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PTPRJ (protein tyrosine phosphatase, receptor type, J)

Written2011-03Francesca Sacco, Savatore Corallino, Luisa Castagnoli
Department of Biology, University of Rome Tor Vergata, via ricerca scientifica, 00133 Rome, Italy

(Note : for Links provided by Atlas : click)


Alias_symbol (synonym)DEP1
Other aliasR-PTP-ETA
LocusID (NCBI) 5795
Atlas_Id 41932
Location 11p11.2  [Link to chromosome band 11p11]
Location_base_pair Starts at 47980558 and ends at 48170842 bp from pter ( according to hg19-Feb_2009)  [Mapping PTPRJ.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)
PTPRJ (11p11.2) / C2CD2L (11q23.3)PTPRJ (11p11.2) / FCER1G (1q23.3)PTPRJ (11p11.2) / LPXN (11q12.1)
PTPRJ (11p11.2) / MED26 (19p13.11)PTPRJ (11p11.2) / PTPRJ (11p11.2)SOX6 (11p15.2) / PTPRJ (11p11.2)
Note This gene is a member of the Human CCDS set: CCDS44596, CCDS7945.


Description Gene ENSG00000149177 has 24 alternate exons.
Transcription Multiple transcript variants encoding different isoforms have been found for this gene. Three transcripts are described in Ensembl (ID: ENSG00000149177).
The first (ENST00000418331) represents the longer isoform and encodes a protein that consists of an extracellular fibronectin type 3 domain and a cytosolic catalytic domain. The second isoform (ENST00000440289) has multiple differences in the presence and absence of exons at its 3' end, compared to the first isoform. These differences produce a unique 3' UTR and the encoded protein is shorter and consists of the extracellular fibronectin type 3 domain without the cytosolic catalytic region. The third transcript (ENST00000278456) has the same length as the first, but it encodes a truncated protein, that consists of fibronectin type 3 domains. Only the first two isoforms are members of the human CCDS set and have been described in NCBI (IDs: NM_001098503.1, NM_001098503.1).
The cDNA encoding PTPRJ/DEP-1 was isolated from a HeLa cell library (Ostman et al., 1994). The expression level and the activity of DEP-1 increase with cell density. This increase occurs gradually with increasing cell contact and is initiated before saturation cell density is reached. These observations suggest that DEP-1 may contribute to the mechanism of contact inhibition of cell growth.


  DEP-1: location of SNPs and mutations reported in human cancer. DEP-1 sequence is according to UniProtKB/Swiss-Prot: PTPRJ_HUMAN, Q12913. FNIII: Fibronectin domain, TM: Trans-membrane, KIM: Kinase Interaction Motif, PTP: Protein Tyrosine Phosphatase.
Description DEP-1 corresponds to a single-pass, type I membrane receptor-type protein tyrosine phosphatase; it is a 200-250 kDa transmembrane molecule with a 35 residue signal peptide, 940 residue extracellular portion, 21 residues in helical transmembrane region and 341 aminoacids in the intracytoplasmic tail, with a single catalytic domain at the carbossi-terminus.
The protein N-terminus has nine fibronectin type III (FNIII) repeats, contains 34 potential N-linked glycosylation sites and it was found glycosylated in seven asparagine residues by mass spectrometry (Liu et al., 2005; Chen et al., 2009). DEP-1 can dimerize (binding site 972-996) through the transmembrane domain (Chin et al., 2005) but it is unclear whether it can exist as dimers, physiologically. Sedimentation velocity measurements show that DEP1, along with other single-domain receptor phosphatases (e.g., IA2, IA2beta, GLEPP1 and STEP) is monomeric in solution (Barr et al., 2009).
The regulation of receptor-like protein tyrosine phosphatases is generally poorly understood. Sorby et al. have identified MatrigelTM (a preparation of extracellular matrix proteins) as a source of DEP-1 ligand(s) and agonist(s) (Sorby et al., 2001).
Expression DEP-1 is expressed in several cell types, including endothelial, epithelial, and in all haematopoietic lineages. It was found to be present on many epithelial cell types with glandular and endocrine differentiation as well as on fibrocytes, melanocytes and Schwann cells (Autschbach et al., 1999). It is widely expressed on B and T cells, granulocytes, macrophages, certain dendritic cells as well as mature thymocytes and it was shown to negatively regulate T cell receptor and terminating its response to stimulation. DEP-1 is thought to play a role in the down regulation of T cell activation and signalling, by interfering with the phosphorylation of Phospholipase C Gamma 1 and Linker for Activation of T Cells (LAT) and by reducing TCR-induced transcription factor (nuclear factor of activated T cells) (Lin and Weiss, 2003; Lin et al., 2004; Zhu et al., 2008; Tangye et al., 1998; Baker et al., 2001). DEP-1 expression is regulated during T cell activation and is constitutive in autoimmune murine T cells. These expression data suggest that DEP-1 plays a regulatory role to control an immune response and the proposed model of action describes DEP-1 as excluded from the immunologic synapse (i.e., the site of APC and T cell contact) during early T cell-APC (Antigen Presenting Cell) interactions. After T cell-APC disengagement, DEP-1 is no longer excluded by the synapse and can access and dephosphorylate substrates to down-regulate prolongation of the response (Lin et al., 2004).
It is interesting to note that the expression patterns of DEP-1 are different between humans and mice, where the expression in the T cell lineage is more restricted (Lin et al., 2004). Recently, DEP-1 is indicated as the phosphatase that can compensate for the absence of CD45, the prototypical receptor-like PTP expressed on immune cells (Zhu et al., 2008).
Function DEP-1 is a member of the protein tyrosine phosphatase (PTP) family. Since its expression is increased with increasing cell density, it is strongly suggested that DEP-1 may contribute to the mechanism of contact inhibition of cell growth (Ostman et al., 1994). It seems to be involved in protein tyrosine kinase signaling, cell-cell signaling, vasculogenesis and heart development (Takahashi et al., 2003).

