PTPN18

PTPN18
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2OC3, 4GFU, 4GFV, 4NND
Identifiers
Aliases	PTPN18, BDP1, PTP-HSCF, protein tyrosine phosphatase, non-receptor type 18, protein tyrosine phosphatase non-receptor type 18
External IDs	OMIM: 606587; MGI: 108410; HomoloGene: 74971; GeneCards: PTPN18; OMA:PTPN18 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q21.1 Start 130,356,045 bp End 130,375,405 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 B|1 13.25 cM Start 34,498,843 bp End 34,514,814 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte monocyte right uterine tube mucosa of transverse colon rectum cerebellar hemisphere right hemisphere of cerebellum spleen tendon of biceps brachii body of pancreas Top expressed in granulocyte thymus blood spleen mesenteric lymph nodes submandibular gland tibiofemoral joint duodenum lacrimal gland primary oocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding non-membrane spanning protein tyrosine phosphatase activity phosphatase activity phosphoprotein phosphatase activity hydrolase activity protein tyrosine phosphatase activity Cellular component nucleus cytoplasm cytosol nucleoplasm Biological process protein dephosphorylation peptidyl-tyrosine dephosphorylation dephosphorylation ERBB2 signaling pathway negative regulation of ERBB signaling pathway cellular response to cytokine stimulus blastocyst formation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 26469 19253 Ensembl ENSG00000072135 ENSMUSG00000026126 UniProt Q99952 Q61152 RefSeq (mRNA) NM_001142370 NM_014369 NM_011206 RefSeq (protein) NP_001135842 NP_055184 NP_035336 Location (UCSC) Chr 2: 130.36 – 130.38 Mb Chr 1: 34.5 – 34.51 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Tyrosine-protein phosphatase non-receptor type 18 is an enzyme that in humans is encoded by the PTPN18 gene.

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.

Interactions

PTPN18 has been shown to interact with PSTPIP1.

Further reading

• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.