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PTPN9 (protein tyrosine phosphatase, non-receptor type 9)

Written2016-11Barnabas Nyesiga and Anette Gjörloff Wingren
Biomedical science, Health and society, Malmö University, Malmö, Sweden;

Abstract Review on PTPN9, with data on DNA, on the protein encoded, and where the gene is implicated.

Keywords PTPN9; Endocytosis;

(Note : for Links provided by Atlas : click)


Alias (NCBI)Protein Tyrosine Phosphatase, Non-Receptor Type 9
Protein-Tyrosine Phosphatase MEG2
Tyrosine-Protein Phosphatase Non-Receptor Type 9
HGNC Alias symbMEG2
LocusID (NCBI) 5780
Atlas_Id 41922
Location 15q24.2  [Link to chromosome band 15q24]
Location_base_pair Starts at 75463251 and ends at 75579315 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping PTPN9.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)
PTPN9 (15q24.2)::AGBL1 (15q25.3)SIN3A (15q24.2)::PTPN9 (15q24.2)


Note PTPN9 was originally cloned by screening libraries of the MEG-01 megakaryocyte leukemia cell line and of human umbilical vein endothelial cells (Gu 1992).
Description The PTPN9 gene was mapped to chromosome 15q24.2 based on an alignment of the PTPN9 sequence (GenBank BC010863) with the genomic sequence (GRCh37).
Transcription MEG2 mRNA detected in 12 cell lines gave an indication that the protein tyrosine phosphatase (PTP) is widely expressed. A 4-kb RNA as analysed by Northern blot analysis was found in a variety of cell lines, indicating widespread expression of the gene (Gu 1992).


