MTAP

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Methylthioadenosine phosphorylase
File:PBB Protein MTAP image.jpg
PDB rendering based on 1cb0.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols MTAP ; MSAP; c86fus
External IDs Template:OMIM5 Template:MGI HomoloGene1838
RNA expression pattern
File:PBB GE MTAP 204956 at tn.png
File:PBB GE MTAP 211363 s at tn.png
File:PBB GE MTAP 216685 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Methylthioadenosine phosphorylase, also known as MTAP, is a human gene.[1]

This gene encodes an enzyme that plays a major role in polyamine metabolism and is important for the salvage of both adenine and methionine. The encoded enzyme is deficient in many cancers because this gene and the tumor suppressor p16 gene are co-deleted. Multiple alternatively spliced transcript variants have been described for this gene, but their full-length natures remain unknown.[1]

References

  1. 1.0 1.1 "Entrez Gene: MTAP methylthioadenosine phosphorylase".

Further reading

  • Carrera CJ, Eddy RL, Shows TB, Carson DA (1984). "Assignment of the gene for methylthioadenosine phosphorylase to human chromosome 9 by mouse-human somatic cell hybridization". Proc. Natl. Acad. Sci. U.S.A. 81 (9): 2665–8. PMID 6425836.
  • Olopade OI, Pomykala HM, Hagos F; et al. (1995). "Construction of a 2.8-megabase yeast artificial chromosome contig and cloning of the human methylthioadenosine phosphorylase gene from the tumor suppressor region on 9p21". Proc. Natl. Acad. Sci. U.S.A. 92 (14): 6489–93. PMID 7604019.
  • Nobori T, Takabayashi K, Tran P; et al. (1996). "Genomic cloning of methylthioadenosine phosphorylase: a purine metabolic enzyme deficient in multiple different cancers". Proc. Natl. Acad. Sci. U.S.A. 93 (12): 6203–8. PMID 8650244.
  • Della Ragione F, Takabayashi K, Mastropietro S; et al. (1996). "Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA". Biochem. Biophys. Res. Commun. 223 (3): 514–9. doi:10.1006/bbrc.1996.0926. PMID 8687427.
  • Appleby TC, Erion MD, Ealick SE (1999). "The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis". Structure. 7 (6): 629–41. PMID 10404592.
  • Schmid M, Sen M, Rosenbach MD; et al. (2001). "A methylthioadenosine phosphorylase (MTAP) fusion transcript identifies a new gene on chromosome 9p21 that is frequently deleted in cancer". Oncogene. 19 (50): 5747–54. doi:10.1038/sj.onc.1203942. PMID 11126361.
  • Gursky S, Olopade OI, Rowley JD (2001). "Identification of a 1.2 Kb cDNA fragment from a region on 9p21 commonly deleted in multiple tumor types". Cancer Genet. Cytogenet. 129 (2): 93–101. PMID 11566337.
  • Christopher SA, Diegelman P, Porter CW, Kruger WD (2002). "Methylthioadenosine phosphorylase, a gene frequently codeleted with p16(cdkN2a/ARF), acts as a tumor suppressor in a breast cancer cell line". Cancer Res. 62 (22): 6639–44. PMID 12438261.
  • 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. doi:10.1073/pnas.242603899. PMID 12477932.
  • Bornhauser BC, Olsson PA, Lindholm D (2003). "MSAP is a novel MIR-interacting protein that enhances neurite outgrowth and increases myosin regulatory light chain". J. Biol. Chem. 278 (37): 35412–20. doi:10.1074/jbc.M306271200. PMID 12826659.
  • Behrmann I, Wallner S, Komyod W; et al. (2003). "Characterization of methylthioadenosin phosphorylase (MTAP) expression in malignant melanoma". Am. J. Pathol. 163 (2): 683–90. PMID 12875987.
  • Subhi AL, Diegelman P, Porter CW; et al. (2004). "Methylthioadenosine phosphorylase regulates ornithine decarboxylase by production of downstream metabolites". J. Biol. Chem. 278 (50): 49868–73. doi:10.1074/jbc.M308451200. PMID 14506228.
  • Beausoleil SA, Jedrychowski M, Schwartz D; et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Bataille F, Rogler G, Modes K; et al. (2005). "Strong expression of methylthioadenosine phosphorylase (MTAP) in human colon carcinoma cells is regulated by TCF1/[beta]-catenin". Lab. Invest. 85 (1): 124–36. doi:10.1038/labinvest.3700192. PMID 15492751.
  • Berasain C, Hevia H, Fernández-Irigoyen J; et al. (2004). "Methylthioadenosine phosphorylase gene expression is impaired in human liver cirrhosis and hepatocarcinoma". Biochim. Biophys. Acta. 1690 (3): 276–84. doi:10.1016/j.bbadis.2004.08.002. PMID 15511635.
  • Subhi AL, Tang B, Balsara BR; et al. (2005). "Loss of methylthioadenosine phosphorylase and elevated ornithine decarboxylase is common in pancreatic cancer". Clin. Cancer Res. 10 (21): 7290–6. doi:10.1158/1078-0432.CCR-04-0972. PMID 15534104.
  • Hustinx SR, Hruban RH, Leoni LM; et al. (2005). "Homozygous deletion of the MTAP gene in invasive adenocarcinoma of the pancreas and in periampullary cancer: a potential new target for therapy". Cancer Biol. Ther. 4 (1): 83–6. PMID 15662124.
  • Hustinx SR, Leoni LM, Yeo CJ; et al. (2005). "Concordant loss of MTAP and p16/CDKN2A expression in pancreatic intraepithelial neoplasia: evidence of homozygous deletion in a noninvasive precursor lesion". Mod. Pathol. 18 (7): 959–63. doi:10.1038/modpathol.3800377. PMID 15832197.
  • Hellerbrand C, Mühlbauer M, Wallner S; et al. (2007). "Promoter-hypermethylation is causing functional relevant downregulation of methylthioadenosine phosphorylase (MTAP) expression in hepatocellular carcinoma". Carcinogenesis. 27 (1): 64–72. doi:10.1093/carcin/bgi201. PMID 16081515.

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