PTPRJ_HUMAN » Receptor-type tyrosine-protein phosphatase eta

PTPRJ_HUMAN » Receptor-type tyrosine-protein phosphatase eta
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
PTPRJ_HUMAN » Receptor-type tyrosine-protein phosphatase eta » Protein-tyrosine phosphatase eta; R-PTP-eta; Density-enhanced phosphatase 1;DEP-1; HPTP eta;Protein-tyrosine phosphatase receptor type J;R-PTP-J;
Hydrophobic Thickness 38.0 ± 2.2 Å
Tilt Angle 0 ± 0°
ΔGtransfer -48.7 kcal/mol
ΔGfold -16.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 974- 996 (970-1000)
Pathways

Adherens junction (KEGG)

PDB 2dle (366-456), 2cfv (A=1019-1311), 2nz6 (A=1019-1311)
OPM none
Complexes none
Interactions

ALK, Complex: ALK:PTPRJ

CADH2, Complex: PTPRJ:CADH2, PubMed

CP17A, Complex: CP17A:PTPRJ, PubMed

EGFR, Complex: PTPRJ:EGFR, PubMed

EPOR, Complex: EPOR:PTPRJ

ERBB2, Complex: ERBB2:PTPRJ, PubMed

FLT3, Complex: FLT3:PTPRJ

GHR, Complex: GHR:PTPRJ

IL2RG, Complex: IL2RG:PTPRJ, PubMed

INSR, Complex: INSR:PTPRJ

KIT, Complex: KIT:PTPRJ

LAT, Complex: PTPRJ:LAT, PubMed

LEPR, Complex: PTPRJ:LEPR, PubMed

MET, Complex: PTPRJ:MET, PubMed

NTRK1, Complex: NTRK1:PTPRJ

PGFRB, Complex: PGFRB:PTPRJ, PubMed

TEFF1, Complex: TEFF1:PTPRJ

TIE1, Complex: PTPRJ:TIE1, PubMed

TIE2, Complex: PTPRJ:TIE2, PubMed

VGFR1, Complex: VGFR1:PTPRJ

VGFR2, Complex: VGFR2:PTPRJ, PubMed

Domains

AA: 120-199, PDBID: 2DLE, Subunit A, Seq Identity:31%, Fibronectin type III domain

AA: 368-445, PDBID: 2DLE, Subunit A, Seq Identity:100%, Fibronectin type III domain

AA: 1065-1297, PDBID: 2CFV, Subunit A, Seq Identity:100%, Protein-tyrosine phosphatase

UniProt annotation for PTPRJ_HUMAN » Receptor-type tyrosine-protein phosphatase eta
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.

CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.

SUBUNIT: Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2.

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.

UniProt features for PTPRJ_HUMAN » Receptor-type tyrosine-protein phosphatase eta
SIGNAL 1 35 Potential.
CHAIN 36 1337 Receptor-type tyrosine-protein phosphatase eta.
DOMAIN 119 205 Fibronectin type-III 1.
DOMAIN 207 291 Fibronectin type-III 2.
DOMAIN 271 364 Fibronectin type-III 3.
DOMAIN 365 452 Fibronectin type-III 4.
DOMAIN 453 538 Fibronectin type-III 5.
DOMAIN 540 620 Fibronectin type-III 6.
DOMAIN 622 717 Fibronectin type-III 7.
DOMAIN 720 811 Fibronectin type-III 8.
DOMAIN 816 902 Fibronectin type-III 9.
DOMAIN 1041 1298 Tyrosine-protein phosphatase.
REGION 1239 1245 Substrate binding (By similarity).
ACT_SITE 1239 1239 Phosphocysteine intermediate (By similarity).
Amino Acid Sequence for PTPRJ_HUMAN » Receptor-type tyrosine-protein phosphatase eta
MKPAAREARL PPRSPGLRWA LPLLLLLLRL GQILCAGGTP SPIPDPSVAT VATGENGITQ ISSTAESFHK QNGTGTPQVE TNTSEDGESS GANDSLRTPE QGSNGTDGAS QKTPSSTGPS PVFDIKAVSI SPTNVILTWK SNDTAASEYK YVVKHKMENE KTITVVHQPW CNITGLRPAT SYVFSITPGI GNETWGDPRV IKVITEPIPV SDLRVALTGV RKAALSWSNG NGTASCRVLL ESIGSHEELT QDSRLQVNIS GLKPGVQYNI NPYLLQSNKT KGDPLGTEGG LDASNTERSR AGSPTAPVHD ESLVGPVDPS SGQQSRDTEV LLVGLEPGTR YNATVYSQAA NGTEGQPQAI EFRTNAIQVF DVTAVNISAT SLTLIWKVSD NESSSNYTYK IHVAGETDSS NLNVSEPRAV IPGLRSSTFY NITVCPVLGD IEGTPGFLQV HTPPVPVSDF RVTVVSTTEI GLAWSSHDAE SFQMHITQEG AGNSRVEITT NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTVP SAVFDIHVVY VTTTEMWLDW KSPDGASEYV YHLVIESKHG SNHTSTYDKA ITLQGLIPGT LYNITISPEV DHVWGDPNST AQYTRPSNVS NIDVSTNTTA ATLSWQNFDD ASPTYSYCLL IEKAGNSSNA TQVVTDIGIT DATVTELIPG SSYTVEIFAQ VGDGIKSLEP GRKSFCTDPA SMASFDCEVV PKEPALVLKW TCPPGANAGF ELEVSSGAWN NATHLESCSS ENGTEYRTEV TYLNFSTSYN ISITTVSCGK MAAPTRNTCT TGITDPPPPD GSPNITSVSH NSVKVKFSGF EASHGPIKAY AVILTTGEAG HPSADVLKYT YEDFKKGASD TYVTYLIRTE EKGRSQSLSE VLKYEIDVGN ESTTLGYYNG KLEPLGSYRA CVAGFTNITF HPQNKGLIDG AESYVSFSRY SDAVSLPQDP GVICGAVFGC IFGALVIVTV GGFIFWRKKR KDAKNNEVSF SQIKPKKSKL IRVENFEAYF KKQQADSNCG FAEEYEDLKL VGISQPKYAA ELAENRGKNR YNNVLPYDIS RVKLSVQTHS TDDYINANYM PGYHSKKDFI ATQGPLPNTL KDFWRMVWEK NVYAIIMLTK CVEQGRTKCE EYWPSKQAQD YGDITVAMTS EIVLPEWTIR DFTVKNIQTS ESHPLRQFHF TSWPDHGVPD TTDLLINFRY LVRDYMKQSP PESPILVHCS AGVGRTGTFI AIDRLIYQIE NENTVDVYGI VYDLRMHRPL MVQTEDQYVF LNQCVLDIVR SQKDSKVDLI YQNTTAMTIY ENLAPVTTFG KTNGYIA