 27851672 bp from pter ( according to hg19-Feb_2009)  [Mapping PPP1R8.png]
Fusion genes
(updated 2016)
LOC100505817 (18q22.3) / PPP1R8 (1p35.3)MYO5B (18q21.1) / PPP1R8 (1p35.3)PRDX6 (1q25.1) / PPP1R8 (1p35.3)

DNA/RNA

Note ARD1 is a frequently used alias for NIPP1, however, this name actually corresponds to an alternative transcript (NIPP1gamma), which encodes a truncated form of NIPP1 encompassing residues 225-351 only. This transcript has been shown to restore endoribonuclease activity to E. coli rne gene mutants (Wang and Cohen, 1994; Claverie-Martin et al., 1997; Chang et al., 1999; Jin et al., 1999; Van Eynde et al., 1999). Moreover, note that the name ARD1 is also used for a completely unrelated protein, TRIM23 (Mishima et al., 1993).
 
  Genomic organization of the PPP1R8 gene and the alternative splice variants with their corresponding coding sequences (black line). Exons and alternative splice sites are indicated by different colors.
Description The entire PPP1R8 gene spans 20.9 kb on the forward strand of the long arm on chromosome 1. The gene contains 7 exons of which exon 1 has 5'-alternative splice sites.
Transcription The PPP1R8 gene contains 7 exons which give rise to 5 alternative splice products (see diagram above). When speaking about NIPP1, one usually refers to the NIPP1alpha isoform (39 kDa, 351 residues) which is by far the most abundant isoform in all examined mammalian tissues. When visualized by immunoblotting with C-terminal antibodies (which recognize all isoforms except NIPP1epsilon), also smaller polypeptides are visualized albeit at a much lower intensity as compared to the alpha-isoform. However, it is not clear yet whether these represent some of the other NIPP1 isoforms or simply degradation products of NIPP1alpha (Van Eynde et al., 1999; Chang et al., 1999; Fardilha et al., 2004).
Pseudogene A processed pseudogene, termed PPP1R8P, has been mapped to chromosome 1p33-32 (48790762-48791795 bp from pter according to hg19 - Feb 2009). Consistent with this notion, it is only 1034 bp in size, contains no introns and encodes an incomplete NIPP1-transcript due to the presence of various premature stop codons (Van Eynde et al., 1999).

Protein

Note Nuclear Inhibitor of PP1 (NIPP1) was first identified in bovine thymus nuclei as a potent inhibitor of the protein Ser/Thr phosphatase PP1 (Beullens et al., 1992; Beullens et al., 1993). Later on, it became clear that NIPP1 exerts various functions in the eukaryotic cell by serving as a kind of scaffold protein onto which a variety of proteins can bind. These interaction partners range from protein kinase MELK, protein phosphatase PP1 (PPP1C-a/PPP1C-b/PPP1C-c), the pre-mRNA splicing factors SAP155 (SF3B1) and CDC5L to the chromatin modifiers EED and EZH2.
 
