PTPN3

PTPN3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2B49, 4QUM, 4QUN, 4RH5, 4RH9, 4RHG, 4RI4, 4RI5, 4S0G
Identifiers
Aliases	PTPN3, PTP-H1, PTPH1, protein tyrosine phosphatase, non-receptor type 3, protein tyrosine phosphatase non-receptor type 3
External IDs	OMIM: 176877; MGI: 105307; HomoloGene: 74451; GeneCards: PTPN3; OMA:PTPN3 - orthologs
Gene location (Human) Chr. Chromosome 9 (human) Band 9q31.3 Start 109,375,466 bp End 109,498,313 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4 B3|4 31.66 cM Start 57,190,841 bp End 57,301,837 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte Skeletal muscle tissue of rectus abdominis secondary oocyte triceps brachii muscle glutes muscle of thigh thoracic diaphragm lateral nuclear group of thalamus gastrocnemius muscle biceps brachii Top expressed in medial dorsal nucleus medial geniculate nucleus lateral geniculate nucleus trigeminal ganglion ankle otolith organ utricle soleus muscle tibialis anterior muscle olfactory system More reference expression data BioGPS More reference expression data
Gene ontology Molecular function sodium channel regulator activity phosphoprotein phosphatase activity phosphatase activity phosphotyrosine residue binding ATPase binding cytoskeletal protein binding protein binding protein tyrosine phosphatase activity hydrolase activity Cellular component cytoplasm membrane cytoplasmic side of plasma membrane cytoskeleton plasma membrane Biological process regulation of membrane depolarization during action potential protein dephosphorylation liver regeneration regulation of sodium ion transmembrane transporter activity negative regulation of membrane protein ectodomain proteolysis negative regulation of mitotic cell cycle dephosphorylation peptidyl-tyrosine dephosphorylation negative regulation of epidermal growth factor receptor signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5774 545622 Ensembl ENSG00000070159 ENSMUSG00000038764 UniProt P26045 A2ALK8 RefSeq (mRNA) NM_001145368 NM_001145369 NM_001145370 NM_001145371 NM_001145372 NM_002829 NM_011207 NM_001384115 RefSeq (protein) NP_001138840 NP_001138841 NP_001138842 NP_001138843 NP_001138844 NP_002820 NP_035337 NP_001371044 Location (UCSC) Chr 9: 109.38 – 109.5 Mb Chr 4: 57.19 – 57.3 Mb PubMed search
Wikidata
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Tyrosine-protein phosphatase non-receptor type 3 is an enzyme that in humans is encoded by the PTPN3 gene.

Function

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 protein contains a C-terminal PTP domain and an N-terminal domain homologous to the band 4.1 superfamily of cytoskeletal-associated proteins. P97, a cell cycle regulator involved in a variety of membrane related functions, has been shown to be a substrate of this PTP. This PTP was also found to interact with, and be regulated by adaptor protein 14-3-3 beta.

Interactions

PTPN3 has been shown to interact with YWHAB.

Further reading

• Arimura Y, Hinoda Y, Itoh F, Takekawa M, Tsujisaki M, Adachi M, Imai K, Yachi A (1992). "cDNA cloning of new protein tyrosine phosphatases in the human colon". Tumour Biol. 13 (3): 180–6. doi:10.1159/000217763. PMID 1626183.
• Ikuta S, Itoh F, Hinoda Y, Toyota M, Makiguchi Y, Imai K, Yachi A (1995). "Expression of cytoskeletal-associated protein tyrosine phosphatase PTPH1 mRNA in human hepatocellular carcinoma". J. Gastroenterol. 29 (6): 727–32. doi:10.1007/BF02349278. PMID 7874267. S2CID 31617297.
• Itoh F, Ikuta S, Hinoda Y, Arimura Y, Ohe M, Adachi M, Ariyama T, Inazawa J, Imai K, Yachi A (1994). "Expression and chromosomal assignment of PTPH1 gene encoding a cytosolic protein tyrosine phosphatase homologous to cytoskeletal-associated proteins". Int. J. Cancer. 55 (6): 947–51. doi:10.1002/ijc.2910550612. PMID 8253532. S2CID 32380202.
• Zhang SH, Kobayashi R, Graves PR, Piwnica-Worms H, Tonks NK (1997). "Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta protein". J. Biol. Chem. 272 (43): 27281–7. doi:10.1074/jbc.272.43.27281. PMID 9341175.
• Zhang SH, Liu J, Kobayashi R, Tonks NK (1999). "Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1". J. Biol. Chem. 274 (25): 17806–12. doi:10.1074/jbc.274.25.17806. PMID 10364224.
• Gjörloff-Wingren A, Saxena M, Han S, Wang X, Alonso A, Renedo M, Oh P, Williams S, Schnitzer J, Mustelin T (2000). "Subcellular localization of intracellular protein tyrosine phosphatases in T cells". Eur. J. Immunol. 30 (8): 2412–21. doi:10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J. PMID 10940933. S2CID 8132613.
• Zheng Y, Schlondorff J, Blobel CP (2003). "Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1". J. Biol. Chem. 277 (45): 42463–70. doi:10.1074/jbc.M207459200. PMID 12207026.
• Sozio MS, Mathis MA, Young JA, Wälchli S, Pitcher LA, Wrage PC, Bartók B, Campbell A, Watts JD, Aebersold R, Hooft van Huijsduijnen R, van Oers NS (2004). "PTPH1 is a predominant protein-tyrosine phosphatase capable of interacting with and dephosphorylating the T cell receptor zeta subunit". J. Biol. Chem. 279 (9): 7760–9. doi:10.1074/jbc.M309994200. PMID 14672952.
• Blanchetot C, Chagnon M, Dubé N, Hallé M, Tremblay ML (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.
• Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell. Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
• Jespersen T, Gavillet B, van Bemmelen MX, Cordonier S, Thomas MA, Staub O, Abriel H (2006). "Cardiac sodium channel Na(v)1.5 interacts with and is regulated by the protein tyrosine phosphatase PTPH1". Biochem. Biophys. Res. Commun. 348 (4): 1455–62. doi:10.1016/j.bbrc.2006.08.014. PMID 16930557.
• Jing M, Bohl J, Brimer N, Kinter M, Vande Pol SB (2007). "Degradation of tyrosine phosphatase PTPN3 (PTPH1) by association with oncogenic human papillomavirus E6 proteins". J. Virol. 81 (5): 2231–9. doi:10.1128/JVI.01979-06. PMC 1865939. PMID 17166906.
• Töpffer S, Müller-Schiffmann A, Matentzoglu K, Scheffner M, Steger G (2007). "Protein tyrosine phosphatase H1 is a target of the E6 oncoprotein of high-risk genital human papillomaviruses". J. Gen. Virol. 88 (Pt 11): 2956–65. doi:10.1099/vir.0.83123-0. PMID 17947517.