# PTPN2

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Protein-coding gene in the species Homo sapiens

PTPN2 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1L8K Identifiers Aliases PTPN2, PTN2, PTPT, TC-PTP, TCELLPTP, TCPTP, protein tyrosine phosphatase, non-receptor type 2, protein tyrosine phosphatase non-receptor type 2 External IDs OMIM: 176887; MGI: 97806; HomoloGene: 7497; GeneCards: PTPN2; OMA:PTPN2 - orthologs Gene location (Human) Chr. Chromosome 18 (human)[1] Band 18p11.21 Start 12,785,478 bp[1] End 12,929,643 bp[1] Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18|18 E1 Start 67,798,581 bp[2] End 67,857,665 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tendon of biceps brachii monocyte granulocyte tonsil cartilage tissue parotid gland oocyte lymph node body of pancreas gonad Top expressed in otic placode saccule condyle primary oocyte fossa Paneth cell hair follicle secondary oocyte submandibular gland primitive streak More reference expression data BioGPS n/a Gene ontology Molecular function protein binding protein kinase binding phosphatase activity integrin binding phosphoprotein phosphatase activity syntaxin binding non-membrane spanning protein tyrosine phosphatase activity receptor tyrosine kinase binding hydrolase activity protein tyrosine phosphatase activity STAT family protein binding Cellular component cytoplasm membrane plasma membrane endoplasmic reticulum nucleus endoplasmic reticulum-Golgi intermediate compartment nucleoplasm cytosol Biological process negative regulation of type I interferon-mediated signaling pathway negative regulation of epidermal growth factor receptor signaling pathway positive regulation of PERK-mediated unfolded protein response dephosphorylation negative regulation of interleukin-4-mediated signaling pathway positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway negative regulation of interleukin-6-mediated signaling pathway negative regulation of cell population proliferation protein dephosphorylation negative regulation of interleukin-2-mediated signaling pathway regulation of interferon-gamma-mediated signaling pathway negative regulation of protein tyrosine kinase activity regulation of hepatocyte growth factor receptor signaling pathway negative regulation of platelet-derived growth factor receptor-beta signaling pathway insulin receptor signaling pathway negative regulation of interferon-gamma-mediated signaling pathway glucose homeostasis negative regulation of chemotaxis negative regulation of tumor necrosis factor-mediated signaling pathway negative regulation of macrophage differentiation negative regulation of T cell receptor signaling pathway negative regulation of positive thymic T cell selection negative regulation of insulin receptor signaling pathway T cell differentiation negative regulation of ERK1 and ERK2 cascade erythrocyte differentiation negative regulation of lipid storage B cell differentiation peptidyl-tyrosine dephosphorylation positive regulation of gluconeogenesis negative regulation of macrophage colony-stimulating factor signaling pathway negative regulation of inflammatory response negative regulation of transcription by RNA polymerase II negative regulation of tyrosine phosphorylation of STAT protein cellular response to cytokine stimulus Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 5771 19255 Ensembl ENSG00000175354 ENSMUSG00000024539 UniProt P17706 Q06180 RefSeq (mRNA) NM_001207013 NM_001308287 NM_002828 NM_080422 NM_080423 NM_001127177 NM_008977 RefSeq (protein) NP_001193942 NP_001295216 NP_002819 NP_536347 NP_536348 NP_001120649 NP_033003 Location (UCSC) Chr 18: 12.79 – 12.93 Mb Chr 18: 67.8 – 67.86 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Tyrosine-protein phosphatase non-receptor type 2** is an [enzyme](/source/Enzyme) that in humans is encoded by the *PTPN2* [gene](/source/Gene).[5][6]

The protein encoded by this gene is a member of the [protein tyrosine phosphatase](/source/Protein_tyrosine_phosphatase) (PTP) family. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be [signaling molecules](/source/Signaling_molecules) that regulate a variety of cellular processes including cell growth, differentiation, [mitotic](/source/Mitosis) cycle, and [oncogenic](/source/Oncogenic) transformation.