Implicated in

Entity Thyroid cancer
Note Allelic loss of this gene is involved in thyroid carcinogenesis: the loss of heterozygosity (LOH) of PTPRJ is detected in 11/76 (14,5%) thyroid tumors (adenomas and carcinomas). DEP-1 overexpression in a malignant rat thyroid cell line was reported to specifically induce dephosphorylation of the Src-inhibitory Y529 and thus to increase Src activity. In addition, there are data suggesting that PTPRJ polymorphisms can affect susceptibility to thyroid carcinomas: DEP-1 homozygous for the Gln276Pro, Arg326Gln and the Glu872Asp allele were more frequent in thyroid carcinoma patients than in healthy individuals. Moreover, PTPRJ LOH was more frequent in thyroid carcinomas of heterozygotes for Gln276Pro and Arg326Gln compared with homozygotes, suggesting that the presence of hemizygosity for these polymorphisms in the tumor facilitates tumor progression (Iuliano et al., 2004). It was recently reported that the homozygous genotype PTPRJ/DEP-1 for Glu872Asp is associated with an increased risk to develop papillary thyroid carcinoma (Iuliano et al., 2010).
DEP-1 can dephosphorylate the single-pass transmembrane tyrosine kinase receptor RET, impairing its signaling. Iervolino et al. show that Tyr1062 is critical for the binding of RET to DEP-1 and that DEP-1 can dephosphorylate the Tyr905 and Tyr1062 of the mutant RET bearing a germ-line Cys634Arg point mutation, responsible for the inheritance of multiple endocrine neoplasia types 2A (RET-MEN2A) and of the RET/PTC (papillary thyroid carcinoma) chimeric oncoprotein (Iervolino et al., 2006). The authors also show a DEP-1 dose dependent reduction of the transforming activity of RET-MEN2A. Furthermore, Iervolino et al. verified that the conformationally altered RET, bearing the mutation Met918Threo, responsible for MEN2B, does not bind or is dephosphorylated by DEP-1. This resistance to DEP-1 may account for the high oncogenic activity of the MEN2B RET alleles.
The rat protein tyrosine phosphatase eta, homologue of DEP-1, suppresses the neoplastic phenotype of retrovirally transformed thyroid cell, causing G1 growth arrest, by increasing the cyclin-dependent kinase inhibitor p27Kip1 protein level, through reduction of its proteasome-dependent degradation rate (Trapasso et al., 2000).
Entity Colon rectal cancer
Note DEP-1 is a candidate human homologue of the mouse colon cancer susceptibility locus SCC1.
Germline allele-specific epigenetic silencing of the gene PTPRJ, encoding DEP-1, is described in early-onset familial colorectal cancer, due to a 170-kb intragenic duplication affecting the 5' end of the phosphatase gene PTPRJ the tandem duplication in a head-to-tail orientation (Venkatachalam et al., 2010; Ruivenkamp et al., 2002; Ruivenkamp et al., 2003a; Ruivenkamp et al., 2003b). PTPRJ is frequently deleted in human colon, lung and breast carcinomas or it shows allelic imbalance in loss of heterozygosity (LOH) and missense mutations. LOH of PTPRJ occurs early in progressed colorectal adenoma. Ruivenkamp et al. (2002) identified 5 somatic missense mutations in the PTPRJ gene, in colon cancer. All are localized in the extracellular fibronectin domains, two, Arg214Cys and Arg326Gln, result in loss of a positive charge. Mita et al. show, in their association study, that the Arg326Gln SNP demonstrates a close association with colon rectal cancer risk (Mita et al., 2010).
