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PTPN1 - protein tyrosine phosphatase, non-receptor type 1
Entrez Gene Name: protein tyrosine phosphatase, non-receptor type 1
Synonyms: MGC93562, PROTEIN-TYROSINE PHOSPHATASE, PTP, PTP-1B, PTP-HA2, PTP1B ALPHA, PTP1BB, Ptpase 1, PTPASE 1B, PTPASE HA2, PTPN1

Gene Summary

  • Human (5770): The protein encoded by this gene is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP has been shown to act as a negative regulator of insulin signaling by dephosphorylating the phosphotryosine residues of insulin receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, and cell response to interferon stimulation. [provided by RefSeq]
  • Rat (24697): protein-tyrosine-phosphatase which has only phosphotyrosine phosphatase activity [RGD]

Cell Regulation

Regulates:
  • INSR
  • SRC
  • IRS1
View all 107 in IPA
Regulated by:
  • INSR
  • troglitazone
  • cyclic AMP
View all 113 in IPA
Binds:
  • INSR
  • PDGFRB
  • EPOR
View all 67 in IPA
Role in cell:
  • apoptosis
  • migration
  • proliferation
View all 20 in IPA
Disease:
  • Waldenstrom's macroglobulinemia
  • bipolar affective disorder
  • lymphoid cancer
View all 8 in IPA

Biological Process

dephosphorylation, insulin receptor signaling pathway, negative regulation of insulin receptor signaling pathway, protein amino acid dephosphorylation, regulation of insulin receptor signaling pathway, signal transduction

Cellular Components

anchored to membrane, cytoplasmic vesicle, cytosol, endoplasmic reticulum, endoplasmic reticulum membrane, insoluble fraction, membrane

Literature References

  • 18467448Picardi PK, Calegari VC, de Oliveira Prada P, Contin Moraes J, Araújo E, Gomes Marcondes MC, Ueno M, Carvalheira JB, Velloso LA, Abdalla Saad MJ. Reduction of hypothalamic protein tyrosine phosphatase improves insulin and leptin resistance in diet-induced obese rats.Endocrinology 2008 Aug 01;149(8):3870-80
  • 18451337Nakamura Y, Patrushev N, Inomata H, Mehta D, Urao N, Kim HW, Razvi M, Kini V, Mahadev K, Goldstein BJ, McKinney R, Fukai T, Ushio-Fukai M. Role of Protein Tyrosine Phosphatase 1B in Vascular Endothelial Growth Factor Signaling and Cell-Cell Adhesions in Endothelial Cells.Circ Res 2008 May 23;102(10):1182-91
  • 17974954Zhu S, Bjorge JD, Fujita DJ. PTP1B Contributes to the Oncogenic Properties of Colon Cancer Cells through Src Activation.Cancer Res 2007 Nov 01;67(21):10129-37
  • View 1061 categorized literature findings and their references in IPA

Molecular Functions

hydrolase activity, insulin receptor binding, phosphatase activity, phosphoprotein phosphatase activity, protein binding, protein tyrosine phosphatase activity, receptor activity, zinc ion binding

Protein Domains

catalytic domain, insulin receptor binding, phosphatase, protein binding, protein-tyrosine-phoshatase, PTPase domain, zinc ion binding

Subcellular Locations

cellular membrane, cytoplasm, cytosolic fraction, endoplasmic reticulum, endoplasmic reticulum membrane