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Q12913 (PTPRJ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase eta

Short name=Protein-tyrosine phosphatase eta
Short name=R-PTP-eta
EC=3.1.3.48
Alternative name(s):
Density-enhanced phosphatase 1
Short name=DEP-1
HPTP eta
Protein-tyrosine phosphatase receptor type J
Short name=R-PTP-J
CD_antigen=CD148
Gene names
Name:PTPRJ
Synonyms:DEP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2. Ref.12 Ref.13 Ref.20 Ref.28

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cell projectionruffle membrane By similarity. Cell junction. Note: After T-cell stimulation, it is temporarily excluded from immunological synapses. Ref.7 Ref.12 Ref.14 Ref.19 Ref.21 Ref.22

Tissue specificity

Expressed in the promyelocytic cell line HL-60, the granulocyte-macrophage colony-stimulating factor-dependent leukemic cell line F-36P, and the IL3 and erythropoietin-dependent leukemic cell line F-36E. Expressed predominantly in epithelial cells and lymphocytes. Enhanced expression at high cell density. Ref.6 Ref.7 Ref.12

Post-translational modification

N- and O-glycosylated. Ref.7

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily.

Contains 9 fibronectin type-III domains.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from electronic annotation. Source: Ensembl

contact inhibition

Non-traceable author statement Ref.1. Source: UniProtKB

heart development

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAP kinase activity

Inferred from direct assay Ref.23. Source: UniProtKB

negative regulation of T cell receptor signaling pathway

Inferred from direct assay Ref.14. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay Ref.15. Source: UniProtKB

negative regulation of cell migration

Inferred from direct assay Ref.18. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay Ref.15Ref.18Ref.17. Source: UniProtKB

negative regulation of epidermal growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.21. Source: UniProtKB

negative regulation of platelet-derived growth factor receptor signaling pathway

Inferred from direct assay Ref.15. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from mutant phenotype Ref.27. Source: UniProtKB

negative regulation of receptor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of vascular permeability

Inferred from direct assay Ref.22. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.9Ref.14Ref.17Ref.19Ref.25Ref.22Ref.7. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.26. Source: UniProtKB

positive chemotaxis

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of cell adhesion

Inferred from mutant phenotype Ref.26. Source: UniProtKB

positive regulation of focal adhesion assembly

Inferred from mutant phenotype Ref.26. Source: UniProtKB

positive regulation of macrophage chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of platelet activation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from mutant phenotype Ref.25. Source: UniProtKB

regulation of cell adhesion

Inferred from mutant phenotype Ref.12. Source: UniProtKB

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay Ref.14. Source: UniProtKB

cell-cell junction

Inferred from direct assay Ref.12Ref.22. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

immunological synapse

Inferred from direct assay Ref.14. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Inferred from direct assay Ref.19Ref.21Ref.7. Source: UniProtKB

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-catenin binding

Inferred from physical interaction Ref.12. Source: UniProtKB

delta-catenin binding

Inferred from physical interaction Ref.12Ref.22. Source: UniProtKB

gamma-catenin binding

Inferred from physical interaction Ref.12. Source: UniProtKB

mitogen-activated protein kinase binding

Inferred from physical interaction Ref.23. Source: UniProtKB

phosphatase activity

Inferred from direct assay Ref.11Ref.12Ref.23. Source: UniProtKB

platelet-derived growth factor receptor binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.22. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay Ref.9Ref.14Ref.17Ref.19Ref.25Ref.22Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12913-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q12913-2)

The sequence of this isoform differs from the canonical sequence as follows:
     539-539: V → G
     540-1337: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 13371302Receptor-type tyrosine-protein phosphatase eta
PRO_0000025444

Regions

Topological domain36 – 975940Extracellular Potential
Transmembrane976 – 99621Helical; Potential
Topological domain997 – 1337341Cytoplasmic Potential
Domain121 – 20989Fibronectin type-III 1
Domain207 – 29185Fibronectin type-III 2
Domain271 – 36494Fibronectin type-III 3
Domain368 – 45689Fibronectin type-III 4
Domain457 – 54185Fibronectin type-III 5
Domain542 – 62382Fibronectin type-III 6
Domain625 – 72096Fibronectin type-III 7
Domain721 – 81797Fibronectin type-III 8
Domain816 – 90287Fibronectin type-III 9
Domain1041 – 1298258Tyrosine-protein phosphatase
Region1239 – 12457Substrate binding By similarity