Nutrients, which are considered to be chemoprotective with respect to colon cancer development, including butyrate, green tea and apple polyphenols, seem to elevate transcription of endogenous DEP-1 mRNA and expression of DEP-1 protein. Upregulation of DEP-1 expression with a consequent inhibition of cell growth and migration may present a mechanism of chemoprevention by nutrients (Balavenkatraman et al., 2006).
Entity Meningiomas
Note Suppressor of epithelial tumor.
LOH of the PTPRJ gene are observed in average 38% of human meningiomas of all grades (Petermann et al., 2010). Also, RNAi-mediated suppression of DEP-1, in DEP-1 positive meningioma cell lines (i.e., KT21, SF3061), causes enhanced motility and colony formation in semi-solid media (Petermann et al., 2010). It is therefore suggested that DEP-1 acts as a negative regulator of PDGF signaling and as a positive regulator of adhesion signalling, cooperating in inhibition of cell motility and tumor invasiveness and behaving as a positive regulator of paxillin tyrosine phosphorylation in epithelial cells. DEP-1 negatively affects PDGF stimulated activation of inositol trisphosphate formation, Erk1/Erk2, p21Ras, and Src. Activation of receptor-associated PI3K activity and of Akt/PKB are weakly attenuated at early time points of PDGF stimulation (Jandt et al., 2003). PDGFR and DEP-1 physically interact and there is a site-specific reduction in tyrosine phosphorylation of the PDGF b-receptor after in vivo and in vitro exposure to DEP-1. In fact, DEP-1 dephosphorylates the PDGFb-receptor P-Tyr751 and P-Tyr1009/1021, which are required for activation of PI3-K and PLCgamma, respectively, while the PDGFR regulatory P-Tyr857 is less affected (Kovalenko et al., 2000). Moreover, DEP-1 interacts with and dephosphorylates the p85 subunit of PI3K, bound to PDGFR (Tsuboi et al., 2008).
Entity Various cancers
Note EGFR and DEP-1
EGFR and DEP-1 physically associate, and EGFR phosphorylates a substrate-trapping mutant of DEP-1. Sacco et al. suggest that DEP-1 could act on EGFR phospho-Tyr998 (Sacco et al., 2009). Tarcic et al. suggest a mechanism by which DEP-1 affects EGFR trafficking and signaling. They show that DEP-1 dephosphorylates EGFR at the cell surface and affects the major phosphorylation site on CBL (at Tyr731), thus hampering EGFR ability to associate with the dedicated ubiquitin ligase complex (i.e., CBL-GRB2). This blocks EGFR ubiquitinylation, translocation to endosomes and, consequently, downstream signalling. DEP-1 silencing, on the contrary, enhances tyrosine phosphorylation of endosomal EGFRs, accelerates degradation of EGFR and increases cell proliferation (Tarcic et al., 2009). Consistent with this observation and with the induction of DEP-1 expression in contact-inhibited cells, the gene encoding DEP-1 is often deleted or mutated in carcinomas (Ruivenkamp et al., 2003a).
A genomic analysis of four different DNA samples (peripheral blood, primary tumor, brain metastasis and an early passage xenograft) from a patient with basal-like breast cancer (i.e., ERBB2 and ER negative), identify a missense mutation (K1017N) in DEP1/PTPRJ that is highly enriched during disease progression, since it is found enriched in metastasis and in the human-in-mouse xenograft, compared to primary tumor (Ding et al., 2010). The mutation site is in the juxtamembrane domain (a basic residue motif) and is in close proximity to the tyrosine-protein phosphatase domain (aa 1041-1298). Sacco et al. reported that the DEP-1 charged peptide 1013-IKPKKSKLIRVE-1024 is responsible for interaction with its substrates, such as ERK1/2 (Sacco et al., 2009). The K1017N mutation found in the basal tumor and the K1016A mutation described in