[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/ptpn18-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/ptpn18-wikipedia\/","headline":"PTPN18 – Wikipedia","name":"PTPN18 – Wikipedia","description":"From Wikipedia, the free encyclopedia Protein-coding gene in the species Homo sapiens Tyrosine-protein phosphatase non-receptor type 18 is an enzyme","datePublished":"2021-06-14","dateModified":"2021-06-14","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/b\/b6\/PDB_2oc3_EBI.png\/180px-PDB_2oc3_EBI.png","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/b\/b6\/PDB_2oc3_EBI.png\/180px-PDB_2oc3_EBI.png","height":"135","width":"180"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/ptpn18-wikipedia\/","about":["Wiki"],"wordCount":4378,"articleBody":"From Wikipedia, the free encyclopediaProtein-coding gene in the species Homo sapiensTyrosine-protein phosphatase non-receptor type 18 is an enzyme that in humans is encoded by the PTPN18 gene.[5][6]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.[6]Interactions[edit]PTPN18 has been shown to interact with PSTPIP1.[7]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000072135 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026126 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ 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\u20139. PMID\u00a08950995.^ a b “Entrez Gene: PTPN18 protein tyrosine phosphatase, non-receptor type 18 (brain-derived)”.^ 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\u2013associated Protein that Is a Substrate for a PEST Tyrosine Phosphatase”. J. Cell Biol. UNITED STATES. 138 (4): 845\u201360. doi:10.1083\/jcb.138.4.845. ISSN\u00a00021-9525. PMC\u00a02138048. PMID\u00a09265651.Further reading[edit]Spencer S, Dowbenko D, Cheng J,  et\u00a0al. (1997). “PSTPIP: A Tyrosine Phosphorylated Cleavage Furrow\u2013associated Protein that Is a Substrate for a PEST Tyrosine Phosphatase”. J. Cell Biol. 138 (4): 845\u201360. doi:10.1083\/jcb.138.4.845. PMC\u00a02138048. PMID\u00a09265651.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\u201396. doi:10.1074\/jbc.273.2.989. PMID\u00a09422760.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\u201396. doi:10.1074\/jbc.273.46.30487. PMID\u00a09804817.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\u201388. doi:10.1128\/MCB.21.4.1077-1088.2001. PMC\u00a099562. PMID\u00a011158295.Cong F, Spencer S, C\u00f4t\u00e9 JF,  et\u00a0al. (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\u201323. doi:10.1016\/S1097-2765(00)00138-6. PMID\u00a011163214.Wise CA, Gillum JD, Seidman CE,  et\u00a0al. (2003). “Mutations in CD2BP1 disrupt binding to PTP PEST and are responsible for PAPA syndrome, an autoinflammatory disorder”. Hum. Mol. Genet. 11 (8): 961\u20139. doi:10.1093\/hmg\/11.8.961. PMID\u00a011971877.Strausberg RL, Feingold EA, Grouse LH,  et\u00a0al. (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\u2013903. Bibcode:2002PNAS…9916899M. doi:10.1073\/pnas.242603899. PMC\u00a0139241. PMID\u00a012477932.Shiota M, Tanihiro T, Nakagawa Y,  et\u00a0al. (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\u201349. doi:10.1210\/me.2002-0187. PMID\u00a012554790.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\u20136. doi:10.1074\/jbc.M309527200. PMID\u00a014660651.Blanchetot C, Chagnon M, Dub\u00e9 N,  et\u00a0al. (2005). “Substrate-trapping techniques in the identification of cellular PTP targets”. Methods. 35 (1): 44\u201353. doi:10.1016\/j.ymeth.2004.07.007. PMID\u00a015588985.Zhang Y, Wolf-Yadlin A, Ross PL,  et\u00a0al. (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\u201350. doi:10.1074\/mcp.M500089-MCP200. PMID\u00a015951569.Tao WA, Wollscheid B, O’Brien R,  et\u00a0al. (2005). “Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry”. Nat. Methods. 2 (8): 591\u20138. doi:10.1038\/nmeth776. PMID\u00a016094384. S2CID\u00a020475874.Gandhi TK, Chandran S, Peri S,  et\u00a0al. (2007). “A bioinformatics analysis of protein tyrosine phosphatases in humans”. DNA Res. 12 (2): 79\u201389. doi:10.1093\/dnares\/12.2.79. PMID\u00a016303740.PDB gallery2oc3: Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 18  "},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/ptpn18-wikipedia\/#breadcrumbitem","name":"PTPN18 – Wikipedia"}}]}]