PTPRJ

PTPRJ
Identifiers
Aliases	PTPRJ, CD148, DEP1, HPTPeta, R-PTP-ETA, SCC1, protein tyrosine phosphatase, receptor type J, protein tyrosine phosphatase receptor type J, R-PTP-J, HPTP eta
External IDs	OMIM: 600925; MGI: 104574; HomoloGene: 2130; GeneCards: PTPRJ; OMA:PTPRJ - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CFV, 2DLE, 2NZ6
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.1.3.48 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 11 (human) Band 11p11.2 Start 47,980,559 bp End 48,170,839 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2 E1|2 50.19 cM Start 90,260,098 bp End 90,410,991 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of ileum white blood cell monocyte blood parotid gland renal medulla pylorus bone marrow cell palpebral conjunctiva jejunal mucosa Top expressed in stroma of bone marrow granulocyte olfactory tubercle dentate gyrus primary motor cortex lateral geniculate nucleus piriform cortex ascending aorta dentate gyrus of hippocampal formation granule cell lumbar subsegment of spinal cord More reference expression data BioGPS More reference expression data
Gene ontology Molecular function beta-catenin binding phosphoprotein phosphatase activity gamma-catenin binding phosphatase activity delta-catenin binding mitogen-activated protein kinase binding platelet-derived growth factor receptor binding protein binding hydrolase activity protein kinase binding protein tyrosine phosphatase activity Cellular component integral component of membrane cell projection membrane cell-cell junction plasma membrane integral component of plasma membrane ruffle membrane cell surface cell junction immunological synapse extracellular exosome specific granule membrane Biological process negative regulation of platelet-derived growth factor receptor signaling pathway negative regulation of protein kinase B signaling positive regulation of protein kinase B signaling negative regulation of epidermal growth factor receptor signaling pathway protein dephosphorylation contact inhibition negative regulation of T cell receptor signaling pathway regulation of cell adhesion negative regulation of cell migration negative regulation of MAP kinase activity negative regulation of cell growth positive regulation of focal adhesion assembly platelet-derived growth factor receptor signaling pathway positive chemotaxis peptidyl-tyrosine dephosphorylation T cell receptor signaling pathway negative regulation of cell population proliferation negative regulation of vascular permeability positive regulation of cell adhesion dephosphorylation neutrophil degranulation B cell differentiation positive regulation of tumor necrosis factor production calcium-mediated signaling using intracellular calcium source positive regulation of MAPK cascade positive regulation of peptidyl-tyrosine phosphorylation positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5795 19271 Ensembl ENSG00000149177 ENSMUSG00000025314 UniProt Q12913 Q64455 RefSeq (mRNA) NM_001098503 NM_002843 NM_001135657 NM_008982 RefSeq (protein) NP_001091973 NP_002834 NP_001129129 NP_033008 Location (UCSC) Chr 11: 47.98 – 48.17 Mb Chr 2: 90.26 – 90.41 Mb PubMed search
Wikidata
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Receptor-type tyrosine-protein phosphatase eta is an enzyme that in humans is encoded by the PTPRJ gene.

Function

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.

Interactions

PTPRJ has been shown to interact with CTNND1.

Further reading

• 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. S2CID 26502472.
• Jallal B, Mossie K, Vasiloudis G, Knyazev P, Zachwieja J, Clairvoyant F, Schilling J, Ullrich A (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, Nicolás JM, Freed JH, Palou E, Thomas AP, Vilella R, Vives J, Gayá A (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. doi:10.1182/blood.V91.8.2800.2800_2800_2809. PMID 9531590.
• Tangye SG, Phillips JH, Lanier LL, de Vries JE, Aversa G (1998). "CD148: a receptor-type protein tyrosine phosphatase involved in the regulation of human T cell activation". J. Immunol. 161 (7): 3249–55. doi:10.4049/jimmunol.161.7.3249. PMID 9759839.
• Gross S, Knebel A, Tenev T, Neininger A, Gaestel M, Herrlich P, Böhmer FD (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, Rohr C, Pirotto F, Gassler N, Otto HF, Schraven B, Gaya A (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, Bensussan A, Boumsell L (2000). "Switch in the protein tyrosine phosphatase associated with human CD100 semaphorin at terminal B-cell differentiation stage". Blood. 95 (3): 965–72. doi:10.1182/blood.V95.3.965.003k39_965_972. PMID 10648410.
• Kovalenko M, Denner K, Sandström J, Persson C, Gross S, Jandt E, Vilella R, Böhmer F, Ostman A (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, Cortegano I, Gallardo S, Rojo M, Arrieta I, Aceituno E, Palomino P, Gaya A, Lahoz C (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. doi:10.1189/jlb.68.1.31. PMID 10914487. S2CID 14259114.
• 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. Bibcode:2002FEBSL.517...27P. doi:10.1016/S0014-5793(02)02570-X. PMID 12062403. S2CID 13481032.
• Ruivenkamp CA, van Wezel T, Zanon C, Stassen AP, Vlcek C, Csikós T, Klous AM, Tripodis N, Perrakis A, Boerrigter L, Groot PC, Lindeman J, Mooi WJ, Meijjer GA, Scholten G, Dauwerse H, Paces V, van Zandwijk N, van Ommen GJ, Demant P (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. S2CID 12338558.
• Holsinger LJ, Ward K, Duffield B, Zachwieja J, Jallal B (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. S2CID 25745858.
• Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA (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. Bibcode:2002PNAS...9916899M. 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. S2CID 37520677.
• 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" (PDF). J. Cell Sci. 117 (Pt 4): 609–18. doi:10.1242/jcs.00879. PMID 14709717. S2CID 12250178.
• Massa A, Barbieri F, Aiello C, Arena S, Pattarozzi A, Pirani P, Corsaro A, Iuliano R, Fusco A, Zona G, Spaziante R, Florio T, Schettini G (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.