Sacco's report, both describe a change of a basic residue into a neutral residue. The DEP-1 positively charged peptide has a loose resemblance to the KIM domains that is essential to bind the common docking domain of ERK1/2 proteins. Therefore, a mutation in the DEP-1 KIM domain affects ERK1/2 recruitment, thus impacting specifically on phospho-Tyr204 ERK1/2 dephosphorylation efficiency. DEP-1 can therefore suppress proliferation by sequestering ERK1/2, irrespective of ERK1/2 phosphorylation state and by dephosphorylating the ERK1/2 activation loop.
Loss of heterozygosity, and missense mutations in the DEP-1 gene have been identified in several human cancers including colon, lung, and breast, which have also been associated with aberrant Hepatocyte Growth Factor Receptor Tyrosine Kinase (Met) signaling. Palka et al. identify the hepatocyte growth factor/scatter factor receptor Met, the adapter protein GAB1 and the junctional component p120 catenin as potential DEP-1 substrates. Moreover, they show that DEP-1 preferentially dephosphorylates Met at sites involved in Met signaling: a GAB1 binding site (Tyr1349) and a COOH-terminal tyrosine implicated in morphogenesis (Tyr1365), while leaving unaltered the phosphorylation at the Met activation loop (Palka et al., 2003; Wang et al., 2010). A phosphatome RNAi (RNA interference) screen in A549 cells (lung adenocarcinoma) designed to identify phosphatases that behave as key negative regulators of oncogenic Ras signalling, characterized DEP-1 as a specific inhibitor of oncogenic K-Ras activation of Akt. The basis for this may be due to the role of DEP-1 in dephosphorylating residues within the p85 subunit of PI3K, resulting in attenuated PI3K/Akt activation (Omerovic et al., 2010).
Whether or not DEP-1 plays a role in hematologic malignancies is not clear.
DEP1 targets VEGFR2 phospho-tyrosines: In contact-inhibited endothelial cells, the phosphatase DEP-1, by binding beta-catenin and p120, may associate with the cadherin-receptor complex and dephosphorylate VEGFR-2 that is in complex with VEC (vascular endothelial cadherin). Retention of VEGFR-2 at the membrane by VEC and its dephosphorylation by DEP-1 limits its internalization and signaling (Lampugnani et al., 2003; Holsinger et al., 2002; Lampugnani et al., 2006; Lampugnani and Dejana, 2007a; Lampugnani and Dejana, 2007b; Dejana et al., 2008).
Despite its negative role on global VEGFR2 phosphorylation, DEP-1 is a positive regulator of VEGF mediated Src and Akt activation and endothelial cell survival.
In fact, when DEP-1 is depleted, inhibitory Src Y529 phosphorylation is increased and consequently, Src activation is impaired. Reduced Src activity correlates with decreased phosphorylation of GAB1 that cannot associate with PI3K (phosphatidylinositol 3-kinase), thus impairing AKT activation (Chabot et al., 2009).
Entity Cogan's syndrome
Note DEP-1 has been implicated in an autoimmune disease, the Cogan's syndrome, which is a chronic inflammatory disease characterized by sensorineural hearing loss, keratitis, and vasculitis. A screen for autoantigens in this disease revealed antibodies to DEP-1, which is expressed on the sensory epithelia of the inner ear and on endothelial cells (Lunardi et al., 2002). These autoantibodies inhibit proliferation of DEP-1 expressing cells and can replicate the hearing loss feature of Cogan's disease, when infused into mice. It is not determined whether these antibodies are causative for this autoimmune disease and/or others (e.g., pseudo-Pendred syndrome) (Davis et al., 2006).