Sites

Active site12391Phosphocysteine intermediate By similarity
Binding site12051Substrate By similarity
Binding site12831Substrate By similarity

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Ref.16
Glycosylation3511N-linked (GlcNAc...) Ref.16
Glycosylation3761N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Ref.16
Glycosylation3961N-linked (GlcNAc...) Ref.16
Glycosylation4131N-linked (GlcNAc...) Ref.24
Glycosylation4311N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation5251N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Glycosylation5821N-linked (GlcNAc...) Potential
Glycosylation6031N-linked (GlcNAc...) Potential
Glycosylation6181N-linked (GlcNAc...) Potential
Glycosylation6281N-linked (GlcNAc...) Potential
Glycosylation6371N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Glycosylation6691N-linked (GlcNAc...) Potential
Glycosylation7611N-linked (GlcNAc...) Potential
Glycosylation7721N-linked (GlcNAc...) Potential
Glycosylation7841N-linked (GlcNAc...) Potential
Glycosylation7901N-linked (GlcNAc...) Potential
Glycosylation8241N-linked (GlcNAc...) Potential
Glycosylation9101N-linked (GlcNAc...) Potential
Glycosylation9371N-linked (GlcNAc...) Ref.24

Natural variations

Alternative sequence5391V → G in isoform 2.
VSP_043652
Alternative sequence540 – 1337798Missing in isoform 2.
VSP_043653
Natural variant2141R → C in a colon cancer sample; somatic mutation. Ref.5
VAR_015905
Natural variant2761Q → P in a colon cancer sample; somatic mutation. Ref.5 Ref.30
Corresponds to variant rs1566734 [ dbSNP | Ensembl ].
VAR_015906
Natural variant2931A → T.
Corresponds to variant rs2229701 [ dbSNP | Ensembl ].
VAR_038414
Natural variant3261R → Q. Ref.30
Corresponds to variant rs1503185 [ dbSNP | Ensembl ].
VAR_024582
Natural variant3721V → I.
Corresponds to variant rs2229703 [ dbSNP | Ensembl ].
VAR_038415
Natural variant8721E → D. Ref.1 Ref.2 Ref.5 Ref.30
Corresponds to variant rs4752904 [ dbSNP | Ensembl ].
VAR_038416
Natural variant12351I → T.
Corresponds to variant rs11039554 [ dbSNP | Ensembl ].
VAR_038417

Experimental info

Mutagenesis10161K → A: 80% decrease in interaction with MAPK1 and MAPK3. Ref.23
Mutagenesis12051D → A: Substrate trapping with much higher affinity for substrate. Ref.12 Ref.13 Ref.17 Ref.19 Ref.21 Ref.22 Ref.23 Ref.25 Ref.28
Mutagenesis12391C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. Ref.12 Ref.13 Ref.21 Ref.22 Ref.25 Ref.28
Sequence conflict2611G → D in AAB36687. Ref.1
Sequence conflict918 – 92912YNGKL…LGSYR → LQWEAGTSGLLP in BAA07035. Ref.2
Sequence conflict11301K → Q no nucleotide entry Ref.6
Sequence conflict12341P → E no nucleotide entry Ref.6
Sequence conflict12431V → I no nucleotide entry Ref.6

Secondary structure

....................................................... 1337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 5, 2008. Version 3.
Checksum: B44F4343FC8FD1B4

FASTA1,337145,941
        10         20         30         40         50         60 
MKPAAREARL PPRSPGLRWA LPLLLLLLRL GQILCAGGTP SPIPDPSVAT VATGENGITQ 

        70         80         90        100        110        120 
ISSTAESFHK QNGTGTPQVE TNTSEDGESS GANDSLRTPE QGSNGTDGAS QKTPSSTGPS 

