PPP1R9B (protein phosphatase 1, regulatory subunit 9B)

Written2012-03Amancio Carnero
Instituto de Biomedicina de Sevilla, (IBIS/HUVR/CSIC/Universidad de Sevilla); Consejo Superior de Investigaciones Cientificas, Edificio IBIS, Campus Hospital Universitario Virgen del Rocio, vda. Manuel Siurot s/n, 41013, Sevilla, Spain

(Note : for Links provided by Atlas : click)

1. Identity

General Information
protein phosphatase 1, regulatory subunit 9B, spinophilin
protein phosphatase 1, regulatory (inhibitor) subunit 9B
protein phosphatase 1, regulatory subunit 9B
Alias_symbol (synonym)Spn
Other alias
LocusID (NCBI) 84687
Atlas_Id 51558
Location 17q21.33  [Link to chromosome band 17q21]
Location_base_pair Starts at 50133735 and ends at 50150517 bp from pter ( according to hg19-Feb_2009)  [Mapping PPP1R9B.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
CERCAM (9q34.11) / PPP1R9B (17q21.33)PPP1R9B (17q21.33) / CLTC (17q23.1)PPP1R9B (17q21.33) / FLNA (Xq28)
SGCA (17q21.33) / PPP1R9B (17q21.33)ZNF318 (6p21.1) / PPP1R9B (17q21.33)


  Scheme of the 17q21 locus. Adapted from Carnero, 2012.

3. Protein

  Scheme of the PPP1R9B protein. Below bars indicate binding regions for proteins indicated. Adapted from Carnero, 2012.
Description PPP1R9B protein have different modular domains that govern protein-protein interactions (Sarrouilhe et al., 2006). These domains include two F-actin-, three potential Src homology 3 (SH3)-, one receptor- and one PP1-binding domains, one PDZ binding domain, three coiled-coil domains, and one potential leucine/isoleucine zipper motif. Many partner proteins of PPP1R9B have been described, including enzymes, guanine nucleotide exchange factors, cytoskeletal and cell adhesion molecules, membrane receptors, ion channels and G-protein signaling protein regulators. PPP1R9B also regulates seven-transmembrane receptor signaling and may link these receptors to intracellular mitogenic signaling dependent on p70S6k and the Rac-GEF. Accordingly, PPP1R9B may serve as a linker between actin cytoskeleton and transmembrane proteins, targeting PP1 to its targets and facilitating the coordination of the external signaling with the downstream pathway (Brady et al., 2003; Küntziger et al., 2011; Sarrouilhe et al., 2006; Vivo et al., 2001; Wang et al., 2004; Carnero, 2012).
Expression PPP1R9B was detected predominantly in dendritic spines in prefrontal cortex and is enriched in cerebral cortex, caudatoputamen, hypocampal formation and cerebellum. But expression in most normal tissues is also clearly detected (Muly et al., 2004; Ouimet et al., 2004). PPP1R9B protein is downrelulated in a great variety of human carcinomas but in a low percentage of tumors. Immunohistochemical analysis of PPP1R9B during cancer progression shows some correlation with tumoral progression and p53 mutations (Carnero, 2012).
Localisation In most tissues, with higher levels in neural system.
Function The structure of PPP1R9B suggests that functions as a protein scaffold that regulates both membrane and cytoskeletal functions. PPP1R9B performs important functions in the nervous system where it is implicated in the regulation of spine morphology and density, synaptic plasticity and neuronal migration. PPP1R9B could serve as a link between excitatory synapse transmission and changes in spine morphology and density (Allen et al., 2006; Hsieh-Wilson et al., 1999; Sarrouilhe et al., 2006).
PPP1R9B is a key modulator of the opiate action. PPP1R9B also promotes endocytosis of the mu-opioid receptor (Charlton et al., 2008).
PPP1R9B has been implicated through PP1 binding in the regulation of AMPA-type glutamate receptor. PPP1R9B may serve to regulate excitatory synaptic transmission and plasticity by targeting PP1 to its cellular substrates, promoting their downregulation by dephosphorylation regulating the post-synaptic glutaminergic neurotransmission. PKA modulation of the localization of the PPP1R9B/PP1 complex could contribute to this effect. Plasticity in dendritic spines may underlie learning and memory, and observations in PPP1R9B null mice shown that PPP1R9B plays a role in learning in vivo (Hsieh-Wilson et al., 2003; Stafstrom-Davis et al., 2001; Yan et al., 1999).
PPP1R9B also has a role in the regulation of blood pressure and cardiac function (da Costa-Goncalves et al., 2008). Since PPP1R9B can control the intensity and duration of the G-protein receptor signaling influencing synaptic activity, PPP1R9B affects blood pressure through central mechanisms. In adult cardiomyocytes it has been proposed that PPP1R9B is an upstream regulator required for normal growth and excitation-contraction coupling, but is dispensable for b-adrenergic stimulation (Petzhold et al., 2011). Association of PPP1R9B with the α2-AR leads to alteration of α2-AR phosphorylation following agonist stimulation, suggesting that Spn acts mainly as an antagonist of arrestin. Thus, PPP1R9B participates in the regulation of signaling duration and sensitivity of the α2-AR response therefore regulating smooth muscle contraction. Following agonist treatment, PPP1R9B competition with GRK for α2-AR also prevents α2-AR endocytosis.
Finally, a role for PPP1R9B in the formation of immunological synapses in dendritic cells has also been proposed, and PPP1R9B may be involved in the maintenance of cellular architecture by regulating actin assembly (Meng et al., 2009; Shaw and Filbert, 2009).

