Recombinant human PTP epsilon protein (ab128555)

General Info

• Alternative names
  • DKFZp313F1310
  • FLJ57799
  • FLJ58245

  • HPTPE
  • Protein tyrosine phosphatase epsilon
  • Protein tyrosine phosphatase receptor type E
  • Protein tyrosine phosphatase receptor type epsilon
  • Protein tyrosine phosphatase receptor type epsilon polypeptide
  • Protein-tyrosine phosphatase epsilon
  • PTPE
  • Ptpre
  • PTPRE_HUMAN
  • R PTP Epsilon
  • R-PTP-epsilon
  • Receptor-type tyrosine-protein phosphatase epsilon

  see all
• Function
  Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function.
  Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake.
  Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+).
• Tissue specificity
  Expressed in giant cell tumor (osteoclastoma rich in multinucleated osteoclastic cells).
• Sequence similarities
  Belongs to the protein-tyrosine phosphatase family. Receptor class 4 subfamily.
  Contains 2 tyrosine-protein phosphatase domains.
• Domain
  The tyrosine-protein phosphatase 2 domain (D2) mediates dimerization. The extreme N- and C- termini of the D2 domain act to inhibit dimerization and removal of these sequences increases dimerization and inhibits enzyme activity.
• Post-translational
  modifications
  A catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3.
  Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu.
  Isoform 1 is glycosylated.
• Cellular localization
  Cytoplasm; Cell membrane and Cytoplasm. Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin induces translocation to the membrane.

• Target information above from: UniProt accession P23469 The UniProt Consortium
  The Universal Protein Resource (UniProt) in 2010
  Nucleic Acids Res. 38:D142-D148 (2010) .

  Information by UniProt