       130        140        150        160        170        180 
PVFDIKAVSI SPTNVILTWK SNDTAASEYK YVVKHKMENE KTITVVHQPW CNITGLRPAT 

       190        200        210        220        230        240 
SYVFSITPGI GNETWGDPRV IKVITEPIPV SDLRVALTGV RKAALSWSNG NGTASCRVLL 

       250        260        270        280        290        300 
ESIGSHEELT QDSRLQVNIS GLKPGVQYNI NPYLLQSNKT KGDPLGTEGG LDASNTERSR 

       310        320        330        340        350        360 
AGSPTAPVHD ESLVGPVDPS SGQQSRDTEV LLVGLEPGTR YNATVYSQAA NGTEGQPQAI 

       370        380        390        400        410        420 
EFRTNAIQVF DVTAVNISAT SLTLIWKVSD NESSSNYTYK IHVAGETDSS NLNVSEPRAV 

       430        440        450        460        470        480 
IPGLRSSTFY NITVCPVLGD IEGTPGFLQV HTPPVPVSDF RVTVVSTTEI GLAWSSHDAE 

       490        500        510        520        530        540 
SFQMHITQEG AGNSRVEITT NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTVP 

       550        560        570        580        590        600 
SAVFDIHVVY VTTTEMWLDW KSPDGASEYV YHLVIESKHG SNHTSTYDKA ITLQGLIPGT 

       610        620        630        640        650        660 
LYNITISPEV DHVWGDPNST AQYTRPSNVS NIDVSTNTTA ATLSWQNFDD ASPTYSYCLL 

       670        680        690        700        710        720 
IEKAGNSSNA TQVVTDIGIT DATVTELIPG SSYTVEIFAQ VGDGIKSLEP GRKSFCTDPA 

       730        740        750        760        770        780 
SMASFDCEVV PKEPALVLKW TCPPGANAGF ELEVSSGAWN NATHLESCSS ENGTEYRTEV 

       790        800        810        820        830        840 
TYLNFSTSYN ISITTVSCGK MAAPTRNTCT TGITDPPPPD GSPNITSVSH NSVKVKFSGF 

       850        860        870        880        890        900 
EASHGPIKAY AVILTTGEAG HPSADVLKYT YEDFKKGASD TYVTYLIRTE EKGRSQSLSE 

       910        920        930        940        950        960 
VLKYEIDVGN ESTTLGYYNG KLEPLGSYRA CVAGFTNITF HPQNKGLIDG AESYVSFSRY 

       970        980        990       1000       1010       1020 
SDAVSLPQDP GVICGAVFGC IFGALVIVTV GGFIFWRKKR KDAKNNEVSF SQIKPKKSKL 

      1030       1040       1050       1060       1070       1080 
IRVENFEAYF KKQQADSNCG FAEEYEDLKL VGISQPKYAA ELAENRGKNR YNNVLPYDIS 

      1090       1100       1110       1120       1130       1140 
RVKLSVQTHS TDDYINANYM PGYHSKKDFI ATQGPLPNTL KDFWRMVWEK NVYAIIMLTK 

      1150       1160       1170       1180       1190       1200 
CVEQGRTKCE EYWPSKQAQD YGDITVAMTS EIVLPEWTIR DFTVKNIQTS ESHPLRQFHF 

      1210       1220       1230       1240       1250       1260 
TSWPDHGVPD TTDLLINFRY LVRDYMKQSP PESPILVHCS AGVGRTGTFI AIDRLIYQIE 

      1270       1280       1290       1300       1310       1320 
NENTVDVYGI VYDLRMHRPL MVQTEDQYVF LNQCVLDIVR SQKDSKVDLI YQNTTAMTIY 

      1330 
ENLAPVTTFG KTNGYIA 

« Hide

Isoform 2 [UniParc].