4. Implicated in

Entity Various cancers
Prognosis Expression levels decrease in some carcinomas.
PPP1R9B expression in colon: left, normal epithelia with high levels PPPR1B; right, PPP1RB downregulation in carcinoma.
Oncogenesis PPP1R9B mRNA is lost in a percentage of renal carcinomas and lung adenocarcinomas (Carnero, 2012). More interestingly, analysis of normal vs tumoral samples of tumors of the CNS showed clear downregulation of PPP1R9B in tumoral samples. Furthermore, lower levels of PPP1R9B mRNA correlates with higher grade of ovarian carcinoma and chronic myelogenous leukaemia (Carnero, 2012). PPP1R9B is also lost in 20% and reduced in another 37% of human lung tumors (Molina-Pinelo et al., 2011). PPP1R9B reduction correlates with malignant grade and p53 mutations (Carnero, 2012).
The PPP1R9B gene is located in chromosome 17, at position 17q21.33, and in a cytogenetic area frequently associated with microsatellite instability and loss of heterozygosity. This region is comprised of a relatively high density of tumor suppressor genes, including known (BRCA1, NME1), putative (JUP, prohibitin), and unidentified candidates distal to the BRCA1 locus (Carnero, 2012).
Most of the studies on the 17q21 locus have focused on BRCA1, which exhibits a variable frequency in LOH depending on the type of tumor, stage and marker employed, and has been extensively studied in breast carcinomas (Caduff et al., 1999; Maitra et al., 1999; Querzoli et al., 2001). However, there are few studies that suggest the existence of unknown tumor suppressor genes for breast tumors in an area that includes the locus of PPP1R9B. LOH in chromosome 17q21.3 has been observed in different tumors, including breast, ovarian, prostate, colorectal, gastric, renal and lung carcinomas, as well as in salivary gland carcinosarcoma, an extremely aggressive neoplasm (Caduff et al., 1999; Maitra et al., 1999; Querzoli et al., 2001).
The markers used in some of these studies with no linkage to BRCA1 point to NME1 as a tumor suppressor gene candidate to justify the functional impact of the allelic loss. However, in different LOH studies an unidentified tumor suppressor gene nearby NME1 has been proposed. PPP1R9B is located in close proximity to NME1, at only 1 Mb, probably sharing the allelic loss in these studies.
The most relevant data according to PPP1R9B LOH came from a study on primary lung carcinoma (Abujiang et al., 1998). This group performed an extensive LOH mapping in human lung cancers, using 15 highly polymorphic markers, 7 of which span 17q11-24 region. The higher LOH value appeared with the D17S588 marker, showing a 53% of loss. The D17S588 marker locates exactly within the PPP1R9B locus. These data provided the first robust data implicating PPP1R9B LOH in cancer. Closer tumor suppressor genes, such as BRCA1, were not seriously affected (6-13% LOH), nor other lung proliferative pathologies (squamous cell carcinoma and small cell carcinoma only showed minimal LOH, below 14%, for both PPP1R9B and BRCA1 markers).
Several genetic linkage studies using the marker D17S588 have suggested the existence of a tumor suppressor gene distal to BRCA1 (Porter et al., 1993; Porter et al., 1994). The maximum LOD scores obtained for D17S588 were of 5,44 in an Edinburgh study of 15 families (Cohen et al., 1993) and 21,68 in an analysis of 271 breast and breast-ovarian cancer families (Easton et al., 1993, Smith et al., 1993), indicating the importance of this locus in the pathology of cancer. The D17S588 marker lies inside the PPP1R9B gene.
Another study that investigated the correlation between p53 abnormalities and allelic loss of BRCA1, BRCA2 and adjacent loci in breast cancer found a strong correlation when using the D17S588 marker (Querzoli et al., 2001; Tseng et al., 1997). Again, PPP1R9B may be involved in the tumorigenic process by functioning, in association with a loss of p53 functionality, as a tumor suppressor (47,1% LOH) (Tseng et al., 1997).
Entity Learning and memory, regulation of blood pressure and cardiac function
Disease Learning and memory defects, problems in the regulation of blood pressure and cardiac function, tumors of different origin.

