Q12913 (PTPRJ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 projection › ruffle 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 component	Cell junction Cell membrane Cell projection Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protein phosphatase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Inferred from electronic annotation. Source: Compara contact inhibition Non-traceable author statement Ref.1. Source: UniProtKB heart development Inferred from electronic annotation. Source: Compara 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 cascade Inferred from mutant phenotype Ref.27. Source: UniProtKB negative regulation of receptor activity Inferred from electronic annotation. Source: Compara negative regulation of vascular permeability Inferred from direct assay Ref.22. 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 focal adhesion assembly Inferred from mutant phenotype Ref.26. Source: UniProtKB positive regulation of macrophage chemotaxis Inferred from electronic annotation. Source: Compara positive regulation of platelet activation Inferred from electronic annotation. Source: Compara positive regulation of protein kinase B signaling cascade Inferred from mutant phenotype Ref.25. Source: UniProtKB vasculogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from direct assay Ref.14. Source: UniProtKB cell-cell junction Inferred from direct assay Ref.12Ref.22. Source: UniProtKB immunological synapse Inferred from direct assay Ref.14. Source: UniProtKB integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein tyrosine phosphatase activity Inferred from direct assay Ref.9Ref.14Ref.17Ref.19Ref.25Ref.22Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERBB2	P04626	2	EBI-2264500,EBI-641062
GHR	P10912	2	EBI-2264500,EBI-286316
TEK	Q02763	2	EBI-2264500,EBI-2257090

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 35

35

Potential

Chain

36 – 1337

1302

Receptor-type tyrosine-protein phosphatase eta

PRO_0000025444

Regions

Topological domain

36 – 975

940

Extracellular Potential

Transmembrane

976 – 996

21

Helical; Potential

Topological domain

997 – 1337

341

Cytoplasmic Potential

Domain

119 – 205

87

Fibronectin type-III 1

Domain

207 – 291

85

Fibronectin type-III 2

Domain

271 – 364

94

Fibronectin type-III 3

Domain

365 – 452

88

Fibronectin type-III 4

Domain

453 – 538

86

Fibronectin type-III 5

Domain

540 – 620

81

Fibronectin type-III 6

Domain

622 – 717

96

Fibronectin type-III 7

Domain

720 – 811

92

Fibronectin type-III 8

Domain

816 – 902

87

Fibronectin type-III 9

Domain

1041 – 1298

258

Tyrosine-protein phosphatase

Region

1239 – 1245

7

Substrate binding By similarity

Sites

Active site

1239

1

Phosphocysteine intermediate By similarity

Binding site

1205

1

Substrate By similarity

Binding site

1283

1

Substrate By similarity

Amino acid modifications

Modified residue

1011

1

Phosphoserine By similarity

Glycosylation

72

1

N-linked (GlcNAc...) Potential

Glycosylation

82

1

N-linked (GlcNAc...) Potential

Glycosylation

93

1

N-linked (GlcNAc...) Potential

Glycosylation

104

1

N-linked (GlcNAc...) Potential

Glycosylation

142

1

N-linked (GlcNAc...) Potential

Glycosylation

172

1

N-linked (GlcNAc...) Potential

Glycosylation

192

1

N-linked (GlcNAc...) Potential

Glycosylation

231

1

N-linked (GlcNAc...) Potential

Glycosylation

258

1

N-linked (GlcNAc...) Potential

Glycosylation

278

1

N-linked (GlcNAc...) Potential

Glycosylation

342

1

N-linked (GlcNAc...) Ref.16

Glycosylation

351

1

N-linked (GlcNAc...) Ref.16

Glycosylation

376

1

N-linked (GlcNAc...) Potential

Glycosylation

391

1

N-linked (GlcNAc...) Ref.16

Glycosylation

396

1

N-linked (GlcNAc...) Ref.16

Glycosylation

413

1

N-linked (GlcNAc...) Ref.24

Glycosylation

431

1

N-linked (GlcNAc...) Potential

Glycosylation

501

1

N-linked (GlcNAc...) Potential

Glycosylation

525

1

N-linked (GlcNAc...) Potential

Glycosylation

536

1

N-linked (GlcNAc...) Potential

Glycosylation

582

1

N-linked (GlcNAc...) Potential

Glycosylation

603

1

N-linked (GlcNAc...) Potential

Glycosylation

618

1

N-linked (GlcNAc...) Potential

Glycosylation

628

1

N-linked (GlcNAc...) Potential

Glycosylation

637

1

N-linked (GlcNAc...) Potential

Glycosylation

666

1

N-linked (GlcNAc...) Potential

Glycosylation

669

1

N-linked (GlcNAc...) Potential

Glycosylation

761

1

N-linked (GlcNAc...) Potential

Glycosylation

772

1

N-linked (GlcNAc...) Potential

Glycosylation

784

1

N-linked (GlcNAc...) Potential

Glycosylation

790

1

N-linked (GlcNAc...) Potential

Glycosylation

824

1

N-linked (GlcNAc...) Potential

Glycosylation

910

1

N-linked (GlcNAc...) Potential

Glycosylation

937

1

N-linked (GlcNAc...) Ref.24

Natural variations

Alternative sequence

539

1

V → G in isoform 2.

VSP_043652

Alternative sequence

540 – 1337

798

Missing in isoform 2.

VSP_043653

Natural variant

214

1

R → C in a colon cancer sample; somatic mutation. Ref.5

VAR_015905

Natural variant

276

1

Q → P in a colon cancer sample; somatic mutation. Ref.5 Ref.30
Corresponds to variant rs1566734 [ dbSNP | Ensembl ].