[Epidermal growth factor](/source/Epidermal_growth_factor) receptor and the adaptor protein [Shc](/source/SHC1) were reported to be substrates of this PTP, which suggested the roles in growth factor mediated cell signaling. Three alternatively spliced variants of this gene, which encode [isoforms](/source/Isoforms) differing at their extreme C-termini, have been described.

The different C-termini are thought to determine the substrate specificity, as well as the cellular localization of the isoforms. Two highly related but distinctly processed [pseudogenes](/source/Pseudogenes) that localize to distinct [chromosomes](/source/Chromosome) have been reported.[6]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000175354](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000175354) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000024539](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000024539) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=5771). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=19255). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid2164224_5-0)** Brown-Shimer S, Johnson KA, Lawrence JB, Johnson C, Bruskin A, Green NR, Hill DE (Aug 1990). ["Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC54279). *Proc Natl Acad Sci U S A*. **87** (13): 5148–52. [Bibcode](/source/Bibcode_(identifier)):[1990PNAS...87.5148B](https://ui.adsabs.harvard.edu/abs/1990PNAS...87.5148B). [doi](/source/Doi_(identifier)):[10.1073/pnas.87.13.5148](https://doi.org/10.1073%2Fpnas.87.13.5148). [PMC](/source/PMC_(identifier)) [54279](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC54279). [PMID](/source/PMID_(identifier)) [2164224](https://pubmed.ncbi.nlm.nih.gov/2164224).

1. ^ [***a***](#cite_ref-entrez_6-0) [***b***](#cite_ref-entrez_6-1) ["Entrez Gene: PTPN2 protein tyrosine phosphatase, non-receptor type 2"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=5771).

## Further reading

- Baumgartner, CK, Ebrahimi-Nik, H, Iracheta-Vellve, A (2023). ["The PTPN2/PTPN1 inhibitor ABBV-CLS-484 unleashes potent anti-tumour immunity"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10599993). *Nature*. **622** (7984): 850–862. [Bibcode](/source/Bibcode_(identifier)):[2023Natur.622..850B](https://ui.adsabs.harvard.edu/abs/2023Natur.622..850B). [doi](/source/Doi_(identifier)):[10.1038/s41586-023-06575-7](https://doi.org/10.1038%2Fs41586-023-06575-7). [PMC](/source/PMC_(identifier)) [10599993](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10599993). [PMID](/source/PMID_(identifier)) [37794185](https://pubmed.ncbi.nlm.nih.gov/37794185).

- LaFleur MW, Nguyen TH, Coxe MA (2019). ["PTPN2 regulates the generation of exhausted CD8+ T cell subpopulations and restrains tumor immunity"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6754306). *Nat. Immunol*. **20** (10): 1335–1347. [doi](/source/Doi_(identifier)):[10.1038/s41590-019-0480-4](https://doi.org/10.1038%2Fs41590-019-0480-4). [PMC](/source/PMC_(identifier)) [6754306](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6754306). [PMID](/source/PMID_(identifier)) [31527834](https://pubmed.ncbi.nlm.nih.gov/31527834).

- Manguso RT, Pope HW, Zimmer MD (2017). ["In vivo CRISPR screening identifies Ptpn2 as a cancer immunotherapy target"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5924693). *Nature*. **547** (7664): 413–418. [doi](/source/Doi_(identifier)):[10.1038/nature23270](https://doi.org/10.1038%2Fnature23270). [PMC](/source/PMC_(identifier)) [5924693](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5924693). [PMID](/source/PMID_(identifier)) [28723893](https://pubmed.ncbi.nlm.nih.gov/28723893).

- Mosinger B, Tillmann U, Westphal H, Tremblay ML (1992). ["Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC48266). *Proc. Natl. Acad. Sci. U.S.A*. **89** (2): 499–503. [Bibcode](/source/Bibcode_(identifier)):[1992PNAS...89..499M](https://ui.adsabs.harvard.edu/abs/1992PNAS...89..499M). [doi](/source/Doi_(identifier)):[10.1073/pnas.89.2.499](https://doi.org/10.1073%2Fpnas.89.2.499). [PMC](/source/PMC_(identifier)) [48266](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC48266). [PMID](/source/PMID_(identifier)) [1731319](https://pubmed.ncbi.nlm.nih.gov/1731319).