5. Bibliography

Loss of heterozygosity (LOH) at 17q and 14q in human lung cancers.
Abujiang P, Mori TJ, Takahashi T, Tanaka F, Kasyu I, Hitomi S, Hiai H.
Oncogene. 1998 Dec 10;17(23):3029-33.
PMID 9881705
Distinct roles for spinophilin and neurabin in dopamine-mediated plasticity.
Allen PB, Zachariou V, Svenningsson P, Lepore AC, Centonze D, Costa C, Rossi S, Bender G, Chen G, Feng J, Snyder GL, Bernardi G, Nestler EJ, Yan Z, Calabresi P, Greengard P.
Neuroscience. 2006 Jul 7;140(3):897-911.
PMID 16600521
Spinophilin stabilizes cell surface expression of alpha 2B-adrenergic receptors.
Brady AE, Wang Q, Colbran RJ, Allen PB, Greengard P, Limbird LE.
J Biol Chem. 2003 Aug 22;278(34):32405-12. Epub 2003 May 8.
PMID 12738775
Comparison of alterations of chromosome 17 in carcinoma of the ovary and of the breast.
Caduff RF, Svoboda-Newman SM, Ferguson AW, Frank TS.
Virchows Arch. 1999 Jun;434(6):517-22.
PMID 10394886
Spinophilin: a new tumor suppressor at 17q21.
Carnero A.
Curr Mol Med. 2012 Jun 1;12(5):528-35.
PMID 22515982
Multiple actions of spinophilin regulate mu opioid receptor function.
Charlton JJ, Allen PB, Psifogeorgou K, Chakravarty S, Gomes I, Neve RL, Devi LA, Greengard P, Nestler EJ, Zachariou V.
Neuron. 2008 Apr 24;58(2):238-47.
PMID 18439408
Linkage of a major breast cancer gene to chromosome 17q12-21: results from 15 Edinburgh families.
Cohen BB, Porter DE, Wallace MR, Carothers A, Steel CM.
Am J Hum Genet. 1993 Apr;52(4):723-9.
PMID 8460638
Genetic linkage analysis in familial breast and ovarian cancer: results from 214 families. The Breast Cancer Linkage Consortium.
Easton DF, Bishop DT, Ford D, Crockford GP.
Am J Hum Genet. 1993 Apr;52(4):678-701.
PMID 8460634
Phosphorylation of spinophilin modulates its interaction with actin filaments.
Hsieh-Wilson LC, Benfenati F, Snyder GL, Allen PB, Nairn AC, Greengard P.
J Biol Chem. 2003 Jan 10;278(2):1186-94. Epub 2002 Nov 1.
PMID 12417592
Protein phosphatase 1 regulators in DNA damage signaling.
Kuntziger T, Landsverk HB, Collas P, Syljuasen RG.
Cell Cycle. 2011 May 1;10(9):1356-62. Epub 2011 May 1. (REVIEW)
PMID 21451260
Molecular abnormalities associated with secretory carcinomas of the breast.
Maitra A, Tavassoli FA, Albores-Saavedra J, Behrens C, Wistuba II, Bryant D, Weinberg AG, Rogers BB, Saboorian MH, Gazdar AF.
Hum Pathol. 1999 Dec;30(12):1435-40.
PMID 10667421
PPP1R9B (Neurabin 2): involvement and dynamics in the NK immunological synapse.
Meng X, Kanwar N, Du Q, Goping IS, Bleackley RC, Wilkins JA.
Eur J Immunol. 2009 Feb;39(2):552-60.
PMID 19130477
Down-regulation of spinophilin in lung tumours contributes to tumourigenesis.
Molina-Pinelo S, Ferrer I, Blanco-Aparicio C, Peregrino S, Pastor MD, Alvarez-Vega J, Suarez R, Verge M, Marin JJ, Hernandez-Losa J, Ramon y Cajal S, Paz-Ares L, Carnero A.
J Pathol. 2011 Sep;225(1):73-82. doi: 10.1002/path.2905. Epub 2011 May 19.
PMID 21598252
Subcellular distribution of spinophilin immunolabeling in primate prefrontal cortex: localization to and within dendritic spines.
Muly EC, Smith Y, Allen P, Greengard P.
J Comp Neurol. 2004 Feb 2;469(2):185-97.
PMID 14694533
Cellular and subcellular distribution of spinophilin, a PP1 regulatory protein that bundles F-actin in dendritic spines.
