PTPRJ

Protein-coding gene in the species Homo sapiens

PTPRJ

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2CFV, 2DLE, 2NZ6

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

Gene location (Human)

Chr.	Chromosome 11 (human)^[1]

Band	11p11.2	Start	47,980,559 bp^[1]
Band	11p11.2	End	48,170,839 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	2 E1\|2 50.19 cM	Start	90,260,098 bp^[2]
Band	2 E1\|2 50.19 cM	End	90,410,991 bp^[2]

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 cells

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Receptor-type tyrosine-protein phosphatase eta is an enzyme that in humans is encoded by the PTPRJ gene.^[5]^[6]^[7]

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.^[7]

Interactions

PTPRJ has been shown to interact with CTNND1.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000149177 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025314 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. Bibcode:1994PNAS...91.9680O. doi:10.1073/pnas.91.21.9680. PMC 44880. PMID 7937872.
^ 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. doi:10.1182/blood.V84.12.4186.bloodjournal84124186. PMID 7994032.
^ ^a ^b "Entrez Gene: PTPRJ protein tyrosine phosphatase, receptor type, J".
^ Holsinger LJ, Ward K, Duffield B, Zachwieja J, Jallal B (Oct 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.

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. 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.

PDB gallery

2cfv: CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE J
2dle: Solution structure of the fourth fn3 domain of human receptor-type tyrosine-protein phosphatase eta
2nz6: Crystal structure of the PTPRJ inactivating mutant C1239S

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs

Receptor type PTPs	PTPRA PTPRB PTPRC PTPRD PTPRE PTPRF PTPRG PTPRH PTPRJ PTPRK PTPRM PTPRN PTPRN2 PTPRO PTPRQ PTPRR PTPRS PTPRT PTPRU PTPRZ1 PTPRZ2
Non receptor type PTPs	PTPN1 PTPN2 PTPN3 PTPN4 PTPN5 PTPN6 PTPN7 PTPN9 PTPN11 PTPN12 PTPN13 PTPN14 PTPN18 PTPN20 PTPN21 PTPN22 PTPN23

VH1-like or
dual specific
phosphatases
(DSPs)

MAPK phosphatases (MKPs)	DUSP1 DUSP2 DUSP4 DUSP5 DUSP6 DUSP7 DUSP8 DUSP9 DUSP10 DUSP16 MK-STYX
Slingshots	SSH1 SSH2 SSH3
PRLs	PTP4A1 PTP4A2 PTP4A3
CDC14s	CDC14A CDC14B CDKN3 PTP9Q22
Atypical DSPs	DUSP3 DUSP11 DUSP12 DUSP13A DUSP13B DUSP14 DUSP15 DUSP18 DUSP19 DUSP21 DUSP22 DUSP23 DUSP24 DUSP25 DUSP26 DUSP27 EMP2A RNGTT STYX
Phosphatase and tensin homologs (PTENs)	PTEN TPIP TPTE TNS TENC1
Myotubularins	MTM1 MTMR2 MTMR3 MTMR4 MTMR5 MTMR6 MTMR7 MTMR8 MTMR9 MTMR10 MTMR11 MTMR12 MTMR13 MTMR14 MTMR15