PTPRJ

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Protein tyrosine phosphatase, receptor type, J
Protein PTPRJ PDB 2cfv.png
PDB rendering based on 2cfv.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PTPRJ ; CD148; DEP1; HPTPeta; R-PTP-ETA; SCC1
External IDs OMIM600925 MGI104574 HomoloGene2130 ChEMBL: 3692 GeneCards: PTPRJ Gene
EC number 3.1.3.48
RNA expression pattern
PBB GE PTPRJ 210173 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5795 19271
Ensembl ENSG00000149177 ENSMUSG00000025314
UniProt Q12913 Q64455
RefSeq (mRNA) NM_001098503 NM_001135657
RefSeq (protein) NP_001091973 NP_001129129
Location (UCSC) Chr 11:
48 – 48.19 Mb
Chr 2:
90.43 – 90.58 Mb
PubMed search [1] [2]

Receptor-type tyrosine-protein phosphatase eta is an enzyme that in humans is encoded by the PTPRJ gene.[1][2][3]

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region containing five fibronectin type III repeats, a single transmembrane region, and a single intracytoplasmic catalytic domain, and thus represents a receptor-type PTP. This PTP is present in all hematopoietic lineages, and was shown to negatively regulate T cell receptor signaling possibly through interfering with the phosphorylation of Phospholipase C Gamma 1 (PLCG1) and Linker for Activation of T Cells (LAT). This PTP was also found to dephosphorylate PDGF beta receptor, and may be involved in UV-induced signal transduction.[3]

Interactions[edit]

PTPRJ has been shown to interact with CTNND1.[4]

References[edit]

  1. ^ Ostman A, Yang Q, Tonks NK (Nov 1994). "Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density". Proc Natl Acad Sci U S A 91 (21): 9680–4. doi:10.1073/pnas.91.21.9680. PMC 44880. PMID 7937872. 
  2. ^ Honda H, Inazawa J, Nishida J, Yazaki Y, Hirai H (Jan 1995). "Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta". Blood 84 (12): 4186–94. PMID 7994032. 
  3. ^ a b "Entrez Gene: PTPRJ protein tyrosine phosphatase, receptor type, J". 
  4. ^ Holsinger, Leslie J; Ward Kevin; Duffield Bill; Zachwieja Joseph; Jallal Bahija (Oct 2002). "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)". Oncogene (England) 21 (46): 7067–76. doi:10.1038/sj.onc.1205858. ISSN 0950-9232. PMID 12370829. 

Further reading[edit]

  • Harrod TR, Justement LB (2003). "Evaluating function of transmembrane protein tyrosine phosphatase CD148 in lymphocyte biology". Immunol. Res. 26 (1–3): 153–66. doi:10.1385/IR:26:1-3:153. PMID 12403354. 
  • Jallal B, Mossie K, Vasiloudis G et al. (1997). "The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase". J. Biol. Chem. 272 (18): 12158–63. doi:10.1074/jbc.272.18.12158. PMID 9115287. 
  • de la Fuente-García MA (1998). "CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes". Blood 91 (8): 2800–9. PMID 9531590. 
  • Tangye SG, Phillips JH, Lanier LL et al. (1998). "CD148: a receptor-type protein tyrosine phosphatase involved in the regulation of human T cell activation". J. Immunol. 161 (7): 3249–55. PMID 9759839. 
  • Gross S, Knebel A, Tenev T et al. (1999). "Inactivation of protein-tyrosine phosphatases as mechanism of UV-induced signal transduction". J. Biol. Chem. 274 (37): 26378–86. doi:10.1074/jbc.274.37.26378. PMID 10473595. 
  • Autschbach F, Palou E, Mechtersheimer G et al. (2000). "Expression of the membrane protein tyrosine phosphatase CD148 in human tissues". Tissue Antigens 54 (5): 485–98. doi:10.1034/j.1399-0039.1999.540506.x. PMID 10599888. 
  • Billard C, Delaire S, Raffoux E et al. (2000). "Switch in the protein tyrosine phosphatase associated with human CD100 semaphorin at terminal B-cell differentiation stage". Blood 95 (3): 965–72. PMID 10648410. 
  • Kovalenko M, Denner K, Sandström J et al. (2000). "Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1". J. Biol. Chem. 275 (21): 16219–26. doi:10.1074/jbc.275.21.16219. PMID 10821867. 
  • del Pozo V, Pirotto F, Cárdaba B et al. (2000). "Expression on human eosinophils of CD148: a membrane tyrosine phosphatase. Implications in the effector function of eosinophils". J. Leukoc. Biol. 68 (1): 31–7. PMID 10914487. 
  • Baker JE, Majeti R, Tangye SG, Weiss A (2001). "Protein Tyrosine Phosphatase CD148-Mediated Inhibition of T-Cell Receptor Signal Transduction Is Associated with Reduced LAT and Phospholipase Cγ1 Phosphorylation". Mol. Cell. Biol. 21 (7): 2393–403. doi:10.1128/MCB.21.7.2393-2403.2001. PMC 86872. PMID 11259588. 
  • Persson C, Engström U, Mowbray SL, Ostman A (2002). "Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1". FEBS Lett. 517 (1–3): 27–31. doi:10.1016/S0014-5793(02)02570-X. PMID 12062403. 
  • Ruivenkamp CA, van Wezel T, Zanon C et al. (2002). "Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers". Nat. Genet. 31 (3): 295–300. doi:10.1038/ng903. PMID 12089527. 
  • Holsinger LJ, Ward K, Duffield B et al. (2002). "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)". Oncogene 21 (46): 7067–76. doi:10.1038/sj.onc.1205858. PMID 12370829. 
  • Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
  • Dong HY, Shahsafaei A, Dorfman DM (2003). "CD148 and CD27 are expressed in B cell lymphomas derived from both memory and naïve B cells". Leuk. Lymphoma 43 (9): 1855–8. doi:10.1080/1042819021000006385. PMID 12685844. 
  • Kellie S, Craggs G, Bird IN, Jones GE (2004). "The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation". J. Cell. Sci. 117 (Pt 4): 609–18. doi:10.1242/jcs.00879. PMID 14709717. 
  • Massa A, Barbieri F, Aiello C et al. (2004). "The expression of the phosphotyrosine phosphatase DEP-1/PTPeta dictates the responsivity of glioma cells to somatostatin inhibition of cell proliferation". J. Biol. Chem. 279 (28): 29004–12. doi:10.1074/jbc.M403573200. PMID 15123617.