- Swarup G, Kamatkar S, Radha V, Rema V (1991). ["Molecular cloning and expression of a protein-tyrosine phosphatase showing homology with transcription factors Fos and Jun"](https://doi.org/10.1016%2F0014-5793%2891%2980205-H). *FEBS Lett*. **280** (1): 65–9. [Bibcode](/source/Bibcode_(identifier)):[1991FEBSL.280...65S](https://ui.adsabs.harvard.edu/abs/1991FEBSL.280...65S). [doi](/source/Doi_(identifier)):[10.1016/0014-5793(91)80205-H](https://doi.org/10.1016%2F0014-5793%2891%2980205-H). [PMID](/source/PMID_(identifier)) [1849097](https://pubmed.ncbi.nlm.nih.gov/1849097). [S2CID](/source/S2CID_(identifier)) [10568838](https://api.semanticscholar.org/CorpusID:10568838).

- Cool DE, Tonks NK, Charbonneau H, et al. (1989). ["cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC297600). *Proc. Natl. Acad. Sci. U.S.A*. **86** (14): 5257–61. [Bibcode](/source/Bibcode_(identifier)):[1989PNAS...86.5257C](https://ui.adsabs.harvard.edu/abs/1989PNAS...86.5257C). [doi](/source/Doi_(identifier)):[10.1073/pnas.86.14.5257](https://doi.org/10.1073%2Fpnas.86.14.5257). [PMC](/source/PMC_(identifier)) [297600](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC297600). [PMID](/source/PMID_(identifier)) [2546150](https://pubmed.ncbi.nlm.nih.gov/2546150).

- Lorenzen JA, Dadabay CY, Fischer EH (1995). ["COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleus"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120615). *J. Cell Biol*. **131** (3): 631–43. [doi](/source/Doi_(identifier)):[10.1083/jcb.131.3.631](https://doi.org/10.1083%2Fjcb.131.3.631). [PMC](/source/PMC_(identifier)) [2120615](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120615). [PMID](/source/PMID_(identifier)) [7593185](https://pubmed.ncbi.nlm.nih.gov/7593185).

- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". *Gene*. **138** (1–2): 171–4. [doi](/source/Doi_(identifier)):[10.1016/0378-1119(94)90802-8](https://doi.org/10.1016%2F0378-1119%2894%2990802-8). [PMID](/source/PMID_(identifier)) [8125298](https://pubmed.ncbi.nlm.nih.gov/8125298).

- Johnson CV, Cool DE, Glaccum MB, et al. (1993). "Isolation and mapping of human T-cell protein tyrosine phosphatase sequences: localization of genes and pseudogenes discriminated using fluorescence hybridization with genomic versus cDNA probes". *Genomics*. **16** (3): 619–29. [doi](/source/Doi_(identifier)):[10.1006/geno.1993.1239](https://doi.org/10.1006%2Fgeno.1993.1239). [PMID](/source/PMID_(identifier)) [8325634](https://pubmed.ncbi.nlm.nih.gov/8325634).

- Tiganis T, Flint AJ, Adam SA, Tonks NK (1997). ["Association of the T-cell protein tyrosine phosphatase with nuclear import factor p97"](https://doi.org/10.1074%2Fjbc.272.34.21548). *J. Biol. Chem*. **272** (34): 21548–57. [doi](/source/Doi_(identifier)):[10.1074/jbc.272.34.21548](https://doi.org/10.1074%2Fjbc.272.34.21548). [PMID](/source/PMID_(identifier)) [9261175](https://pubmed.ncbi.nlm.nih.gov/9261175).

- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". *Gene*. **200** (1–2): 149–56. [doi](/source/Doi_(identifier)):[10.1016/S0378-1119(97)00411-3](https://doi.org/10.1016%2FS0378-1119%2897%2900411-3). [PMID](/source/PMID_(identifier)) [9373149](https://pubmed.ncbi.nlm.nih.gov/9373149).

