PTPN14

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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Tyrosine-protein phosphatase non-receptor type 14 is an enzyme that in humans is encoded by the PTPN14 gene.[1][2]

Function

The protein encoded by this gene is a member of the PTP family and PTPN14 subfamily of tyrosine protein phosphatases. PTPs are known to be signalling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an N-terminal noncatalytic domain similar to that of band 4.1 superfamily cytoskeleton-associated proteins, which suggested the membrane or cytoskeleton localization of this protein. The specific function of this PTP has not yet been determined.[2]

Interactions

PTPN14 has been shown to interact with Beta-catenin.[3]

References

  1. Smith AL, Mitchell PJ, Shipley J, Gusterson BA, Rogers MV, Crompton MR (Apr 1995). "Pez: a novel human cDNA encoding protein tyrosine phosphatase- and ezrin-like domains". Biochemical and Biophysical Research Communications. 209 (3): 959–65. doi:10.1006/bbrc.1995.1591. PMID 7733990.
  2. 2.0 2.1 "Entrez Gene: PTPN14 protein tyrosine phosphatase, non-receptor type 14".
  3. Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y (Jun 2003). "The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin". Molecular Biology of the Cell. 14 (6): 2520–9. doi:10.1091/mbc.E02-09-0577. PMC 194899. PMID 12808048.

Further reading

  • Gyapay G, Morissette J, Vignal A, Dib C, Fizames C, Millasseau P, Marc S, Bernardi G, Lathrop M, Weissenbach J (Jun 1994). "The 1993-94 Généthon human genetic linkage map". Nature Genetics. 7 (2 Spec No): 246–339. doi:10.1038/ng0694supp-246. PMID 7545953.
  • Ogata M, Takada T, Mori Y, Oh-hora M, Uchida Y, Kosugi A, Miyake K, Hamaoka T (Apr 1999). "Effects of overexpression of PTP36, a putative protein tyrosine phosphatase, on cell adhesion, cell growth, and cytoskeletons in HeLa cells". The Journal of Biological Chemistry. 274 (18): 12905–9. doi:10.1074/jbc.274.18.12905. PMID 10212280.
  • Ogata M, Takada T, Mori Y, Uchida Y, Miki T, Okuyama A, Kosugi A, Sawada M, Oh-hora M, Hamaoka T (Jul 1999). "Regulation of phosphorylation level and distribution of PTP36, a putative protein tyrosine phosphatase, by cell-substrate adhesion". The Journal of Biological Chemistry. 274 (29): 20717–24. doi:10.1074/jbc.274.29.20717. PMID 10400706.
  • Aoyama K, Matsuda T, Aoki N (Dec 1999). "Characterization of newly identified four isoforms for a putative cytosolic protein tyrosine phosphatase PTP36". Biochemical and Biophysical Research Communications. 266 (2): 523–31. doi:10.1006/bbrc.1999.1845. PMID 10600535.
  • Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y (Sep 2000). "Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation". Journal of Cell Science. 113 ( Pt 17) (17): 3117–23. PMID 10934049.
  • Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y (Jun 2003). "The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin". Molecular Biology of the Cell. 14 (6): 2520–9. doi:10.1091/mbc.E02-09-0577. PMC 194899. PMID 12808048.
  • Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
  • Barr AJ, Debreczeni JE, Eswaran J, Knapp S (Jun 2006). "Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-A resolution". Proteins. 63 (4): 1132–6. doi:10.1002/prot.20958. PMID 16534812.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.