PTPN18
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Template:Short description An Error has occurred retrieving Wikidata item for infobox Tyrosine-protein phosphatase non-receptor type 18 is an enzyme that in humans is encoded by the PTPN18 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 a PEST motif, which often serves as a protein-protein interaction domain, and may be related to protein intracellular half-life. This gene was found to be expressed in brain, colon tissues, and several different tumor-derived cell lines. The biological function of this PTP has not yet been determined.[2]
Interactions
PTPN18 has been shown to interact with PSTPIP1.[3]
References
Page Template:Reflist/styles.css has no content.
- ^ Page Module:Citation/CS1/styles.css has no content.Kim YW, Wang H, Sures I, Lammers R, Martell KJ, Ullrich A (January 1997). "Characterization of the PEST family protein tyrosine phosphatase BDP1". Oncogene. 13 (10): 2275–9. PMID 8950995.
- ^ a b Page Module:Citation/CS1/styles.css has no content."Entrez Gene: PTPN18 protein tyrosine phosphatase, non-receptor type 18 (brain-derived)".
- ^ Page Module:Citation/CS1/styles.css has no content.Spencer, S; Dowbenko D; Cheng J; Li W; Brush J; Utzig S; Simanis V; Lasky L A (August 1997). "PSTPIP: A Tyrosine Phosphorylated Cleavage Furrow–associated Protein that Is a Substrate for a PEST Tyrosine Phosphatase". J. Cell Biol. 138 (4). UNITED STATES: 845–60. doi:10.1083/jcb.138.4.845. ISSN 0021-9525. PMC 2138048. PMID 9265651.
Further reading
Page Template:Refbegin/styles.css has no content.
- Page Module:Citation/CS1/styles.css has no content.Spencer S, Dowbenko D, Cheng J, et al. (1997). "PSTPIP: A Tyrosine Phosphorylated Cleavage Furrow–associated Protein that Is a Substrate for a PEST Tyrosine Phosphatase". J. Cell Biol. 138 (4): 845–60. doi:10.1083/jcb.138.4.845. PMC 2138048. PMID 9265651.
- Page Module:Citation/CS1/styles.css has no content.Dowbenko D, Spencer S, Quan C, Lasky LA (1998). "Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein". J. Biol. Chem. 273 (2): 989–96. doi:10.1074/jbc.273.2.989. PMID 9422760.
- Page Module:Citation/CS1/styles.css has no content.Wu Y, Dowbenko D, Lasky LA (1998). "PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase". J. Biol. Chem. 273 (46): 30487–96. doi:10.1074/jbc.273.46.30487. PMID 9804817.
- Page Module:Citation/CS1/styles.css has no content.Wang B, Lemay S, Tsai S, Veillette A (2001). "SH2 Domain-Mediated Interaction of Inhibitory Protein Tyrosine Kinase Csk with Protein Tyrosine Phosphatase-HSCF". Mol. Cell. Biol. 21 (4): 1077–88. doi:10.1128/MCB.21.4.1077-1088.2001. PMC 99562. PMID 11158295.
- Page Module:Citation/CS1/styles.css has no content.Cong F, Spencer S, Côté JF, et al. (2001). "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation". Mol. Cell. 6 (6): 1413–23. doi:10.1016/S1097-2765(00)00138-6. PMID 11163214.
- Page Module:Citation/CS1/styles.css has no content.Wise CA, Gillum JD, Seidman CE, et al. (2003). "Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible for PAPA syndrome, an autoinflammatory disorder". Hum. Mol. Genet. 11 (8): 961–9. doi:10.1093/hmg/11.8.961. PMID 11971877.
- Page Module:Citation/CS1/styles.css has no content.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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Page Module:Citation/CS1/styles.css has no content.Shiota M, Tanihiro T, Nakagawa Y, et al. (2004). "Protein tyrosine phosphatase PTP20 induces actin cytoskeleton reorganization by dephosphorylating p190 RhoGAP in rat ovarian granulosa cells stimulated with follicle-stimulating hormone". Mol. Endocrinol. 17 (4): 534–49. doi:10.1210/me.2002-0187. PMID 12554790.
- Page Module:Citation/CS1/styles.css has no content.Gensler M, Buschbeck M, Ullrich A (2004). "Negative regulation of HER2 signaling by the PEST-type protein-tyrosine phosphatase BDP1". J. Biol. Chem. 279 (13): 12110–6. doi:10.1074/jbc.M309527200. PMID 14660651.
- Page Module:Citation/CS1/styles.css has no content.Blanchetot C, Chagnon M, Dubé N, et al. (2005). "Substrate-trapping techniques in the identification of cellular PTP targets". Methods. 35 (1): 44–53. doi:10.1016/j.ymeth.2004.07.007. PMID 15588985.
- Page Module:Citation/CS1/styles.css has no content.Zhang Y, Wolf-Yadlin A, Ross PL, et al. (2005). "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules". Mol. Cell. Proteomics. 4 (9): 1240–50. doi:10.1074/mcp.M500089-MCP200. PMID 15951569.
- Page Module:Citation/CS1/styles.css has no content.Tao WA, Wollscheid B, O'Brien R, et al. (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nat. Methods. 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384. S2CID 20475874.
- Page Module:Citation/CS1/styles.css has no content.Gandhi TK, Chandran S, Peri S, et al. (2007). "A bioinformatics analysis of protein tyrosine phosphatases in humans". DNA Res. 12 (2): 79–89. doi:10.1093/dnares/12.2.79. PMID 16303740.
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