PTPN14
Tyrosine-protein phosphatase non-receptor type 14 is an enzyme that in humans is encoded by the PTPN14 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 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
Further reading
- Gyapay G; Morissette J; Vignal A et al. (1994). "The 1993-94 Généthon human genetic linkage map". Nat. Genet. 7 (2 Spec No): 246–339. doi:10.1038/ng0694supp-246. PMID 7545953.
- Ogata M; Takada T; Mori Y et al. (1999). "Effects of overexpression of PTP36, a putative protein tyrosine phosphatase, on cell adhesion, cell growth, and cytoskeletons in HeLa cells". J. Biol. Chem. 274 (18): 12905–9. doi:10.1074/jbc.274.18.12905. PMID 10212280.
- Ogata M; Takada T; Mori Y et al. (1999). "Regulation of phosphorylation level and distribution of PTP36, a putative protein tyrosine phosphatase, by cell-substrate adhesion". J. Biol. Chem. 274 (29): 20717–24. doi:10.1074/jbc.274.29.20717. PMID 10400706.
- Aoyama K, Matsuda T, Aoki N (2000). "Characterization of newly identified four isoforms for a putative cytosolic protein tyrosine phosphatase PTP36". Biochem. Biophys. Res. Commun. 266 (2): 523–31. doi:10.1006/bbrc.1999.1845. PMID 10600535.
- Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y (2000). "Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation". J. Cell. Sci. 113 (17): 3117–23. PMID 10934049.
- Strausberg RL; Feingold EA; Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y (2004). "The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin". Mol. Biol. Cell 14 (6): 2520–9. doi:10.1091/mbc.E02-09-0577. PMC 194899. PMID 12808048.
- Ota T; Suzuki Y; Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Jin J; Smith FD; Stark C et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
- Barr AJ, Debreczeni JE, Eswaran J, Knapp S (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 et al. (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.
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| | 2bzl: CRYSTAL STRUCTURE OF THE HUMAN PROTEIN TYROSINE PHOSPHATASE N14 AT 1.65 A RESOLUTION |
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