Checksum: E970DA55A6B2E38D
Show »

FASTA53957,190

References

« Hide 'large scale' references
[1]"Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density."
Oestman A., Yang Q., Tonks N.K.
Proc. Natl. Acad. Sci. U.S.A. 91:9680-9684(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-872.
[2]"Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta."
Honda H., Inazawa J., Nishida J., Yazaki Y., Hirai H.
Blood 84:4186-4194(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-872.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Pancreas.
[5]"Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers."
Ruivenkamp C.A.L., van Wezel T., Zanon C., Stassen A.P.M., Vlcek C., Csikos T., Klous A.M., Tripodis N., Perrakis A., Boerrigter L., Groot P.C., Lindeman J., Mooi W.J., Meijjer G.A., Scholten G., Dauwerse H., Paces V., van Zandwijk N., van Ommen G.J.B., Demant P.
Nat. Genet. 31:295-300(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-1337, VARIANTS CYS-214; PRO-276 AND ASP-872.
Tissue: Colon.
[6]"Identification of novel protein-tyrosine phosphatases in a human leukemia cell line, F-36P."
Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.
Leukemia 7:742-746(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1124-1245 (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Leukemia.
[7]"CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes."
de la Fuente-Garcia M.A., Nicolas J.M., Freed J.H., Palou E., Thomas A.P., Vilella R., Vives J., Gaya A.
Blood 91:2800-2809(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-49; 485-502 AND 723-739, FUNCTION, TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
[8]"Negative regulation of human T cell activation by the receptor-type protein tyrosine phosphatase CD148."
Tangye S.G., Wu J., Aversa G., de Vries J.E., Lanier L.L., Phillips J.H.
J. Immunol. 161:3803-3807(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1."
Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E., Vilella R., Bohmer F., Ostman A.
J. Biol. Chem. 275:16219-16226(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation."
Baker J.E., Majeti R., Tangye S.G., Weiss A.
Mol. Cell. Biol. 21:2393-2403(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1."
Persson C., Engstrom U., Mowbray S.L., Ostman A.
FEBS Lett. 517:27-31(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)."
Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.
Oncogene 21:7067-7076(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTNNB1 AND JUP, MUTAGENESIS OF ASP-1205 AND CYS-1239, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[13]"Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1."
Palka H.L., Park M., Tonks N.K.
J. Biol. Chem. 278:5728-5735(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTNNB1; GRB2; GAB1 AND JUP, MUTAGENESIS OF ASP-1205 AND CYS-1239.
[14]"The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling."
Lin J., Weiss A.
J. Cell Biol. 162:673-682(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]"The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation."
Kellie S., Craggs G., Bird I.N., Jones G.E.
J. Cell Sci. 117:609-618(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-342; ASN-351; ASN-391 AND ASN-396.
Tissue: Plasma.
[17]"The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins."
Iervolino A., Iuliano R., Trapasso F., Viglietto G., Melillo R.M., Carlomagno F., Santoro M., Fusco A.
Cancer Res. 66:6280-6287(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-1205.
[18]"DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients."
Balavenkatraman K.K., Jandt E., Friedrich K., Kautenburger T., Pool-Zobel B.L., Ostman A., Bohmer F.D.
Oncogene 25:6319-6324(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase."
Tsuboi N., Utsunomiya T., Roberts R.L., Ito H., Takahashi K., Noda M., Takahashi T.
Biochem. J. 413:193-200(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-1205, SUBCELLULAR LOCATION.
[20]"The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis."
Senis Y.A., Tomlinson M.G., Ellison S., Mazharian A., Lim J., Zhao Y., Kornerup K.N., Auger J.M., Thomas S.G., Dhanjal T., Kalia N., Zhu J.W., Weiss A., Watson S.P.
Blood 113:4942-4954(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[21]"An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis."
Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F., Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.
Curr. Biol. 19:1788-1798(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EGFR REGULATION, MUTAGENESIS OF ASP-1205 AND CYS-1239, SUBCELLULAR LOCATION.
[22]"Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells."
Sallee J.L., Burridge K.
J. Biol. Chem. 284:14997-15006(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-1205 AND CYS-1239, SUBCELLULAR LOCATION.
[23]"Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases."
Sacco F., Tinti M., Palma A., Ferrari E., Nardozza A.P., Hooft van Huijsduijnen R., Takahashi T., Castagnoli L., Cesareni G.
J. Biol. Chem. 284:22048-22058(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-1016 AND ASP-1205.
[24]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-413 AND ASN-937.
Tissue: Liver.
[25]"New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival."
Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.
Mol. Cell. Biol. 29:241-253(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-1205 AND CYS-1239.
[26]"Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives meningioma cell motility."
Petermann A., Haase D., Wetzel A., Balavenkatraman K.K., Tenev T., Guhrs K.H., Friedrich S., Nakamura M., Mawrin C., Bohmer F.D.
Brain Pathol. 21:405-418(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[27]"Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative regulators of PKB/Akt activation in Ras-mutated cancer cells."
Omerovic J., Clague M.J., Prior I.A.
Biochem. J. 426:65-72(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling."
Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K., Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D., Muller J.P.
J. Biol. Chem. 286:10918-10929(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FLT3, MUTAGENESIS OF ASP-1205 AND CYS-1239.
[29]"Solution structure of the fourth FN3 domain of human receptor-type tyrosine-protein phosphatase eta."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 366-456.
[30]"The tyrosine phosphatase PTPRJ/DEP-1 genotype affects thyroid carcinogenesis."
Iuliano R., Le Pera I., Cristofaro C., Baudi F., Arturi F., Pallante P., Martelli M.L., Trapasso F., Chiariotti L., Fusco A.
Oncogene 23:8432-8438(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PRO-276; GLN-326 AND ASP-872.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10886 mRNA. Translation: AAB36687.1.
D37781 mRNA. Translation: BAA07035.1.
AC026975 Genomic DNA. No translation available.
AC103828 Genomic DNA. No translation available.
BC063417 mRNA. Translation: AAH63417.1.
AH011675 Genomic DNA. Translation: AAM69432.1.
PIRI38670.
RefSeqNP_001091973.1. NM_001098503.1.
NP_002834.3. NM_002843.3.
UniGeneHs.318547.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CFVX-ray2.50A1019-1311[»]
2DLENMR-A366-456[»]
2NZ6X-ray2.30A1019-1311[»]
ProteinModelPortalQ12913.
SMRQ12913. Positions 319-714, 1018-1303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111759. 10 interactions.
IntActQ12913. 38 interactions.
MINTMINT-1349281.
STRING9606.ENSP00000400010.