  A schematic representation of the domain structure of NIPP1 and its interactor binding sites. The FHA-domain (red) binds the indicated interactors via a phosphorylated TP dipeptide motif. NIPP1 binds PP1 via the indicated RVXF-motif and via a C-terminal binding site (green). EED and RNA binding sites are colored blue and orange, respectively. Known phosphorylation sites are indicated in black (in vivo validated) or grey (in vitro data).
Description NIPP1 consists of 351 amino acids and has a molecular mass of 39 kDa. However, it migrates at a size of about 45 kDa on SDS-PAGE. NIPP1 contains an N-terminal ForkHead Associated (FHA) domain. Via this established phosphothreonine-binding domain, NIPP1 interacts with protein kinase MELK, the splicing factors SAP155 and CDC5L and the histone methyltransferase EZH2. Moreover, it was shown that the NIPP1 FHA-domain binds to its ligands via phosphorylated TP-dipeptide motifs, present in the interacting proteins (Boudrez et al., 2000; Boudrez et al., 2002; Vulsteke et al., 2004; Nuytten et al., 2008).
Two additional interactors, PP1 and EED, have two separate binding sites on NIPP1: one in the central domain and the other at the C-terminus. In the central domain, the binding of NIPP1 to PP1 is mediated by a so called RVXF-motif, which is present in about two thirds of all known PP1 interacting proteins (Beullens et al., 1999; Beullens et al., 2000; Hendrickx et al., 2009). In addition, the C-terminal 22 residues can interact with nucleic acids (Jin et al., 1999).
Expression NIPP1 is ubiquitously expressed (Van Eynde et al., 1995).
Localisation NIPP1 is a nuclear protein and is enriched in splicing factor storage sites called speckles (Trinkle-Mulcahy et al., 1999; Jagiello et al., 2000). Although largely nuclear, some data suggest that there also exists a cytoplasmic pool of NIPP1 (Boudrez et al., 1999; Jagiello et al., 1997).
Function NIPP1 is a scaffold protein and exerts its functions via its interacting proteins. NIPP1 was discovered as a potent inhibitor and a major nuclear interactor of the phosphatase PP1 (Beullens et al., 1999). PP1 functions as a holoenzyme in which the interacting proteins confine substrate specificity, activity and/or localization of PP1 (Bollen et al., 2010). For NIPP1, it has been shown that it acts as a physiological PP1 inhibitor for some substrates, while functioning as an activator towards other substrates (Parker et al., 2002; Lesage et al., 2004; Comerford et al., 2006; Shi and Manley, 2007). Also, the interaction between NIPP1 and PP1 can be regulated by phosphorylation (Beullens et al., 1993; Van Eynde et al., 1994; Jagiello et al., 1995; Vulsteke et al., 1997; Beullens et al., 1999).
NIPP1 is also involved in 3 other major cellular processes: splicing, transcription and development. Firstly, NIPP1 is associated with spliceosomes and splicing factor storage sites called "speckles", probably mediated by its interaction with the splicing factors CDC5L and SAP155 (Boudrez et al., 2000; Deckert et al., 2006). Pre-mRNA splicing assays showed that NIPP1 is required for late stage spliceosome formation (Beullens and Bollen, 2002). Recently it was published that NIPP1 directs associated PP1 to dephosphorylate SAP155 (Tanuma et al., 2008). Secondly, NIPP1 is a transcriptional repressor via its interaction with EED and EZH2 (Jin et al., 2003; Roy et al., 2007), two core components of the Polycomb repressive complex 2 (PRC2). Through its interaction with PRC2, NIPP1 directs it to a subset of Polycomb target genes, where the methyltransferase EZH2 will mark genes proned for silencing by trimethylating histone 3 on lysine 27 (Nuytten et al, 2008). In 2010, Van Dessel et al. showed that this targeting function of NIPP1 is dependent on associated PP1. Finally, NIPP1 is essential for embryonic development as a NIPP1 knock out mouse is embryonically lethal at the onset of gastrulation (Van Eynde et al., 2004).
The splice variant NIPP1gamma or ARD1 displays a site-specific Mg2+-dependent endoribonuclease activity, in contrast to the NIPP1alpha isoform, which does not possess this function (Wang and Cohen, 1994; Claverie-Martin et al., 1997; Chang et al., 1999; Jin et al., 1999; Van Eynde et al., 1999).
Homology NIPP1 is highly conserved in all multicellular organisms.

Implicated in

Note
  
Entity Hepatoma
Disease Cancer.
Prognosis An increase in NIPP1 mRNA is correlated with a malignant phenotype in rats (Kim et al., 2000).
  

Bibliography

The protein phosphatase-1 regulator NIPP1 is also a splicing factor involved in a late step of spliceosome assembly.
Beullens M, Bollen M.
J Biol Chem. 2002 May 31;277(22):19855-60. Epub 2002 Mar 21.
PMID 11909864
 
The extended PP1 toolkit: designed to create specificity.
Bollen M, Peti W, Ragusa MJ, Beullens M.
Trends Biochem Sci. 2010 Aug;35(8):450-8. Epub 2010 May 1. (REVIEW)
PMID 20399103
 
Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1.
Boudrez A, Beullens M, Waelkens E, Stalmans W, Bollen M.
J Biol Chem. 2002 Aug 30;277(35):31834-41. Epub 2002 Jun 24.
PMID 12105215
 
Identification of MYPT1 and NIPP1 as subunits of protein phosphatase 1 in rat liver cytosol.
Boudrez A, Evens K, Beullens M, Waelkens E, Stalmans W, Bollen M.
FEBS Lett. 1999 Jul 16;455(1-2):175-8.
PMID 10428496
 
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.
Chang AC, Sohlberg B, Trinkle-Mulcahy L, Claverie-Martin F, Cohen P, Cohen SN.
Gene. 1999 Nov 15;240(1):45-55.
PMID 10564811
 
ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E.
Claverie-Martin F, Wang M, Cohen SN.
J Biol Chem. 1997 May 23;272(21):13823-8.
PMID 9153239
 
Regulation of protein phosphatase 1gamma activity in hypoxia through increased interaction with NIPP1: implications for cellular metabolism.
Comerford KM, Leonard MO, Cummins EP, Fitzgerald KT, Beullens M, Bollen M, Taylor CT.
J Cell Physiol. 2006 Oct;209(1):211-8.
PMID 16826568
 
Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions.
Deckert J, Hartmuth K, Boehringer D, Behzadnia N, Will CL, Kastner B, Stark H, Urlaub H, Luhrmann R.
Mol Cell Biol. 2006 Jul;26(14):5528-43.
PMID 16809785
 
Alternatively spliced protein variants as potential therapeutic targets for male infertility and contraception.
Fardilha M, Wu W, Sa R, Fidalgo S, Sousa C, Mota C, da Cruz e Silva OA, da Cruz e Silva EF.
Ann N Y Acad Sci. 2004 Dec;1030:468-78.
PMID 15659832
 
Docking motif-guided mapping of the interactome of protein phosphatase-1.
Hendrickx A, Beullens M, Ceulemans H, Den Abt T, Van Eynde A, Nicolaescu E, Lesage B, Bollen M.
Chem Biol. 2009 Apr 24;16(4):365-71.
PMID 19389623
 
NIPP-1, a nuclear inhibitory subunit of protein phosphatase-1, has RNA-binding properties.
Jagiello I, Beullens M, Vulsteke V, Wera S, Sohlberg B, Stalmans W, von Gabain A, Bollen M.
J Biol Chem. 1997 Aug 29;272(35):22067-71.
PMID 9268347
 
Mapping of the RNA-binding and endoribonuclease domains of NIPP1, a nuclear targeting subunit of protein phosphatase 1.
Jin Q, Beullens M, Jagiello I, Van Eynde A, Vulsteke V, Stalmans W, Bollen M.
Biochem J. 1999 Aug 15;342 ( Pt 1):13-9.
PMID 10432294
 
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.
Jin Q, van Eynde A, Beullens M, Roy N, Thiel G, Stalmans W, Bollen M.
J Biol Chem. 2003 Aug 15;278(33):30677-85. Epub 2003 Jun 3.
PMID 12788942
 
Increased expression of NIPP-1 mRNA correlates positively with malignant phenotype in rat hepatomas.
Kim SE, Ishita A, Shima H, Nakamura K, Yamada Y, Ogawa K, Kikuchi K.
Int J Oncol. 2000 Apr;16(4):751-5.
PMID 10717244
 
Interactor-mediated nuclear translocation and retention of protein phosphatase-1.
Lesage B, Beullens M, Nuytten M, Van Eynde A, Keppens S, Himpens B, Bollen M.
J Biol Chem. 2004 Dec 31;279(53):55978-84. Epub 2004 Oct 22.
PMID 15501817
 
ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain.
Mishima K, Tsuchiya M, Nightingale MS, Moss J, Vaughan M.
J Biol Chem. 1993 Apr 25;268(12):8801-7.
PMID 8473324
 
The transcriptional repressor NIPP1 is an essential player in EZH2-mediated gene silencing.
Nuytten M, Beke L, Van Eynde A, Ceulemans H, Beullens M, Van Hummelen P, Fuks F, Bollen M.
Oncogene. 2008 Feb 28;27(10):1449-60. Epub 2007 Sep 3.
PMID 17724462
 
Functional interaction between nuclear inhibitor of protein phosphatase type 1 (NIPP1) and protein phosphatase type 1 (PP1) in Drosophila: consequences of over-expression of NIPP1 in flies and suppression by co-expression of PP1.
Parker L, Gross S, Beullens M, Bollen M, Bennett D, Alphey L.
Biochem J. 2002 Dec 15;368(Pt 3):789-97.
PMID 12358598
 
The transcriptional repression by NIPP1 is mediated by Polycomb group proteins.
Roy N, Van Eynde A, Beke L, Nuytten M, Bollen M.
Biochim Biophys Acta. 2007 Sep-Oct;1769(9-10):541-5. Epub 2007 Aug 8.
PMID 17804093
 
A complex signaling pathway regulates SRp38 phosphorylation and pre-mRNA splicing in response to heat shock.
Shi Y, Manley JL.
Mol Cell. 2007 Oct 12;28(1):79-90.
PMID 17936706
 
Nuclear inhibitor of protein phosphatase-1 (NIPP1) directs protein phosphatase-1 (PP1) to dephosphorylate the U2 small nuclear ribonucleoprotein particle (snRNP) component, spliceosome-associated protein 155 (Sap155).
Tanuma N, Kim SE, Beullens M, Tsubaki Y, Mitsuhashi S, Nomura M, Kawamura T, Isono K, Koseki H, Sato M, Bollen M, Kikuchi K, Shima H.
J Biol Chem. 2008 Dec 19;283(51):35805-14. Epub 2008 Oct 8.
PMID 18842582
 
Nuclear organisation of NIPP1, a regulatory subunit of protein phosphatase 1 that associates with pre-mRNA splicing factors.
Trinkle-Mulcahy L, Ajuh P, Prescott A, Claverie-Martin F, Cohen S, Lamond AI, Cohen P.
J Cell Sci. 1999 Jan;112 ( Pt 2):157-68.
PMID 9858469
 
The phosphatase interactor NIPP1 regulates the occupancy of the histone methyltransferase EZH2 at Polycomb targets.
Van Dessel N, Beke L, Gornemann J, Minnebo N, Beullens M, Tanuma N, Shima H, Van Eynde A, Bollen M.
Nucleic Acids Res. 2010 Nov 1;38(21):7500-12. Epub 2010 Jul 29.
PMID 20671031
 
The nuclear scaffold protein NIPP1 is essential for early embryonic development and cell proliferation.
Van Eynde A, Nuytten M, Dewerchin M, Schoonjans L, Keppens S, Beullens M, Moons L, Carmeliet P, Stalmans W, Bollen M.
Mol Cell Biol. 2004 Jul;24(13):5863-74.
PMID 15199142
 
Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1.
Vulsteke V, Beullens M, Boudrez A, Keppens S, Van Eynde A, Rider MH, Stalmans W, Bollen M.
J Biol Chem. 2004 Mar 5;279(10):8642-7. Epub 2003 Dec 29.
PMID 14699119
 
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.
Wang M, Cohen SN.
Proc Natl Acad Sci U S A. 1994 Oct 25;91(22):10591-5.
PMID 7524097
 

Citation

This paper should be referenced as such :
Minnebo, N ; Van, Dessel N ; Beullens, M ; van, Eynde A ; Bollen, M
PPP1R8 (protein phosphatase 1, regulatory (inhibitor) subunit 8)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(11):968-971.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/PPP1R8ID41811ch1p35.html