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PMID 11259588
DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients.
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This paper should be referenced as such :
Sacco, F ; Corallino, S ; Castagnoli, L
PTPRJ (protein tyrosine phosphatase, receptor type, J)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(10):867-872.
Free journal version : [ pdf ]   [ DOI ]
On line version :

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(11;11)(p11;q23) PTPRJ/C2CD2L

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 2 ]
  t(1;11)(q23;p11) PTPRJ/FCER1G
t(11;11)(p11;p15) SOX6/PTPRJ

External links

HGNC (Hugo)PTPRJ   9673
Entrez_Gene (NCBI)PTPRJ  5795  protein tyrosine phosphatase, receptor type J
AliasesCD148; DEP1; HPTPeta; R-PTP-ETA; 
GeneCards (Weizmann)PTPRJ
Ensembl hg19 (Hinxton)ENSG00000149177 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000149177 [Gene_View]  ENSG00000149177 [Sequence]  chr11:47980558-48170842 [Contig_View]  PTPRJ [Vega]
ICGC DataPortalENSG00000149177
Genatlas (Paris)PTPRJ
Genetics Home Reference (NIH)PTPRJ
Genomic and cartography
GoldenPath hg38 (UCSC)PTPRJ  -     chr11:47980558-48170842 +  11p11.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)PTPRJ  -     11p11.2   [Description]    (hg19-Feb_2009)
EnsemblPTPRJ - 11p11.2 [CytoView hg19]  PTPRJ - 11p11.2 [CytoView hg38]
Mapping of homologs : NCBIPTPRJ [Mapview hg19]  PTPRJ [Mapview hg38]
Gene and transcription
Genbank (Entrez)AI218139 AL359057 AL832403 BC019824 BC063417
RefSeq transcript (Entrez)NM_001098503 NM_002843
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)PTPRJ
Cluster EST : UnigeneHs.318547 [ NCBI ]
CGAP (NCI)Hs.318547
Alternative Splicing GalleryENSG00000149177
Gene Expression Viewer (FireBrowse)PTPRJ [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5795
GTEX Portal (Tissue expression)PTPRJ
Human Protein AtlasENSG00000149177-PTPRJ [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ12913   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ12913  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ12913
Splice isoforms : SwissVarQ12913
Catalytic activity : Enzyme3.1.3.48 [ Enzyme-Expasy ] [ IntEnz-EBI ] [ BRENDA ] [ KEGG ]   
Domaine pattern : Prosite (Expaxy)FN3 (PS50853)    TYR_PHOSPHATASE_1 (PS00383)    TYR_PHOSPHATASE_2 (PS50056)    TYR_PHOSPHATASE_PTP (PS50055)   
Domains : Interpro (EBI)FN3_dom    FN3_sf    Ig-like_fold    Prot-tyrosine_phosphatase-like    PTPase_domain    Tyr_Pase_AS    Tyr_Pase_cat    TYR_PHOSPHATASE_dom   
Domain families : Pfam (Sanger)fn3 (PF00041)    Y_phosphatase (PF00102)   
Domain families : Pfam (NCBI)pfam00041    pfam00102   
Domain families : Smart (EMBL)FN3 (SM00060)  PTPc (SM00194)  PTPc_motif (SM00404)  
Conserved Domain (NCBI)PTPRJ
DMDM Disease mutations5795
Blocks (Seattle)PTPRJ
PDB (SRS)2CFV    2DLE    2NZ6   
PDB (PDBSum)2CFV    2DLE    2NZ6   
PDB (IMB)2CFV    2DLE    2NZ6   
PDB (RSDB)2CFV    2DLE    2NZ6   
Structural Biology KnowledgeBase2CFV    2DLE    2NZ6   
SCOP (Structural Classification of Proteins)2CFV    2DLE    2NZ6   
CATH (Classification of proteins structures)2CFV    2DLE    2NZ6   
Human Protein Atlas [tissue]ENSG00000149177-PTPRJ [tissue]
Peptide AtlasQ12913
IPIIPI00943343   IPI00290328   IPI00847732   IPI00982486   IPI00982293   
Protein Interaction databases
IntAct (EBI)Q12913
Ontologies - Pathways
Ontology : AmiGOimmunological synapse  protein tyrosine phosphatase activity  protein tyrosine phosphatase activity  protein tyrosine phosphatase activity  platelet-derived growth factor receptor binding  protein binding  plasma membrane  plasma membrane  integral component of plasma membrane  cell-cell junction  beta-catenin binding  negative regulation of cell proliferation  cell surface  negative regulation of platelet-derived growth factor receptor signaling pathway  phosphatase activity  phosphatase activity  protein kinase binding  regulation of cell adhesion  negative regulation of cell growth  negative regulation of cell migration  ruffle membrane  peptidyl-tyrosine dephosphorylation  peptidyl-tyrosine dephosphorylation  specific granule membrane  negative regulation of epidermal growth factor receptor signaling pathway  identical protein binding  negative regulation of