UniProt:Q12913 PTPRJ

chain
  • signal peptide:1-35
  • chain:36-1337
checksum B44F4343FC8FD1B4
comment
  • FUNCTION Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2 (PubMed:10821867, PubMed:12062403, PubMed:12370829, PubMed:12475979, PubMed:18348712, PubMed:19494114, PubMed:19922411, PubMed:21262971). Plays a role in cell adhesion, migration, proliferation and differentiation (PubMed:12370829, PubMed:14709717, PubMed:16682945, PubMed:19836242). Has a role in megakaryocytes and platelet formation (PubMed:30591527). Involved in vascular development (By similarity). Regulator of macrophage adhesion and spreading (By similarity). Positively affects cell-matrix adhesion (By similarity). Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation (PubMed:16682945). Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR (PubMed:21091576). Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation (PubMed:18936167). Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation (PubMed:19836242). Enhances the barrier function of epithelial junctions during reassembly (PubMed:19332538). Negatively regulates T-cell receptor (TCR) signaling (PubMed:11259588, PubMed:9531590, PubMed:9780142). 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 (PubMed:11259588, PubMed:12913111).FUNCTION Activates angiogenesis and cell migration (PubMed:28052032). Downregulates the expression of the endothelial adhesion molecules ICAM1 and VCAM1 (PubMed:28052032).CATALYTIC ACTIVITY O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphateSUBUNIT Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2.INTERACTION After T-cell stimulation, it is temporarily excluded from immunological synapses.SUBCELLULAR LOCATION Isoform 1 and isoform 3 result from alternative initiation of translation within the same 5' exon but produce the same functional protein following cleavage of their respective signal peptides (PubMed:18603590). Alternative initiation is probably a conserved mechanism in mammals to regulate the overall expression of that functional protein (PubMed:18603590, PubMed:33296397).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.TISSUE SPECIFICITY Expressed in the brain.PTM N- and O-glycosylated.PTM N-glycosylated.DISEASE The disease is caused by variants affecting the gene represented in this entry.MISCELLANEOUS Expressed in several normal and cancer cell lines, including A549, HUVEC, MCF7, HeLa, A172 and ADF cells (at protein level) (PubMed:28052032). Up-regulated in high-grade glioma samples (PubMed:28052032).SIMILARITY Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily.CAUTION Originally thought to dephosphorylate RET. However this paper was retracted due to manipulation of immunoblot data.
crossReference
databaseName UniProt
dbId 62467
description
  • recommendedName: Receptor-type tyrosine-protein phosphatase eta shortName: Protein-tyrosine phosphatase eta shortName: R-PTP-eta ecNumber: 3.1.3.48 alternativeName: fullName evidence="38"Density-enhanced phosphatase 1 shortName evidence="37"DEP-1 alternativeName: HPTP eta alternativeName: Protein-tyrosine phosphatase receptor type J shortName: R-PTP-J cdAntigenName evidence="41"CD148/cdAntigenName
displayName UniProt:Q12913 PTPRJ
geneName
  • PTPRJ
  • DEP1
identifier Q12913
isSequenceChanged false
keyword
  • 3D-structure
  • Alternative initiation
  • Alternative splicing
  • Angiogenesis
  • Cell junction
  • Cell membrane
  • Cell projection
  • Direct protein sequencing
  • Glycoprotein
  • Hydrolase
  • Membrane
  • Phosphoprotein
  • Protein phosphatase
  • Proteomics identification
  • Reference proteome
  • Repeat
  • Secreted
  • Signal
  • Transmembrane
  • Transmembrane helix
modified [InstanceEdit:9939033] Weiser, Joel, 2025-02-21
moleculeType Protein
name
  • PTPRJ
otherIdentifier
  • 11728971_at
  • 11728972_a_at
  • 11736511_at
  • 11756011_a_at
  • 16724633
  • 1697_s_at
  • 210173_PM_at
  • 210173_at
  • 227396_PM_at
  • 227396_at
  • 3329980
  • 3329984
  • 3329985
  • 3329986
  • 3330038
  • 3330041
  • 3330042
  • 3330043
  • 3330044
  • 3330045
  • 3330046
  • 3330047
  • 3330048
  • 3330050
  • 3330051
  • 3330052
  • 3330053
  • 3330054
  • 3330057
  • 3330058
  • 3330060
  • 3330061
  • 3330064
  • 3330065
  • 3330066
  • 3330068
  • 3330069
  • 3330070
  • 3330071
  • 3330072
  • 3330073
  • 3330074
  • 3330075
  • 3330076
  • 3330077
  • 3330078
  • 3330079
  • 3330080
  • 3330081
  • 3330082
  • 3330083
  • 40583_at
  • 44024_at
  • 5795
  • 73378_at
  • 7939839
  • A_14_P125829
  • A_23_P405049
  • A_24_P282434
  • A_24_P921321
  • A_33_P3309561
  • D37781_s_at
  • GE62543
  • GE852110
  • GO:0001525
  • GO:0001570
  • GO:0001772
  • GO:0001954
  • GO:0002376
  • GO:0003013
  • GO:0003824
  • GO:0004721
  • GO:0004725
  • GO:0005161
  • GO:0005515
  • GO:0005576
  • GO:0005654
  • GO:0005730
  • GO:0005886
  • GO:0005911
  • GO:0006470
  • GO:0007165
  • GO:0007411
  • GO:0007507
  • GO:0007596
  • GO:0008013
  • GO:0008285
  • GO:0009653
  • GO:0009986
  • GO:0010572
  • GO:0010642
  • GO:0010759
  • GO:0016020
  • GO:0016311
  • GO:0016604
  • GO:0016787
  • GO:0016791
  • GO:0019221
  • GO:0019901
  • GO:0030054
  • GO:0030097
  • GO:0030154
  • GO:0030155
  • GO:0030183
  • GO:0030220
  • GO:0030308
  • GO:0030336
  • GO:0032587
  • GO:0032760
  • GO:0035335
  • GO:0035579
  • GO:0042059
  • GO:0042593
  • GO:0042995
  • GO:0043116
  • GO:0043407
  • GO:0043410
  • GO:0045295
  • GO:0045296
  • GO:0045785
  • GO:0046627
  • GO:0048008
  • GO:0048709
  • GO:0048856
  • GO:0050766
  • GO:0050778
  • GO:0050850
  • GO:0050852
  • GO:0050860
  • GO:0050918
  • GO:0051019
  • GO:0051130
  • GO:0051894
  • GO:0051897
  • GO:0051898
  • GO:0060242
  • GO:0060369
  • GO:0065008
  • GO:0070062
  • GO:0070097
  • GO:0070161
  • GO:0140096
  • GO:1902533
  • HMNXSV003026351
  • HMNXSV003044689
  • Hs.306163.0.A1_3p_at
  • ILMN_1731589
  • PH_hs_0010301
  • TC11000412.hg
  • TC11002664.hg
  • U10886_at
  • g633072_3p_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • PTPRJ_HUMAN
  • Q15255
  • Q6P4H4
  • Q8NHM2
  • Q9UDA9
sequenceLength 1337
species [Species:48887] Homo sapiens
stId uniprot:Q12913
url http://purl.uniprot.org/uniprot/Q12913
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