MTAP

S-methyl-5'-thioadenosine phosphorylase is an enzyme that in humans is encoded by the MTAP gene.[5][6]

MTAP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1SD1, 3OZD, 3OZC, 3LN5, 3OZE, 1SD2, 1CB0, 1CG6, 1K27
Identifiers
Aliases	MTAP, BDMF, DMSFH, DMSMFH, HEL-249, LGMBF, MSAP, c86fus, methylthioadenosine phosphorylase
External IDs	OMIM: 156540 MGI: 1914152 HomoloGene: 1838 GeneCards: MTAP
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9p21.3 Start 21,802,636 bp[1] End 21,937,651 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 C4 Start 89,137,122 bp[2] End 89,181,081 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • transferase activity, transferring glycosyl groups • phosphorylase activity • catalytic activity • GO:0001948 protein binding • transferase activity, transferring pentosyl groups • S-methyl-5-thioadenosine phosphorylase activity Cellular component • extracellular exosome • cell nucleus • cytosol • cytoplasm Biological process • L-methionine salvage from methylthioadenosine • purine ribonucleoside salvage • nucleoside metabolic process • nicotinamide riboside catabolic process • nucleobase-containing compound metabolic process • interleukin-12-mediated signaling pathway • methylation • response to testosterone Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4507	66902
Ensembl	ENSG00000099810	ENSMUSG00000062937
UniProt	Q13126	Q9CQ65
RefSeq (mRNA)	NM_002451	NM_024433
RefSeq (protein)	NP_002442	NP_077753
Location (UCSC)	Chr 9: 21.8 – 21.94 Mb	Chr 4: 89.14 – 89.18 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000099810 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000062937 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Schmid M, Sen M, Rosenbach MD, Carrera CJ, Friedman H, Carson DA (Dec 2000). "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.
6. "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. doi:10.1073/pnas.81.9.2665. PMC 345130. 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. doi:10.1073/pnas.92.14.6489. PMC 41543. 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. doi:10.1073/pnas.93.12.6203. PMC 39214. 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. doi:10.1016/S0969-2126(99)80084-7. PMID 10404592.
• 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. doi:10.1016/S0165-4608(01)00444-7. 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. PMC 139241. 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. doi:10.1016/S0002-9440(10)63695-4. PMC 1868213. 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. PMC 514446. 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. PMC 528928. 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. hdl:10171/21382. 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. doi:10.4161/cbt.4.1.1380. 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.