vascular permeability  neutrophil degranulation  negative regulation of MAP kinase activity  gamma-catenin binding  positive regulation of cell adhesion  platelet-derived growth factor receptor signaling pathway  T cell receptor signaling pathway  negative regulation of T cell receptor signaling pathway  negative regulation of T cell receptor signaling pathway  positive chemotaxis  mitogen-activated protein kinase binding  positive regulation of focal adhesion assembly  positive regulation of protein kinase B signaling  negative regulation of protein kinase B signaling  contact inhibition  extracellular exosome  delta-catenin binding  
Ontology : EGO-EBIimmunological synapse  protein tyrosine phosphatase activity  protein tyrosine phosphatase activity  protein tyrosine phosphatase activity  platelet-derived growth factor receptor binding  protein binding  plasma membrane  plasma membrane  integral component of plasma membrane  cell-cell junction  beta-catenin binding  negative regulation of cell proliferation  cell surface  negative regulation of platelet-derived growth factor receptor signaling pathway  phosphatase activity  phosphatase activity  protein kinase binding  regulation of cell adhesion  negative regulation of cell growth  negative regulation of cell migration  ruffle membrane  peptidyl-tyrosine dephosphorylation  peptidyl-tyrosine dephosphorylation  specific granule membrane  negative regulation of epidermal growth factor receptor signaling pathway  identical protein binding  negative regulation of vascular permeability  neutrophil degranulation  negative regulation of MAP kinase activity  gamma-catenin binding  positive regulation of cell adhesion  platelet-derived growth factor receptor signaling pathway  T cell receptor signaling pathway  negative regulation of T cell receptor signaling pathway  negative regulation of T cell receptor signaling pathway  positive chemotaxis  mitogen-activated protein kinase binding  positive regulation of focal adhesion assembly  positive regulation of protein kinase B signaling  negative regulation of protein kinase B signaling  contact inhibition  extracellular exosome  delta-catenin binding  
Pathways : KEGGAdherens junction   
REACTOMEQ12913 [protein]
REACTOME PathwaysR-HSA-6807004 [pathway]   
Atlas of Cancer Signalling NetworkPTPRJ
Wikipedia pathwaysPTPRJ
Orthology - Evolution
GeneTree (enSembl)ENSG00000149177
Phylogenetic Trees/Animal Genes : TreeFamPTPRJ
Homologs : HomoloGenePTPRJ
Homology/Alignments : Family Browser (UCSC)PTPRJ
Gene fusions - Rearrangements
Fusion : MitelmanPTPRJ/C2CD2L [11p11.2/11q23.3]  
Fusion : MitelmanPTPRJ/FCER1G [11p11.2/1q23.3]  [t(1;11)(q23;p11)]  
Fusion : MitelmanSOX6/PTPRJ [11p15.2/11p11.2]  [t(11;11)(p11;p15)]  
Fusion PortalPTPRJ 11p11.2 C2CD2L 11q23.3 LAML
Fusion PortalPTPRJ 11p11.2 FCER1G 1q23.3 LUAD
Fusion PortalSOX6 11p15.2 PTPRJ 11p11.2 LGG
Fusion : QuiverPTPRJ
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPTPRJ [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PTPRJ
Exome Variant ServerPTPRJ
ExAC (Exome Aggregation Consortium)ENSG00000149177
GNOMAD BrowserENSG00000149177
Varsome BrowserPTPRJ
Genetic variants : HAPMAP5795
Genomic Variants (DGV)PTPRJ [DGVbeta]
DECIPHERPTPRJ [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisPTPRJ 
ICGC Data PortalPTPRJ 
TCGA Data PortalPTPRJ 
Broad Tumor PortalPTPRJ
OASIS PortalPTPRJ [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPTPRJ  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDPTPRJ
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 PTPRJ
DgiDB (Drug Gene Interaction Database)PTPRJ
DoCM (Curated mutations)PTPRJ (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PTPRJ (select a term)
NCG5 (London)PTPRJ
Cancer3DPTPRJ(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry PTPRJ
NextProtQ12913 [Medical]
Target ValidationPTPRJ
Huge Navigator PTPRJ [HugePedia]
snp3D : Map Gene to Disease5795
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD5795
Chemical/Pharm GKB GenePA34018
Clinical trialPTPRJ
canSAR (ICR)PTPRJ (select the gene name)
PubMed99 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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indexed on : Fri Oct 12 18:11:19 CEST 2018

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