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External IDsGeneCards: [1]
RefSeq (mRNA)



RefSeq (protein)



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Receptor-type tyrosine-protein phosphatase F is an enzyme that in humans is encoded by the PTPRF gene.[1][2]

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. 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 possesses an extracellular region, a single transmembrane region, and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains three Ig-like domains, and nine non-Ig like domains similar to that of neural cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell–cell contacts at adherens junctions, as well as in the control of beta-catenin signaling. An increased expression level of this protein was found in the insulin-responsive tissue of obese, insulin-resistant individuals, and may contribute to the pathogenesis of insulin resistance. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.[2]


PTPRF has been shown to interact with Beta-catenin[3][4] and liprin-alpha-1.[5][6][7]


  1. Harder KW, Saw J, Miki N, Jirik F (Nov 1995). "Coexisting amplifications of the chromosome 1p32 genes (PTPRF and MYCL1) encoding protein tyrosine phosphatase LAR and L-myc in a small cell lung cancer line". Genomics. 27 (3): 552–3. doi:10.1006/geno.1995.1092. PMID 7558042.
  2. 2.0 2.1 "Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F".
  3. Bonvini P, An WG, Rosolen A, Nguyen P, Trepel J, Garcia de Herreros A, Dunach M, Neckers LM (Feb 2001). "Geldanamycin abrogates ErbB2 association with proteasome-resistant beta-catenin in melanoma cells, increases beta-catenin-E-cadherin association, and decreases beta-catenin-sensitive transcription". Cancer Res. 61 (4): 1671–7. PMID 11245482.
  4. Aicher B, Lerch MM, Müller T, Schilling J, Ullrich A (Aug 1997). "Cellular Redistribution of Protein Tyrosine Phosphatases LAR and PTPσ by Inducible Proteolytic Processing". J. Cell Biol. 138 (3): 681–96. doi:10.1083/jcb.138.3.681. PMC 2141638. PMID 9245795.
  5. Pulido R, Serra-Pagès C, Tang M, Streuli M (Dec 1995). "The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1". Proc. Natl. Acad. Sci. U.S.A. 92 (25): 11686–90. doi:10.1073/pnas.92.25.11686. PMC 40467. PMID 8524829.
  6. Serra-Pagès C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M (Jun 1995). "The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions". EMBO J. 14 (12): 2827–38. PMC 398401. PMID 7796809.
  7. Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M (Jun 1998). "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611–20. doi:10.1074/jbc.273.25.15611. PMID 9624153.

Further reading