Chemistry

BindingDBQ12913.
ChEMBLCHEMBL3692.

PTM databases

PhosphoSiteQ12913.

Polymorphism databases

DMDM166899088.

Proteomic databases

PaxDbQ12913.
PRIDEQ12913.

Protocols and materials databases

DNASU5795.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000418331; ENSP00000400010; ENSG00000149177. [Q12913-1]
ENST00000440289; ENSP00000409733; ENSG00000149177. [Q12913-2]
GeneID5795.
KEGGhsa:5795.
UCSCuc001ngo.4. human. [Q12913-2]
uc001ngp.4. human. [Q12913-1]

Organism-specific databases

CTD5795.
GeneCardsGC11P047958.
H-InvDBHIX0035923.
HGNCHGNC:9673. PTPRJ.
HPAHPA006026.
MIM600925. gene.
neXtProtNX_Q12913.
PharmGKBPA34018.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000232054.
HOVERGENHBG053761.
InParanoidQ12913.
KOK05698.
OMAYENLAPV.
OrthoDBEOG7PCJFZ.
PhylomeDBQ12913.
TreeFamTF351926.

Enzyme and pathway databases

SignaLinkQ12913.

Gene expression databases

ArrayExpressQ12913.
BgeeQ12913.
CleanExHS_PTPRJ.
GenevestigatorQ12913.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 4 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 8 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 4 hits.
PROSITEPS50853. FN3. 6 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPRJ. human.
EvolutionaryTraceQ12913.
GeneWikiPTPRJ.
GenomeRNAi5795.
NextBio22564.
PROQ12913.
SOURCESearch...

Entry information

Entry namePTPRJ_HUMAN
AccessionPrimary (citable) accession number: Q12913
Secondary accession number(s): Q15255 expand/collapse secondary AC list , Q6P4H4, Q8NHM2, Q9UDA9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries