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PTPN14

{{Short description|Protein-coding gene in the species Homo sapiens}}

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Tyrosine-protein phosphatase non-receptor type 14 is an enzyme that in humans is encoded by the PTPN14 gene.{{cite journal | vauthors = Smith AL, Mitchell PJ, Shipley J, Gusterson BA, Rogers MV, Crompton MR | title = Pez: a novel human cDNA encoding protein tyrosine phosphatase- and ezrin-like domains | journal = Biochemical and Biophysical Research Communications | volume = 209 | issue = 3 | pages = 959–65 | date = Apr 1995 | pmid = 7733990 | doi = 10.1006/bbrc.1995.1591 }}{{cite web | title = Entrez Gene: PTPN14 protein tyrosine phosphatase, non-receptor type 14| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5784}}

Function

The protein encoded by this gene is a member of the PTP family and [http://phosphatome.net/wiki/index.php/Phosphatase_Subfamily_PTPN14 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.

Interactions

PTPN14 has been shown to interact with Beta-catenin.{{cite journal | vauthors = Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y | title = The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin | journal = Molecular Biology of the Cell | volume = 14 | issue = 6 | pages = 2520–9 | date = Jun 2003 | pmid = 12808048 | pmc = 194899 | doi = 10.1091/mbc.E02-09-0577 }}

References

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Further reading

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  • {{cite journal | vauthors = Gyapay G, Morissette J, Vignal A, Dib C, Fizames C, Millasseau P, Marc S, Bernardi G, Lathrop M, Weissenbach J | title = The 1993-94 Généthon human genetic linkage map | journal = Nature Genetics | volume = 7 | issue = 2 Spec No | pages = 246–339 | date = Jun 1994 | pmid = 7545953 | doi = 10.1038/ng0694supp-246 | s2cid = 24662426 }}
  • {{cite journal | vauthors = Ogata M, Takada T, Mori Y, Oh-hora M, Uchida Y, Kosugi A, Miyake K, Hamaoka T | title = Effects of overexpression of PTP36, a putative protein tyrosine phosphatase, on cell adhesion, cell growth, and cytoskeletons in HeLa cells | journal = The Journal of Biological Chemistry | volume = 274 | issue = 18 | pages = 12905–9 | date = Apr 1999 | pmid = 10212280 | doi = 10.1074/jbc.274.18.12905 | doi-access = free }}
  • {{cite journal | vauthors = Ogata M, Takada T, Mori Y, Uchida Y, Miki T, Okuyama A, Kosugi A, Sawada M, Oh-hora M, Hamaoka T | title = Regulation of phosphorylation level and distribution of PTP36, a putative protein tyrosine phosphatase, by cell-substrate adhesion | journal = The Journal of Biological Chemistry | volume = 274 | issue = 29 | pages = 20717–24 | date = Jul 1999 | pmid = 10400706 | doi = 10.1074/jbc.274.29.20717 | doi-access = free }}
  • {{cite journal | vauthors = Aoyama K, Matsuda T, Aoki N | title = Characterization of newly identified four isoforms for a putative cytosolic protein tyrosine phosphatase PTP36 | journal = Biochemical and Biophysical Research Communications | volume = 266 | issue = 2 | pages = 523–31 | date = Dec 1999 | pmid = 10600535 | doi = 10.1006/bbrc.1999.1845 }}
  • {{cite journal | vauthors = Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y | title = Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation | journal = Journal of Cell Science | volume = 113 ( Pt 17) | issue = 17 | pages = 3117–23 | date = Sep 2000 | doi = 10.1242/jcs.113.17.3117 | pmid = 10934049 | hdl = 2440/9579 | hdl-access = free }}
  • {{cite journal | vauthors = Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y | title = The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin | journal = Molecular Biology of the Cell | volume = 14 | issue = 6 | pages = 2520–9 | date = Jun 2003 | pmid = 12808048 | pmc = 194899 | doi = 10.1091/mbc.E02-09-0577 }}
  • {{cite journal | vauthors = 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 | title = Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization | journal = Current Biology | volume = 14 | issue = 16 | pages = 1436–50 | date = Aug 2004 | pmid = 15324660 | doi = 10.1016/j.cub.2004.07.051 | s2cid = 2371325 | doi-access = free | bibcode = 2004CBio...14.1436J }}
  • {{cite journal | vauthors = Barr AJ, Debreczeni JE, Eswaran J, Knapp S | title = Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-A resolution | journal = Proteins | volume = 63 | issue = 4 | pages = 1132–6 | date = Jun 2006 | pmid = 16534812 | doi = 10.1002/prot.20958 | s2cid = 7186900 | doi-access = free }}
  • {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = Nov 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 | s2cid = 7827573 | doi-access = free }}

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External links

  • [https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/Q15678 PDBe-KB] provides an overview of all the structure information available in the PDB for Human Tyrosine-protein phosphatase non-receptor type 14 (PTPN14)

{{PDB Gallery|geneid=5784}}

{{Protein tyrosine phosphatases}}

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