Ouimet CC, Katona I, Allen P, Freund TF, Greengard P.
J Comp Neurol. 2004 Nov 22;479(4):374-88.
PMID 15514983
Spinophilin is required for normal morphology, Ca(2+) homeostasis and contraction but dispensable for ?-adrenergic stimulation of adult cardiomyocytes.
Petzhold D, da Costa-Goncalves AC, Gross V, Morano I.
J Muscle Res Cell Motil. 2011 Dec;32(4-5):243-8. Epub 2011 Sep 16.
PMID 21922228
Breast cancer incidence, penetrance and survival in probable carriers of BRCA1 gene mutation in families linked to BRCA1 on chromosome 17q12-21.
Porter DE, Cohen BB, Wallace MR, Smyth E, Chetty U, Dixon JM, Steel CM, Carter DC.
Br J Surg. 1994 Oct;81(10):1512-5.
PMID 7820489
Genetic linkage analysis applied to unaffected women from families with breast cancer can discriminate high- from low-risk individuals.
Porter DE, Steel CM, Cohen BB, Wallace MR, Carothers A, Chetty U, Carter DC.
Br J Surg. 1993 Nov;80(11):1381-5.
PMID 8252342
Biophenotypes and survival of BRCA1 and TP53 deleted breast cancer in young women.
Querzoli P, Albonico G, di Iasio MG, Ferretti S, Rinaldi R, Cariello A, Pedriali M, Matteuzzi M, Maestri I, Nenci I.
Breast Cancer Res Treat. 2001 Mar;66(2):135-42.
PMID 11437099
Spinophilin: from partners to functions.
Sarrouilhe D, di Tommaso A, Metaye T, Ladeveze V.
Biochimie. 2006 Sep;88(9):1099-113. Epub 2006 May 17. (REVIEW)
PMID 16737766
Scaffold proteins and immune-cell signalling.
Shaw AS, Filbert EL.
Nat Rev Immunol. 2009 Jan;9(1):47-56. (REVIEW)
PMID 19104498
Genetic heterogeneity and localization of a familial breast-ovarian cancer gene on chromosome 17q12-q21.
Smith SA, Easton DF, Ford D, Peto J, Anderson K, Averill D, Stratton M, Ponder M, Pye C, Ponder BA.
Am J Hum Genet. 1993 Apr;52(4):767-76.
PMID 8460642
Impaired conditioned taste aversion learning in spinophilin knockout mice.
Stafstrom-Davis CA, Ouimet CC, Feng J, Allen PB, Greengard P, Houpt TA.
Learn Mem. 2001 Sep-Oct;8(5):272-8.
PMID 11584074
Allelic loss at BRCA1, BRCA2, and adjacent loci in relation to TP53 abnormality in breast cancer.
Tseng SL, Yu IC, Yue CT, Chang SF, Chang TM, Wu CW, Shen CY.
Genes Chromosomes Cancer. 1997 Dec;20(4):377-82.
PMID 9408754
The human tumor suppressor arf interacts with spinophilin/neurabin II, a type 1 protein-phosphatase-binding protein.
Vivo M, Calogero RA, Sansone F, Calabro V, Parisi T, Borrelli L, Saviozzi S, La Mantia G.
J Biol Chem. 2001 Apr 27;276(17):14161-9. Epub 2001 Jan 30.
PMID 11278317
Spinophilin blocks arrestin actions in vitro and in vivo at G protein-coupled receptors.
Wang Q, Zhao J, Brady AE, Feng J, Allen PB, Lefkowitz RJ, Greengard P, Limbird LE.
Science. 2004 Jun 25;304(5679):1940-4.
PMID 15218143
Protein phosphatase 1 modulation of neostriatal AMPA channels: regulation by DARPP-32 and spinophilin.
Yan Z, Hsieh-Wilson L, Feng J, Tomizawa K, Allen PB, Fienberg AA, Nairn AC, Greengard P.
Nat Neurosci. 1999 Jan;2(1):13-7.
PMID 10195174
Role of the multidomain protein spinophilin in blood pressure and cardiac function regulation.
da Costa-Goncalves AC, Tank J, Plehm R, Diedrich A, Todiras M, Gollasch M, Heuser A, Wellner M, Bader M, Jordan J, Luft FC, Gross V.
Hypertension. 2008 Oct;52(4):702-7. Epub 2008 Aug 18.
PMID 18711009