VAR_015906

Natural variant

293

1

A → T.
Corresponds to variant rs2229701 [ dbSNP | Ensembl ].

VAR_038414

Natural variant

326

1

R → Q. Ref.30
Corresponds to variant rs1503185 [ dbSNP | Ensembl ].

VAR_024582

Natural variant

372

1

V → I.
Corresponds to variant rs2229703 [ dbSNP | Ensembl ].

VAR_038415

Natural variant

872

1

E → D. Ref.1 Ref.2 Ref.5 Ref.30
Corresponds to variant rs4752904 [ dbSNP | Ensembl ].

VAR_038416

Natural variant

1235

1

I → T.
Corresponds to variant rs11039554 [ dbSNP | Ensembl ].

VAR_038417

Experimental info

Mutagenesis

1016

1

K → A: 80% decrease in interaction with MAPK1 and MAPK3. Ref.23

Mutagenesis

1205

1

D → 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

Mutagenesis

1239

1

C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. Ref.12 Ref.13 Ref.21 Ref.22 Ref.25 Ref.28

Sequence conflict

261

1

G → D in AAB36687. Ref.1

Sequence conflict

918 – 929

12

YNGKL…LGSYR → LQWEAGTSGLLP in BAA07035. Ref.2

Sequence conflict

1130

1

K → Q no nucleotide entry Ref.6

Sequence conflict

1234

1

P → E no nucleotide entry Ref.6

Sequence conflict

1243

1

V → I no nucleotide entry Ref.6

Secondary structure

1

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1337

Helix Strand Turn

Details...

Beta strand

368 – 377

10

Beta strand

382 – 389

8

Beta strand

398 – 404

7

Beta strand

409 – 420

12

Beta strand

429 – 440

12

Beta strand

446 – 451

6

Helix

1023 – 1047

25

Turn

1048 – 1054

7

Turn

1058 – 1061

4

Helix

1063 – 1068

6

Turn

1078 – 1080

3

Beta strand

1087 – 1089

3

Helix

1090 – 1093

4

Beta strand

1096 – 1100

5

Beta strand

1108 – 1113

6

Turn

1117 – 1119

3

Helix

1120 – 1129

10

Beta strand

1134 – 1138

5

Beta strand

1155 – 1157

3

Beta strand

1159 – 1161

3

Beta strand

1164 – 1173

10

Beta strand

1175 – 1186

12

Turn

1187 – 1189

3

Beta strand

1192 – 1200

9

Helix

1212 – 1225

14

Beta strand

1235 – 1243

9

Helix

1244 – 1261

18

Beta strand

1262 – 1265

4

Helix

1267 – 1275

9

Helix

1285 – 1302

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 5, 2008. Version 3. Checksum: B44F4343FC8FD1B4	FASTA	1,337	145,941
	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
	Isoform 2 [UniParc]. Checksum: E970DA55A6B2E38D	FASTA	539	57,190
	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 SFQMHITQEG AGNSRVEITT NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTG

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.

IPI

IPI00290328.
IPI00847732.

PIR

I38670.

RefSeq

NP_001091973.1. NM_001098503.1.
NP_002834.3. NM_002843.3.

UniGene

Hs.318547.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CFV	X-ray	2.50	A	1019-1311	[»]
2DLE	NMR	-	A	366-456	[»]
2NZ6	X-ray	2.30	A	1019-1311	[»]

ProteinModelPortal

Q12913.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12913. 32 interactions.

MINT

MINT-1349281.

STRING

9606.ENSP00000400010.

PTM databases

PhosphoSite

Q12913.

Polymorphism databases

DMDM

166899088.

Proteomic databases

PaxDb

Q12913.

PRIDE

Q12913.

Protocols and materials databases

DNASU

5795.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000418331; ENSP00000400010; ENSG00000149177.
ENST00000440289; ENSP00000409733; ENSG00000149177.

GeneID

5795.

KEGG

hsa:5795.

UCSC

uc001ngp.4. human.

Organism-specific databases

CTD

5795.

GeneCards

GC11P047958.

H-InvDB

HIX0035923.

HGNC

HGNC:9673. PTPRJ.

HPA

HPA006026.

MIM

600925. gene.

neXtProt

NX_Q12913.

PharmGKB

PA34018.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOGENOM

HOG000232054.

HOVERGEN

HBG053761.

InParanoid

Q12913.

KO

K05698.

OMA

STLYNIT.

OrthoDB

EOG43BMN7.

Enzyme and pathway databases

Pathway_Interaction_DB

pdgfrbpathway. PDGFR-beta signaling pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).

Gene expression databases

ArrayExpress

Q12913.

Bgee

Q12913.

CleanEx

HS_PTPRJ.

Genevestigator

Q12913.

GermOnline

ENSG00000149177. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 5 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF00041. fn3. 4 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PRINTS

PR00700. PRTYPHPHTASE.

SMART

SM00060. FN3. 8 hits.
SM00194. PTPc. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 5 hits.

PROSITE

PS50853. FN3. 9 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q12913.

ChEMBL

CHEMBL3692.

ChiTaRS

PTPRJ. human.

EvolutionaryTrace

Q12913.

GenomeRNAi

5795.

NextBio

22564.

SOURCE

Search...

Entry information

Entry name

PTPRJ_HUMAN

Accession

Primary (citable) accession number: Q12913
Secondary accession number(s): Q15255 , Q6P4H4, Q8NHM2, Q9UDA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.