Note NOTE PTPN9 has a conserved PTP catalytic domain, and an NH2-terminal lipid-binding domain homologous to Sec14p, a yeast protein with phosphatidylinositol transferase activity, which is unique among PTPs (Gu 1992). The N-terminal 254 amino acids are about 28% identical to cellular retinaldehyde binding protein-1 (RLBP1; 180090) and 24% identical to the yeast protein SEC14p. The former is a carrier protein for 11-cis-retinaldehyde or 11-cis-retinol found in the retina and pineal gland, and the latter is a phosphatidylinositol transfer protein required for protein secretion from the Golgi apparatus. The PTPN9 cDNA encodes a 593-amino acid protein that has no apparent signal or transmembrane domains but does include a C-terminal region with a catalytic domain that shows 30-40% identity with other PTPs (
  Figure 1. Schematic diagram of recombinant PTPN9 protein (Adapted from Zhao et al. 2003).The open and solid bars indicate SEC14 lipid-binding domain and PTP catalytic domain, respectively.
Description PTPN9 is a 68-kDa, class I, cysteine-based, non-receptor PTP is widely expressed in many cell types including the brain and leukocytes (Gu 1992, Saito 2007). In these cells, most of the PTPN9 is located on the cytoplasmic face of secretory vesicles (Gjörloff-Wingren 2000, Wang 2002, Kruger 2002 and Huynh 2004). On the cytoplasmic face of the enclosing membrane of secretory vesicles, PTPN9 regulates vesicle size by promoting homotypic vesicle fusion through dephosphorylating NSF (N-ethylmaleimide-sensitive factor), a key regulator of vesicle fusion (Saito 2007). PTPN9 structural uniqueness among mammalian PTPs lies in the fact that it contains a domain in its N terminus with homology to yeast Sec14p, a phosphatidylinositol-binding protein (Sha 1998). This Sec14p homology (SEC14) domain of PTPN9 (Fig 1) is known to bind phosphoinositides (Kruger 2002, Huynh 2003, Krugmann 2002), a process that leads into enzymatic activation of the phosphatase domain (Kruger 2002, Huynh 2003). Using a series of deletion mutants, Saito et al identified the N-terminal SEC14 domain of PTPN9, residues 1-261, as the region containing the secretory vesicle targeting signal (Saito 2007). The SEC14 domain, alone or attached to a heterologous protein, was localized to intracellular vesicle membranes. In addition, two proteins, mannose 6-phosphate receptor-interacting protein PLIN3 (TIP47) and ARFIP2 Arfaptin2 altered PTPN9 localization when overexpressed, and elimination of TIP47 resulted in loss of PTPN9 function. It has been shown that the truncated form of the N-terminal SEC14 domain of PTPN9 has a significantly higher activity than the full-length enzyme (Qi 2002, Kruger 2002). By using lipid-membrane overlay and liposome binding assays, a specific binding of PTPN9 to phosphatidylserine was demonstrated (Zhao 2003). The binding was found to be mediated by the SEC14 domain. In intact cells, the SEC14 domain was found to play a prominent role in the localization of PTPN9 to the perinuclear region. Moreover, PTPN9 may play an important role through specific binding of phosphatidylserine, in regulating the signaling processes associated with phagocytosis of apoptotic cells (Zhao 2003).
Expression The enzyme is expressed in many cell types (Gu 1992, Saito 2007), including at low levels in Jurkat T cells (Gjörloff-Wingren 2000), mast cells and lymphocytes (Wang 2002, Wang 2005).
Localisation Reports have shown PTPN9 residence on internal membranes, including secretory vesicles and granules in neutrophils and lymphocytes where it regulates secretory vesicle size and fusion (Gjörloff-Wingren 2000, Wang 2002, Huynh 2003, Wang 2005). It is possible that once engulfed by phagocytes, a high level of phosphatidylserine in the outer membrane of apoptotic cells may alter the distribution of PTPN9 in phagocytes (Zhao 2003). It has been suggested that the physiological function of PTPN9 may be to regulate formation of secretory vesicles of a defined and cell type-specific size (Wang 2002). PTPN9 expression is higher in mast cells (granule size 400-600 nm) than in lymphocytes (granule size 200-300 nm) (Wang 2002).
Function It was proposed that PTPN9 promotes homotypic fusion of immature secretory vesicles, which is a major step in the formation of these vesicles from post-Golgi transport vesicles containing cargo destined for secretion (Wang 2002, Huynh 2004, Huynh 2003, Wang 2005, Mustelin 2004). Additionally, PTPN9 may represent a novel connection between dephosphorylation of tyrosine and the regulation of secretory vesicles in hematopoietic cells (Wang 2002). Moreover, the possibility of PTPN9 expression in controlling the extent of the secretory apparatus of hematopoietic cells was proposed. Huyhn et al showed that PTPN9 regulates homotypic fusion of immature secretory vesicles by dephosphorylating the key regulator of vesicle fusion, N-ethylmaleimide-sensitive factor (NSF) (Huyhn 2004). PTPN9 can also regulate embryonic development (Wang 2005) and expansion of erythroid cells (Xu 2003). Studies have further demonstrated that PTPN9 controls insulin production, beta cell growth or insulin signaling by reducing insulin receptor (INSR) dephosphorylation in type II diabetes (Cho 2006, Chen 2010). Other studies have shown that PTPN9 promotes dephosphorylation of epidermal growth factor receptor (EGFR) and the receptor tyrosine protein kinase ERBB2, thereby impairing the activation of signal transducer and activator of transcription 3 (STAT3) (Yuan 2010) and STAT5 (Yuan 2010, Furth 2011) in breast cancer cells. From their observations, it was suggested that PTPN9-mediated modulation of secretory vesicle genesis and function plays an essential role in neural tube, vascular, and bone development as well as activation may participate in the transfer of hydrophobic ligands or may be involved in Golgi-related functions (Gu 1992). PTPN9 appears to regulate a balance by promoting fusion (anterograde transport) and reducing condensation (retrograde transport), thus increasing the size of secretory vesicles (Saito 2007). In addition, it was recently shown that the transport of neurotrophin receptor TRKA ( NTRK1) to the cell surface requires PTPN9 activity (Zhang 2016). Trk A is a novel substrate of PTPN9 and is dephosphorylated at both the kinase activation domain (Tyr674/675) and the signaling effector binding site (Tyr490). The studies were performed in neurite outgrowth and cortical neurons (Zhang 2016).

Implicated in

Entity Breast cancer
Note ErbB family of the receptor protein-tyrosine kinase plays an important role in the progression of human cancers including breast cancer. Among the 43 human protein-tyrosine phosphatases analysed, Yuan 2010 discovered the knockdown of PTPN9 to significantly increase ERBB2 tyrosine phosphorylation in the SKBR3 breast cancer cell line. Additionally, knockdown of PTPN9 expression enhances tyrosine phosphorylation of the ErbB1/EGFR in the MDA-MB-231 breast cancer cell line. Their data suggested PTPN9 to be a negative regulator of breast cancer cells through targeting ErbB2 and EGFR and inhibiting STAT activation (Yuan 2010).
Entity Hepatocellular carcinoma
Note PTPN9 expression was down-regulated in human hepatocellular carcinoma (HCC) tumor tissues, associate with worsened overall survival in HCC patients (Hu 2016). Depletion ofPTPN9 inhibits the apoptosis and promotes the proliferation of HCC cells.
Entity Diabetes
Note PTPN9 have been identified as a modulator of insulin-dependent FOXO1 subcellular localization (Cho 2006). Ectopic expression of PTPN9 in cells to suppress insulin-induced phosphorylation of the insulin receptor, while RNAi-mediated reduction of PTPN9 transcript levels enhanced insulin action. Their findings implicated PTPN9 as a mediator of blood glucose homeostasis through antagonism of insulin signaling, and proposed modulation of PTPN9 activity to be an adequate strategy in type 2 diabetes treatment. Indeed, treatment with PTPN9 inhibitors can lead to enhanced insulin action both in vitro and in vivo (Zhang 2012).
Entity Hematopoiesis
Note Xu et al identified PTPN9 to be contained in erythroid colony-forming cells (ECFCs) from polycythemia vera (PV), a human clonal myeloproliferative disorder (Xu 2003). Increased activity of PTPN9 in PV cells to be attributed to its elevated distribution in the membrane fraction. Additionally, the findings showed that PTPN9 plays a major role in the development of erythroid cells.
Entity Immunodeficiency
Note PTPN9-/- mice were reported to be immunodeficient as they displayed severe developmental malformations, such as defective skull formation and intracranial bleeding (Wang 2005). The mice remained small and the majority of them died before birth or within the first neonatal days. Furthermore, they detected defective platelet activation and very little interleukin-2 secretion in these mice. They attributed all these abnormalities to defective PTPN9 secretion.


[Research progress of several protein tyrosine phosphatases in diabetes]
Chen M, Sun JP, Liu J, Yu X
Sheng Li Xue Bao 2010 Apr 25;62(2):179-89
PMID 20401454
Identification of the tyrosine phosphatase PTP-MEG2 as an antagonist of hepatic insulin signaling
Cho CY, Koo SH, Wang Y, Callaway S, Hedrick S, Mak PA, Orth AP, Peters EC, Saez E, Montminy M, Schultz PG, Chanda SK
Cell Metab 2006 May;3(5):367-78
PMID 16679294
Signal transducer and activator of transcription 5 as a key signaling pathway in normal mammary gland developmental biology and breast cancer
Furth PA, Nakles RE, Millman S, Diaz-Cruz ES, Cabrera MC
Breast Cancer Res 2011 Oct 12;13(5):220
PMID 22018398
Subcellular localization of intracellular protein tyrosine phosphatases in T cells
Gjörloff-Wingren A, Saxena M, Han S, Wang X, Alonso A, Renedo M, Oh P, Williams S, Schnitzer J, Mustelin T
Eur J Immunol 2000 Aug;30(8):2412-21
PMID 10940933
Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14p
Gu M, Warshawsky I, Majerus PW
Proc Natl Acad Sci U S A 1992 Apr 1;89(7):2980-4
PMID 1557404
Downregulated Expression of PTPN9 Contributes to Human Hepatocellular Carcinoma Growth and Progression
Hu B, Yan X, Liu F, Zhu C, Zhou H, Chen Y, Liu J, Gu X, Ni R, Zhang T
Pathol Oncol Res 2016 Jul;22(3):555-65
PMID 26715439
Control of vesicle fusion by a tyrosine phosphatase
Huynh H, Bottini N, Williams S, Cherepanov V, Musumeci L, Saito K, Bruckner S, Vachon E, Wang X, Kruger J, Chow CW, Pellecchia M, Monosov E, Greer PA, Trimble W, Downey GP, Mustelin T
Nat Cell Biol 2004 Sep;6(9):831-9
PMID 15322554
Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells
Huynh H, Wang X, Li W, Bottini N, Williams S, Nika K, Ishihara H, Godzik A, Mustelin T
J Immunol 2003 Dec 15;171(12):6661-71
PMID 14662869
Protein-tyrosine phosphatase MEG2 is expressed by human neutrophils
Kruger JM, Fukushima T, Cherepanov V, Borregaard N, Loeve C, Shek C, Sharma K, Tanswell AK, Chow CW, Downey GP
Localization to the phagosome and activation by polyphosphoinositides J Biol Chem
PMID 11711529
Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices
Krugmann S, Anderson KE, Ridley SH, Risso N, McGregor A, Coadwell J, Davidson K, Eguinoa A, Ellson CD, Lipp P, Manifava M, Ktistakis N, Painter G, Thuring JW, Cooper MA, Lim ZY, Holmes AB, Dove SK, Michell RH, Grewal A, Nazarian A, Erdjument-Bromage H, Tempst P, Stephens LR, Hawkins PT
Mol Cell 2002 Jan;9(1):95-108
PMID 11804589
Protein tyrosine phosphatases in T cell physiology
Mustelin T, Alonso A, Bottini N, Huynh H, Rahmouni S, Nika K, Louis-dit-Sully C, Tautz L, Togo SH, Bruckner S, Mena-Duran AV, al-Khouri AM
Mol Immunol 2004 Jul;41(6-7):687-700
PMID 15220004
Purification and characterization of protein tyrosine phosphatase PTP-MEG2
Qi Y, Zhao R, Cao H, Sui X, Krantz SB, Zhao ZJ
J Cell Biochem 2002;86(1):79-89
PMID 12112018
Association of protein-tyrosine phosphatase MEG2 via its Sec14p homology domain with vesicle-trafficking proteins
Saito K, Williams S, Bulankina A, Höning S, Mustelin T
J Biol Chem 2007 May 18;282(20):15170-8
PMID 17387180
Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein
Sha B, Phillips SE, Bankaitis VA, Luo M
Nature 1998 Jan 29;391(6666):506-10
PMID 9461221
Enlargement of secretory vesicles by protein tyrosine phosphatase PTP-MEG2 in rat basophilic leukemia mast cells and Jurkat T cells
Wang X, Huynh H, Gjörloff-Wingren A, Monosov E, Stridsberg M, Fukuda M, Mustelin T
J Immunol 2002 May 1;168(9):4612-9
PMID 11971009
Tyrosine phosphatase MEG2 modulates murine development and platelet and lymphocyte activation through secretory vesicle function
Wang Y, Vachon E, Zhang J, Cherepanov V, Kruger J, Li J, Saito K, Shannon P, Bottini N, Huynh H, Ni H, Yang H, McKerlie C, Quaggin S, Zhao ZJ, Marsden PA, Mustelin T, Siminovitch KA, Downey GP
J Exp Med 2005 Dec 5;202(11):1587-97
PMID 16330817
PTP-MEG2 is activated in polycythemia vera erythroid progenitor cells and is required for growth and expansion of erythroid cells
Xu MJ, Sui X, Zhao R, Dai C, Krantz SB, Zhao ZJ
Blood 2003 Dec 15;102(13):4354-60
PMID 12920026
Protein-tyrosine phosphatase PTPN9 negatively regulates ErbB2 and epidermal growth factor receptor signaling in breast cancer cells
Yuan T, Wang Y, Zhao ZJ, Gu H
J Biol Chem 2010 May 14;285(20):14861-70
PMID 20335174
The Protein Tyrosine Phosphatase MEG2 Regulates the Transport and Signal Transduction of Tropomyosin Receptor Kinase A
Zhang D, Marlin MC, Liang Z, Ahmad M, Ashpole NM, Sonntag WE, Zhao ZJ, Li G
J Biol Chem 2016 Nov 11;291(46):23895-23905
PMID 27655914
A highly selective and potent PTP-MEG2 inhibitor with therapeutic potential for type 2 diabetes
Zhang S, Liu S, Tao R, Wei D, Chen L, Shen W, Yu ZH, Wang L, Jones DR, Dong XC, Zhang ZY
J Am Chem Soc 2012 Oct 31;134(43):18116-24
PMID 23075115
Specific interaction of protein tyrosine phosphatase-MEG2 with phosphatidylserine
Zhao R, Fu X, Li Q, Krantz SB, Zhao ZJ
J Biol Chem 2003 Jun 20;278(25):22609-14
PMID 12702726


This paper should be referenced as such :
Barnabas Nyesiga, Anette Gjörloff Wingren
PTPN9 (protein tyrosine phosphatase, non-receptor type 9)
Atlas Genet Cytogenet Oncol Haematol. 2017;21(8):288-291.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)PTPN9   9661
Entrez_Gene (NCBI)PTPN9    protein tyrosine phosphatase non-receptor type 9
AliasesMEG2; PTPMEG2
GeneCards (Weizmann)PTPN9
Ensembl hg19 (Hinxton)ENSG00000169410 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000169410 [Gene_View]  ENSG00000169410 [Sequence]  chr15:75463251-75579315 [Contig_View]  PTPN9 [Vega]
ICGC DataPortalENSG00000169410
TCGA cBioPortalPTPN9
Genatlas (Paris)PTPN9
SOURCE (Princeton)PTPN9
Genetics Home Reference (NIH)PTPN9
Genomic and cartography
GoldenPath hg38 (UCSC)PTPN9  -     chr15:75463251-75579315 -  15q24.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)PTPN9  -     15q24.2   [Description]    (hg19-Feb_2009)
GoldenPathPTPN9 - 15q24.2 [CytoView hg19]  PTPN9 - 15q24.2 [CytoView hg38]
Genome Data Viewer NCBIPTPN9 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)BC010863 BC071574 BT007405 M83738
RefSeq transcript (Entrez)NM_002833
Consensus coding sequences : CCDS (NCBI)PTPN9
Gene ExpressionPTPN9 [ NCBI-GEO ]   PTPN9 [ EBI - ARRAY_EXPRESS ]   PTPN9 [ SEEK ]   PTPN9 [ MEM ]
Gene Expression Viewer (FireBrowse)PTPN9 [ Firebrowse - Broad ]
GenevisibleExpression of PTPN9 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5780
GTEX Portal (Tissue expression)PTPN9
Human Protein AtlasENSG00000169410-PTPN9 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP43378   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP43378  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP43378
Catalytic activity : Enzyme3.1.3.48 [ Enzyme-Expasy ] [ IntEnz-EBI ] [ BRENDA ] [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)CRAL_TRIO (PS50191)    TYR_PHOSPHATASE_1 (PS00383)    TYR_PHOSPHATASE_2 (PS50056)    TYR_PHOSPHATASE_PTP (PS50055)   
Domains : Interpro (EBI)CRAL-TRIO_dom    CRAL-TRIO_dom_sf    CRAL/TRIO_N_dom    CRAL/TRIO_N_dom_sf    Prot-tyrosine_phosphatase-like    PTPase_domain    Tyr_Pase_AS    Tyr_Pase_cat    TYR_PHOSPHATASE_dom   
Domain families : Pfam (Sanger)CRAL_TRIO (PF00650)    Y_phosphatase (PF00102)   
Domain families : Pfam (NCBI)pfam00650    pfam00102   
Domain families : Smart (EMBL)CRAL_TRIO_N (SM01100)  PTPc (SM00194)  PTPc_motif (SM00404)  SEC14 (SM00516)  
Conserved Domain (NCBI)PTPN9
PDB (RSDB)2PA5    4GE2    4GE5    4GE6    4ICZ    6KZQ    6L03   
PDB Europe2PA5    4GE2    4GE5    4GE6    4ICZ    6KZQ    6L03   
PDB (PDBSum)2PA5    4GE2    4GE5    4GE6    4ICZ    6KZQ    6L03   
PDB (IMB)2PA5    4GE2    4GE5    4GE6    4ICZ    6KZQ    6L03   
Structural Biology KnowledgeBase2PA5    4GE2    4GE5    4GE6    4ICZ    6KZQ    6L03   