6. Citation

This paper should be referenced as such :
Carnero, A
PPP1R9B (protein phosphatase 1, regulatory subunit 9B)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(8):545-548.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://atlasgeneticsoncology.usal.es/classic/Genes/PPP1R9BID51558ch17q21.html

7. Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]

  t(17;17)(q21;q21) SGCA/PPP1R9B

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(17;17)(q21;q23) PPP1R9B/CLTC

8. External links

HGNC (Hugo)PPP1R9B   9298
Entrez_Gene (NCBI)PPP1R9B  84687  protein phosphatase 1 regulatory subunit 9B
AliasesPPP1R6; PPP1R9; SPINO; Spn
GeneCards (Weizmann)PPP1R9B
Ensembl hg19 (Hinxton)ENSG00000108819 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000108819 [Gene_View] &nbspENSG00000108819 [Sequence]  chr17:50133735-50150517 [Contig_View]  PPP1R9B [Vega]
ICGC DataPortalENSG00000108819
TCGA cBioPortalPPP1R9B
Genatlas (Paris)PPP1R9B
SOURCE (Princeton)PPP1R9B
Genetics Home Reference (NIH)PPP1R9B
Genomic and cartography
GoldenPath hg38 (UCSC)PPP1R9B  -     chr17:50133735-50150517 -  17q21.33   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)PPP1R9B  -     17q21.33   [Description]    (hg19-Feb_2009)
EnsemblPPP1R9B - 17q21.33 [CytoView hg19]  PPP1R9B - 17q21.33 [CytoView hg38]
Mapping of homologs : NCBIPPP1R9B [Mapview hg19]  PPP1R9B [Mapview hg38]
Gene and transcription
Genbank (Entrez)AI056581 AJ401189 AK054907 AL157449 AL713642
RefSeq transcript (Entrez)NM_032595
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)PPP1R9B
Cluster EST : UnigeneHs.514323 [ NCBI ]
CGAP (NCI)Hs.514323
Alternative Splicing GalleryENSG00000108819
Gene ExpressionPPP1R9B [ NCBI-GEO ]   PPP1R9B [ EBI - ARRAY_EXPRESS ]   PPP1R9B [ SEEK ]   PPP1R9B [ MEM ]
Gene Expression Viewer (FireBrowse)PPP1R9B [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets] &nbsp [Normal Tissue Atlas] &nbsp[carcinoma Classsification] &nbsp[NCI60]
GenevestigatorExpression in : [tissues] &nbsp[cell-lines] &nbsp[cancer] &nbsp[perturbations] &nbsp
BioGPS (Tissue expression)84687
GTEX Portal (Tissue expression)PPP1R9B
Human Protein AtlasENSG00000108819-PPP1R9B [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ96SB3   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ96SB3  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ96SB3
Splice isoforms : SwissVarQ96SB3
Domaine pattern : Prosite (Expaxy)PDZ (PS50106)   
Domains : Interpro (EBI)NEB2    PDZ    PDZ_sf   
Domain families : Pfam (Sanger)PDZ (PF00595)   
Domain families : Pfam (NCBI)pfam00595   
Domain families : Smart (EMBL)PDZ (SM00228)  
Conserved Domain (NCBI)PPP1R9B
DMDM Disease mutations84687
Blocks (Seattle)PPP1R9B
Human Protein Atlas [tissue]ENSG00000108819-PPP1R9B [tissue]
Peptide AtlasQ96SB3
IPIIPI00816035   IPI00045550   IPI00921290   
Protein Interaction databases
IntAct (EBI)Q96SB3
Ontologies - Pathways