External links

Nomenclature
HGNC (Hugo)PPP1R8   9296
Cards
AtlasPPP1R8ID41811ch1p35
Entrez_Gene (NCBI)PPP1R8  5511  protein phosphatase 1 regulatory subunit 8
AliasesARD-1; ARD1; NIPP-1; NIPP1; 
PRO2047
GeneCards (Weizmann)PPP1R8
Ensembl hg19 (Hinxton)ENSG00000117751 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000117751 [Gene_View]  chr1:27830814-27851672 [Contig_View]  PPP1R8 [Vega]
ICGC DataPortalENSG00000117751
TCGA cBioPortalPPP1R8
AceView (NCBI)PPP1R8
Genatlas (Paris)PPP1R8
WikiGenes5511
SOURCE (Princeton)PPP1R8
Genetics Home Reference (NIH)PPP1R8
Genomic and cartography
GoldenPath hg38 (UCSC)PPP1R8  -     chr1:27830814-27851672 +  1p35.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)PPP1R8  -     1p35.3   [Description]    (hg19-Feb_2009)
EnsemblPPP1R8 - 1p35.3 [CytoView hg19]  PPP1R8 - 1p35.3 [CytoView hg38]
Mapping of homologs : NCBIPPP1R8 [Mapview hg19]  PPP1R8 [Mapview hg38]
OMIM602636   
Gene and transcription
Genbank (Entrez)AF061958 AF061959 AF126488 AK292077 AK297771
RefSeq transcript (Entrez)NM_002713 NM_014110 NM_138558
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)PPP1R8
Cluster EST : UnigeneHs.533474 [ NCBI ]
CGAP (NCI)Hs.533474
Alternative Splicing GalleryENSG00000117751
Gene ExpressionPPP1R8 [ NCBI-GEO ]   PPP1R8 [ EBI - ARRAY_EXPRESS ]   PPP1R8 [ SEEK ]   PPP1R8 [ MEM ]
Gene Expression Viewer (FireBrowse)PPP1R8 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5511
GTEX Portal (Tissue expression)PPP1R8
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ12972   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ12972  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ12972
Splice isoforms : SwissVarQ12972
Catalytic activity : Enzyme3.1.4.- [ Enzyme-Expasy ]   3.1.4.-3.1.4.- [ IntEnz-EBI ]   3.1.4.- [ BRENDA ]   3.1.4.- [ KEGG ]   
PhosPhoSitePlusQ12972
Domaine pattern : Prosite (Expaxy)FHA_DOMAIN (PS50006)   
Domains : Interpro (EBI)FHA_dom    SMAD_FHA_domain   
Domain families : Pfam (Sanger)FHA (PF00498)   
Domain families : Pfam (NCBI)pfam00498   
Domain families : Smart (EMBL)FHA (SM00240)  
Conserved Domain (NCBI)PPP1R8
DMDM Disease mutations5511
Blocks (Seattle)PPP1R8
PDB (SRS)3V4Y   
PDB (PDBSum)3V4Y   
PDB (IMB)3V4Y   
PDB (RSDB)3V4Y   
Structural Biology KnowledgeBase3V4Y   
SCOP (Structural Classification of Proteins)3V4Y   
CATH (Classification of proteins structures)3V4Y   
SuperfamilyQ12972
Human Protein AtlasENSG00000117751
Peptide AtlasQ12972
HPRD04028
IPIIPI00030383   IPI00142629   IPI00218794   IPI00911009   IPI00655724   IPI00028793   IPI00645094   
Protein Interaction databases
DIP (DOE-UCLA)Q12972
IntAct (EBI)Q12972
FunCoupENSG00000117751
BioGRIDPPP1R8
STRING (EMBL)PPP1R8
ZODIACPPP1R8
Ontologies - Pathways
QuickGOQ12972
Ontology : AmiGODNA binding  RNA binding  mRNA binding  endonuclease activity  protein serine/threonine phosphatase inhibitor activity  protein binding  nucleus  nucleoplasm  spliceosomal complex  cytoplasm  transcription, DNA-templated  regulation of transcription, DNA-templated  mRNA processing  RNA catabolic process  cell proliferation  RNA splicing  ribonuclease E activity  nuclear speck  negative regulation of protein dephosphorylation  negative regulation of catalytic activity  RNA phosphodiester bond hydrolysis  
Ontology : EGO-EBIDNA binding  RNA binding  mRNA binding  endonuclease activity  protein serine/threonine phosphatase inhibitor activity  protein binding  nucleus  nucleoplasm  spliceosomal complex  cytoplasm  transcription, DNA-templated  regulation of transcription, DNA-templated  mRNA processing  RNA catabolic process  cell proliferation  RNA splicing  ribonuclease E activity  nuclear speck  negative regulation of protein dephosphorylation  negative regulation of catalytic activity  RNA phosphodiester bond hydrolysis  
NDEx NetworkPPP1R8
Atlas of Cancer Signalling NetworkPPP1R8
Wikipedia pathwaysPPP1R8
Orthology - Evolution
OrthoDB5511
GeneTree (enSembl)ENSG00000117751
Phylogenetic Trees/Animal Genes : TreeFamPPP1R8
HOVERGENQ12972
HOGENOMQ12972
Homologs : HomoloGenePPP1R8
Homology/Alignments : Family Browser (UCSC)PPP1R8
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPPP1R8 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PPP1R8
dbVarPPP1R8
ClinVarPPP1R8
1000_GenomesPPP1R8 
Exome Variant ServerPPP1R8
ExAC (Exome Aggregation Consortium)PPP1R8 (select the gene name)
Genetic variants : HAPMAP5511
Genomic Variants (DGV)PPP1R8 [DGVbeta]
DECIPHERPPP1R8 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisPPP1R8 
Mutations
ICGC Data PortalPPP1R8 
TCGA Data PortalPPP1R8 
Broad Tumor PortalPPP1R8
OASIS PortalPPP1R8 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPPP1R8  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDPPP1R8
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch PPP1R8
DgiDB (Drug Gene Interaction Database)PPP1R8
DoCM (Curated mutations)PPP1R8 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PPP1R8 (select a term)
intoGenPPP1R8
NCG5 (London)PPP1R8
Cancer3DPPP1R8(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM602636   
Orphanet
MedgenPPP1R8
Genetic Testing Registry PPP1R8
NextProtQ12972 [Medical]
TSGene5511
GENETestsPPP1R8
Target ValidationPPP1R8
Huge Navigator PPP1R8 [HugePedia]
snp3D : Map Gene to Disease5511
BioCentury BCIQPPP1R8
ClinGenPPP1R8
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD5511
Chemical/Pharm GKB GenePA33659
Clinical trialPPP1R8
Miscellaneous
canSAR (ICR)PPP1R8 (select the gene name)
Other databaseUCSD Molecule pages
Probes
Litterature
PubMed63 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMinePPP1R8
EVEXPPP1R8
GoPubMedPPP1R8
iHOPPPP1R8
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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