Selected-GenAtlas references SOURCE GeneCards NCBI Gene Swiss-Prot Ensembl
HGNC UniGene Nucleotide OMIM UCSC
Home Page
FLASH GENE
Symbol PTPRJ contributors: shn/npt/pgu - updated : 08-02-2016
HGNC name protein tyrosine phosphatase, receptor type, J
HGNC id 9673
EXPRESSION
Type widely
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Lymphoid/Immunethymus     Homo sapiens
Nervousbrain    
Reproductivefemale systembreast    Homo sapiens
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Blood / hematopoietic   predominantly
Connectivebone   
Epithelial   predominantly
cells
SystemCellPubmedSpeciesStageRna symbol
Blood/Hematopoieticplatelet Homo sapiens
Lymphoid/ImmuneT cell Homo sapiens
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • an extracellular segment containing eight fibronectin type III repeats
  • a single intracellular catalytic domain
  • a transmembrane domain
  • a single intracellular protein-tyrosine phosphatase (PTP) domain
  • a short C-terminal tail containing three conserved tyrosine residues
    • HOMOLOGY
    interspecies ortholog to Ptprj, murine
    ortholog to PTPRJ, Pan troglodytes
    ortholog to Ptprj, Rattus norvegicus
    Homologene
    FAMILY
  • protein tyrosine phosphatase (PTP) family
  • R3 family receptor-like PTP
    • CATEGORY enzyme , receptor
    SUBCELLULAR LOCALIZATION     plasma membrane,junction
    basic FUNCTION
  • may be contributing to the mechanism of contact inhibition of cell growth
  • inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients
  • may act as a tumor suppressor
  • DEP-1 contributes to the contact inhibition of endothelial cell growth via dephosphorylation of vascular endothelial growth factor receptor 2
  • positive regulator of VEGF mediated Src and Akt activation and endothelial cell survival
  • implicated in cell growth and differentiation as well as in regulating phosphorylation of junctional proteins
  • can modify the phosphorylation state of tight junction proteins and play a role in regulating permeability
  • enhances platelet responsiveness to collagen by maintaining a pool of active Src family kinases
  • receptor-like protein-tyrosine phosphatase known to inhibit transduction of mitogenic signals in non-hematopoietic cells, and in in the hematopoietic lineage, inhibited signal transduction downstream of T cell receptor
  • also plays an activating role via dephosphorylation of the inhibitory tyrosine in SRC
  • negative regulator of TCR signaling, which is in apparent contradiction with data obtained from other leukocyte populations
  • able to activate Src Family Kinases involved in TCR signal transduction
  • may regulate differentiation of normal mammary epithelia and dysregulation of protein localisation may be associated with tumorigenesis
  • plays a dominant role in activating SRC family kinases in platelets relative to PTPN1, and both PTPs are required for optimal platelet activation and aggregate formation under high arterial shear rates
  • promotes airway hyperresponsiveness through SRC family kinases
  • PTPRC and PTPRJ are transmembrane tyrosine phosphatases with large ectodomains that have activatory and inhibitory effects on TCR triggering
  • positively regulates SRC family kinases and critical biological functions in endothelial and hematopoietic cells
  • receptor-like protein tyrosine phosphatase mainly known for its antiproliferative and tumor-suppressive functions
  • role as a mediator of an invasive cell program implicating SRC activation and the promotion of breast cancer progression
    • CELLULAR PROCESS cell life, proliferation/growth
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    PTPRJ regulates negatively T cell receptor signaling possibly through interfering with the phosphorylation of Phospholipase C Gamma 1 and Linker for Activation of T Cells. This protein can also dephosphorylate the PDGF beta receptor, and may be involved in UV-induced signal transduction
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • VEGFR2
  • may interact with and dephosphorylate PIK3CD when it is phosphorylated and modulate the magnitude of PI3K activity
    • EGFR and PTPRJ physically interact at the cell surface and maintain bidirectional enzyme-substrate interactions, which are relevant to their respective oncogenic and tumor-suppressive functions
  • interaction with occludin and TJP1 specific (occludin and TJP1 were dephosphorylated by PTPRJ but not the other phosphatases)
  • PTP negatively regulating FLT3 phosphorylation and signaling
  • PTPRJ is negatively regulating FLT3 signaling activity and its loss may contribute to but is not sufficient for leukemogenic cell transformation
  • SDC2 is a novel ligand for the protein tyrosine phosphatase receptor PTPRJ
  • functions as a receptor for THBS1 and mediates its inhibition of cell growth
  • direct interaction of PTPRJ with the hematopoietic receptor-tyrosine kinase Fms-like tyrosine kinase-3 (FLT3)
    • cell & other
    REGULATION
    Other phosphorylation of on threonine 1318 regulates SRC activation and endothelial cell permeability induced by vascular endothelial growth factor
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral   deletion    
    in colorectal, lung and breast cancer.
    tumoral     --low  
    may contribute to but is not sufficient for leukemogenic cell transformation (
    Susceptibility to breast cancer
    Variant & Polymorphism
    Candidate gene candidate tumor suppressor in the colon epithelium
    Marker
    Therapy target upregulation of PTPRJ expression, and in turn inhibition of cell growth and migration may present a previously unrecognized mechanism of chemoprevention by nutrients
    ANIMAL & CELL MODELS
    Cd148-deficient mouse platelets exhibited reduced collagen-mediated aggregation, secretion and spreading in association with reduced expression of GPVI and FcR gamma-chain and reduced tyrosine phosphorylation