Ontology : AmiGOprotein phosphatase type 1 complex  regulation of cell growth by extracellular stimulus  protein phosphatase inhibitor activity  protein binding  nucleoplasm  cytoplasm  cytoplasm  plasma membrane  adherens junction  actin filament organization  cell cycle arrest  regulation of exit from mitosis  protein phosphatase 1 binding  RNA splicing  postsynaptic density  actin cytoskeleton  cell migration  calcium-mediated signaling  lamellipodium  filopodium  negative regulation of cell growth  dendrite  neuron projection development  negative regulation of phosphoprotein phosphatase activity  ruffle membrane  regulation of cell proliferation  dendritic spine  filopodium assembly  modulation of chemical synaptic transmission  actin filament binding  cellular response to morphine  regulation of opioid receptor signaling pathway  
Ontology : EGO-EBIprotein phosphatase type 1 complex  regulation of cell growth by extracellular stimulus  protein phosphatase inhibitor activity  protein binding  nucleoplasm  cytoplasm  cytoplasm  plasma membrane  adherens junction  actin filament organization  cell cycle arrest  regulation of exit from mitosis  protein phosphatase 1 binding  RNA splicing  postsynaptic density  actin cytoskeleton  cell migration  calcium-mediated signaling  lamellipodium  filopodium  negative regulation of cell growth  dendrite  neuron projection development  negative regulation of phosphoprotein phosphatase activity  ruffle membrane  regulation of cell proliferation  dendritic spine  filopodium assembly  modulation of chemical synaptic transmission  actin filament binding  cellular response to morphine  regulation of opioid receptor signaling pathway  
NDEx NetworkPPP1R9B
Atlas of Cancer Signalling NetworkPPP1R9B
Wikipedia pathwaysPPP1R9B
Orthology - Evolution
GeneTree (enSembl)ENSG00000108819
Phylogenetic Trees/Animal Genes : TreeFamPPP1R9B
Homologs : HomoloGenePPP1R9B
Homology/Alignments : Family Browser (UCSC)PPP1R9B
Gene fusions - Rearrangements
Fusion : MitelmanSGCA/PPP1R9B [17q21.33/17q21.33] &nbsp[t(17;17)(q21;q21)]  
Fusion : QuiverPPP1R9B
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPPP1R9B [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PPP1R9B
Exome Variant ServerPPP1R9B
ExAC (Exome Aggregation Consortium)ENSG00000108819
GNOMAD BrowserENSG00000108819
Varsome BrowserPPP1R9B
Genetic variants : HAPMAP84687
Genomic Variants (DGV)PPP1R9B [DGVbeta]
DECIPHERPPP1R9B [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisPPP1R9B 
ICGC Data PortalPPP1R9B 
TCGA Data PortalPPP1R9B 
Broad Tumor PortalPPP1R9B
OASIS PortalPPP1R9B [ Somatic mutations - Copy number]
Mutations and Diseases : HGMDPPP1R9B
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch PPP1R9B
DgiDB (Drug Gene Interaction Database)PPP1R9B
DoCM (Curated mutations)PPP1R9B (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PPP1R9B (select a term)
NCG5 (London)PPP1R9B
Cancer3DPPP1R9B(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry PPP1R9B
NextProtQ96SB3 [Medical]
Target ValidationPPP1R9B
Huge Navigator PPP1R9B [HugePedia]
snp3D : Map Gene to Disease84687
BioCentury BCIQPPP1R9B
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD84687
Chemical/Pharm GKB GenePA33662
Clinical trialPPP1R9B
canSAR (ICR)PPP1R9B (select the gene name)
DataMed IndexPPP1R9B
PubMed68 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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