- Tiganis T, Bennett AM, Ravichandran KS, Tonks NK (1998). ["Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108877). *Mol. Cell. Biol*. **18** (3): 1622–34. [doi](/source/Doi_(identifier)):[10.1128/MCB.18.3.1622](https://doi.org/10.1128%2FMCB.18.3.1622). [PMC](/source/PMC_(identifier)) [108877](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC108877). [PMID](/source/PMID_(identifier)) [9488479](https://pubmed.ncbi.nlm.nih.gov/9488479).

- Tiganis T, Kemp BE, Tonks NK (1999). ["The protein-tyrosine phosphatase TCPTP regulates epidermal growth factor receptor-mediated and phosphatidylinositol 3-kinase-dependent signaling"](https://doi.org/10.1074%2Fjbc.274.39.27768). *J. Biol. Chem*. **274** (39): 27768–75. [doi](/source/Doi_(identifier)):[10.1074/jbc.274.39.27768](https://doi.org/10.1074%2Fjbc.274.39.27768). [PMID](/source/PMID_(identifier)) [10488121](https://pubmed.ncbi.nlm.nih.gov/10488121).

- Iversen LF, Moller KB, Pedersen AK, et al. (2002). ["Structure determination of T cell protein-tyrosine phosphatase"](https://doi.org/10.1074%2Fjbc.M200567200). *J. Biol. Chem*. **277** (22): 19982–90. [doi](/source/Doi_(identifier)):[10.1074/jbc.M200567200](https://doi.org/10.1074%2Fjbc.M200567200). [PMID](/source/PMID_(identifier)) [11907034](https://pubmed.ncbi.nlm.nih.gov/11907034).

- Simoncic PD, Lee-Loy A, Barber DL, et al. (2002). ["The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3"](https://doi.org/10.1016%2FS0960-9822%2802%2900697-8). *Curr. Biol*. **12** (6): 446–53. [Bibcode](/source/Bibcode_(identifier)):[2002CBio...12..446S](https://ui.adsabs.harvard.edu/abs/2002CBio...12..446S). [doi](/source/Doi_(identifier)):[10.1016/S0960-9822(02)00697-8](https://doi.org/10.1016%2FS0960-9822%2802%2900697-8). [PMID](/source/PMID_(identifier)) [11909529](https://pubmed.ncbi.nlm.nih.gov/11909529). [S2CID](/source/S2CID_(identifier)) [16693906](https://api.semanticscholar.org/CorpusID:16693906).

- ten Hoeve J, de Jesus Ibarra-Sanchez M, Fu Y, et al. (2002). ["Identification of a nuclear Stat1 protein tyrosine phosphatase"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC133976). *Mol. Cell. Biol*. **22** (16): 5662–8. [doi](/source/Doi_(identifier)):[10.1128/MCB.22.16.5662-5668.2002](https://doi.org/10.1128%2FMCB.22.16.5662-5668.2002). [PMC](/source/PMC_(identifier)) [133976](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC133976). [PMID](/source/PMID_(identifier)) [12138178](https://pubmed.ncbi.nlm.nih.gov/12138178).

- Zhu W, Mustelin T, David M (2002). ["Arginine methylation of STAT1 regulates its dephosphorylation by T cell protein tyrosine phosphatase"](https://doi.org/10.1074%2Fjbc.C200346200). *J. Biol. Chem*. **277** (39): 35787–90. [doi](/source/Doi_(identifier)):[10.1074/jbc.C200346200](https://doi.org/10.1074%2Fjbc.C200346200). [PMID](/source/PMID_(identifier)) [12171910](https://pubmed.ncbi.nlm.nih.gov/12171910).

- Yamamoto T, Sekine Y, Kashima K, et al. (2002). "The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation". *Biochem. Biophys. Res. Commun*. **297** (4): 811–7. [doi](/source/Doi_(identifier)):[10.1016/S0006-291X(02)02291-X](https://doi.org/10.1016%2FS0006-291X%2802%2902291-X). [hdl](/source/Hdl_(identifier)):[2115/28124](https://hdl.handle.net/2115%2F28124). [PMID](/source/PMID_(identifier)) [12359225](https://pubmed.ncbi.nlm.nih.gov/12359225).

