PTPRF

Protein tyrosine phosphatase, receptor type, F, also known as PTPRF, is a human gene.cite web | title = Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5792| accessdate = ]

PBB_Summary
section_title =
summary_text = 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 adherents 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.cite web | title = Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5792| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Chernoff J |title=Protein tyrosine phosphatases as negative regulators of mitogenic signaling. |journal=J. Cell. Physiol. |volume=180 |issue= 2 |pages= 173–81 |year= 1999 |pmid= 10395287 |doi= 10.1002/(SICI)1097-4652(199908)180:2<173::AID-JCP5>3.0.CO;2-Y |doilabel=10.1002/(SICI)1097-4652(199908)180:2173::AID-JCP53.0.CO;2-Y
*cite journal | author=Hashimoto N, Feener EP, Zhang WR, Goldstein BJ |title=Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain. |journal=J. Biol. Chem. |volume=267 |issue= 20 |pages= 13811–4 |year= 1992 |pmid= 1321126 |doi=
*cite journal | author=Jirik FR, Harder KW, Melhado IG, "et al." |title=The gene for leukocyte antigen-related tyrosine phosphatase (LAR) is localized to human chromosome 1p32, a region frequently deleted in tumors of neuroectodermal origin. |journal=Cytogenet. Cell Genet. |volume=61 |issue= 4 |pages= 266–8 |year= 1993 |pmid= 1486801 |doi=
*cite journal | author=Streuli M, Krueger NX, Thai T, "et al." |title=Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. |journal=EMBO J. |volume=9 |issue= 8 |pages= 2399–407 |year= 1990 |pmid= 1695146 |doi=
*cite journal | author=Streuli M, Krueger NX, Tsai AY, Saito H |title=A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 22 |pages= 8698–702 |year= 1989 |pmid= 2554325 |doi=
*cite journal | author=Streuli M, Krueger NX, Hall LR, "et al." |title=A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen. |journal=J. Exp. Med. |volume=168 |issue= 5 |pages= 1523–30 |year= 1988 |pmid= 2972792 |doi=
*cite journal | author=Harder KW, Saw J, Miki N, Jirik F |title=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. |journal=Genomics |volume=27 |issue= 3 |pages= 552–3 |year= 1995 |pmid= 7558042 |doi= 10.1006/geno.1995.1092
*cite journal | author=Schaapveld RQ, van den Maagdenberg AM, Schepens JT, "et al." |title=The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization. |journal=Genomics |volume=27 |issue= 1 |pages= 124–30 |year= 1995 |pmid= 7665159 |doi=
*cite journal | author=Serra-Pagès C, Kedersha NL, Fazikas L, "et al." |title=The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions. |journal=EMBO J. |volume=14 |issue= 12 |pages= 2827–38 |year= 1995 |pmid= 7796809 |doi=
*cite journal | author=O'Grady P, Krueger NX, Streuli M, Saito H |title=Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains. |journal=J. Biol. Chem. |volume=269 |issue= 40 |pages= 25193–9 |year= 1994 |pmid= 7929208 |doi=
*cite journal | author=Pulido R, Serra-Pagès C, Tang M, Streuli M |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 25 |pages= 11686–90 |year= 1996 |pmid= 8524829 |doi=
*cite journal | author=Liu X, Vega QC, Decker RA, "et al." |title=Oncogenic RET receptors display different autophosphorylation sites and substrate binding specificities. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5309–12 |year= 1996 |pmid= 8621380 |doi=
*cite journal | author=Debant A, Serra-Pagès C, Seipel K, "et al." |title=The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 11 |pages= 5466–71 |year= 1996 |pmid= 8643598 |doi=
*cite journal | author=Zhang WR, Li PM, Oswald MA, Goldstein BJ |title=Modulation of insulin signal transduction by eutopic overexpression of the receptor-type protein-tyrosine phosphatase LAR. |journal=Mol. Endocrinol. |volume=10 |issue= 5 |pages= 575–84 |year= 1996 |pmid= 8732688 |doi=
*cite journal | author=Tabiti K, Cui L, Chhatwal VJ, "et al." |title=Novel alternative splicing predicts a secreted extracellular isoform of the human receptor-like protein tyrosine phosphatase LAR. |journal=Gene |volume=175 |issue= 1-2 |pages= 7–13 |year= 1996 |pmid= 8917069 |doi=
*cite journal | author=Ahmad F, Goldstein BJ |title=Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells. |journal=J. Biol. Chem. |volume=272 |issue= 1 |pages= 448–57 |year= 1997 |pmid= 8995282 |doi=
*cite journal | author=Aicher B, Lerch MM, Müller T, "et al." |title=Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing. |journal=J. Cell Biol. |volume=138 |issue= 3 |pages= 681–96 |year= 1997 |pmid= 9245795 |doi=
*cite journal | author=Serra-Pagès C, Medley QG, Tang M, "et al." |title=Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins. |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15611–20 |year= 1998 |pmid= 9624153 |doi=
*cite journal | author=O'Grady P, Thai TC, Saito H |title=The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. |journal=J. Cell Biol. |volume=141 |issue= 7 |pages= 1675–84 |year= 1998 |pmid= 9647658 |doi=
*cite journal | author=Chiplunkar S, Chamblis K, Chwa M, "et al." |title=Enhanced expression of a transmembrane phosphotyrosine phosphatase (LAR) in keratoconus cultures and corneas. |journal=Exp. Eye Res. |volume=68 |issue= 3 |pages= 283–93 |year= 1999 |pmid= 10079136 |doi= 10.1006/exer.1998.0604

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