SCOP (Structural Classification of Proteins)2PA5    4GE2    4GE5    4GE6    4ICZ    6KZQ    6L03   
CATH (Classification of proteins structures)2PA5    4GE2    4GE5    4GE6    4ICZ    6KZQ    6L03   
AlphaFold pdb e-kbP43378   
Human Protein Atlas [tissue]ENSG00000169410-PTPN9 [tissue]
Protein Interaction databases
IntAct (EBI)P43378
Ontologies - Pathways
Ontology : AmiGOprotein tyrosine phosphatase activity  protein tyrosine phosphatase activity  non-membrane spanning protein tyrosine phosphatase activity  protein binding  nucleoplasm  cytoplasm  protein dephosphorylation  negative regulation of neuron projection development  peptidyl-tyrosine dephosphorylation  neuron projection terminus  cellular response to cytokine stimulus  positive regulation of protein localization to plasma membrane  
Ontology : EGO-EBIprotein tyrosine phosphatase activity  protein tyrosine phosphatase activity  non-membrane spanning protein tyrosine phosphatase activity  protein binding  nucleoplasm  cytoplasm  protein dephosphorylation  negative regulation of neuron projection development  peptidyl-tyrosine dephosphorylation  neuron projection terminus  cellular response to cytokine stimulus  positive regulation of protein localization to plasma membrane  
REACTOMEP43378 [protein]
REACTOME PathwaysR-HSA-9008059 [pathway]   
NDEx NetworkPTPN9
Atlas of Cancer Signalling NetworkPTPN9
Wikipedia pathwaysPTPN9
Orthology - Evolution
GeneTree (enSembl)ENSG00000169410
Phylogenetic Trees/Animal Genes : TreeFamPTPN9
Homologs : HomoloGenePTPN9
Homology/Alignments : Family Browser (UCSC)PTPN9
Gene fusions - Rearrangements
Fusion : MitelmanPTPN9::AGBL1 [15q24.2/15q25.3]  
Fusion : MitelmanSIN3A::PTPN9 [15q24.2/15q24.2]  
Fusion : QuiverPTPN9
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPTPN9 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PTPN9
Exome Variant ServerPTPN9
GNOMAD BrowserENSG00000169410
Varsome BrowserPTPN9
ACMGPTPN9 variants
Genomic Variants (DGV)PTPN9 [DGVbeta]
DECIPHERPTPN9 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisPTPN9 
ICGC Data PortalPTPN9 
TCGA Data PortalPTPN9 
Broad Tumor PortalPTPN9
OASIS PortalPTPN9 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPTPN9  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DPTPN9
Mutations and Diseases : HGMDPTPN9
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)PTPN9
DoCM (Curated mutations)PTPN9
CIViC (Clinical Interpretations of Variants in Cancer)PTPN9
NCG (London)PTPN9
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry PTPN9
NextProtP43378 [Medical]
Target ValidationPTPN9
Huge Navigator PTPN9 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDPTPN9
Pharm GKB GenePA34005
Clinical trialPTPN9
DataMed IndexPTPN9
PubMed46 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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