- Gupta S, Radha V, Sudhakar Ch, Swarup G (2003). ["A nuclear protein tyrosine phosphatase activates p53 and induces caspase-1-dependent apoptosis"](https://doi.org/10.1016%2FS0014-5793%2802%2903628-1). *FEBS Lett*. **532** (1–2): 61–6. [doi](/source/Doi_(identifier)):[10.1016/S0014-5793(02)03628-1](https://doi.org/10.1016%2FS0014-5793%2802%2903628-1). [PMID](/source/PMID_(identifier)) [12459463](https://pubmed.ncbi.nlm.nih.gov/12459463). [S2CID](/source/S2CID_(identifier)) [33468275](https://api.semanticscholar.org/CorpusID:33468275).

- 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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). *Proc. Natl. Acad. Sci. U.S.A*. **99** (26): 16899–903. [Bibcode](/source/Bibcode_(identifier)):[2002PNAS...9916899M](https://ui.adsabs.harvard.edu/abs/2002PNAS...9916899M). [doi](/source/Doi_(identifier)):[10.1073/pnas.242603899](https://doi.org/10.1073%2Fpnas.242603899). [PMC](/source/PMC_(identifier)) [139241](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). [PMID](/source/PMID_(identifier)) [12477932](https://pubmed.ncbi.nlm.nih.gov/12477932).

- Galic S, Klingler-Hoffmann M, Fodero-Tavoletti MT, et al. (2003). ["Regulation of insulin receptor signaling by the protein tyrosine phosphatase TCPTP"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC149470). *Mol. Cell. Biol*. **23** (6): 2096–108. [doi](/source/Doi_(identifier)):[10.1128/MCB.23.6.2096-2108.2003](https://doi.org/10.1128%2FMCB.23.6.2096-2108.2003). [PMC](/source/PMC_(identifier)) [149470](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC149470). [PMID](/source/PMID_(identifier)) [12612081](https://pubmed.ncbi.nlm.nih.gov/12612081).

v t e PDB gallery 1l8k: T Cell Protein-Tyrosine Phosphatase Structure

v t e Esterase: protein tyrosine phosphatases (EC 3.1.3.48) Class I Classical PTPs Receptor type PTPs PTPRA PTPRB PTPRC PTPRD PTPRE PTPRF PTPRG PTPRH PTPRJ PTPRK PTPRM PTPRN PTPRN2 PTPRO PTPRQ PTPRR PTPRS PTPRT PTPRU PTPRZ1 PTPRZ2 Non receptor type PTPs PTPN1 PTPN2 PTPN3 PTPN4 PTPN5 PTPN6 PTPN7 PTPN9 PTPN11 PTPN12 PTPN13 PTPN14 PTPN18 PTPN20 PTPN21 PTPN22 PTPN23 VH1-like or dual specific phosphatases (DSPs) MAPK phosphatases (MKPs) DUSP1 DUSP2 DUSP4 DUSP5 DUSP6 DUSP7 DUSP8 DUSP9 DUSP10 DUSP16 MK-STYX Slingshots SSH1 SSH2 SSH3 PRLs PTP4A1 PTP4A2 PTP4A3 CDC14s CDC14A CDC14B CDKN3 PTP9Q22 Atypical DSPs DUSP3 DUSP11 DUSP12 DUSP13A DUSP13B DUSP14 DUSP15 DUSP18 DUSP19 DUSP21 DUSP22 DUSP23 DUSP24 DUSP25 DUSP26 DUSP27 EMP2A RNGTT STYX Phosphatase and tensin homologs (PTENs) PTEN TPIP TPTE TNS TENC1 Myotubularins MTM1 MTMR2 MTMR3 MTMR4 MTMR5 MTMR6 MTMR7 MTMR8 MTMR9 MTMR10 MTMR11 MTMR12 MTMR13 MTMR14 MTMR15 Class II ACP1 Class III Cdc25 CDC25A CDC25B CDC25C Class IV EYA1 EYA2 EYA3 EYA4

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Adapted from the Wikipedia article [PTPN2](https://en.wikipedia.org/wiki/PTPN2) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/PTPN2?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.