OAZ1

Ornithine decarboxylase antizyme 1
Identifiers
Symbols	OAZ1 ; AZI; MGC138338; OAZ
External IDs	Template:OMIM5 Template:MGI HomoloGene: 7455
Gene ontology Molecular function Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
File:PBB GE OAZ1 215952 s at tn.png
File:PBB GE OAZ1 200077 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

Ornithine decarboxylase antizyme 1, also known as OAZ1, is a human gene.

Ornithine decarboxylase catalyzes the conversion of ornithine to putrescine in the first and apparently rate-limiting step in polyamine biosynthesis. The ornithine decarboxylase antizymes play a role in the regulation of polyamine synthesis by binding to and inhibiting ornithine decarboxylase. Antizyme expression is auto-regulated by polyamine-enhanced translational frameshifting. The antizyme encoded by this gene inhibits ornithine decarboxylase and accelerates its degradation.

Further reading

• Coffino P (2000). "Polyamines in spermiogenesis: not now, darling". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4421–3. PMID 10781034.
• Savage RE, Nofzinger K, Bedell C; et al. (1989). "Chloroform-induced multiple forms of ornithine decarboxylase: differential sensitivity of forms to enhancement by diethyl maleate and inhibition by ODC-antizyme". Journal of toxicology and environmental health. 27 (1): 57–64. PMID 2724368.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tewari DS, Qian Y, Thornton RD; et al. (1995). "Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme". Biochim. Biophys. Acta. 1209 (2): 293–5. PMID 7811704.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Matsufuji S, Matsufuji T, Miyazaki Y; et al. (1995). "Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme". Cell. 80 (1): 51–60. PMID 7813017.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mamroud-Kidron E, Omer-Itsicovich M, Bercovich Z; et al. (1995). "A unified pathway for the degradation of ornithine decarboxylase in reticulocyte lysate requires interaction with the polyamine-induced protein, ornithine decarboxylase antizyme". Eur. J. Biochem. 226 (2): 547–54. PMID 8001569.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ichiba T, Matsufuji S, Miyazaki Y; et al. (1994). "Functional regions of ornithine decarboxylase antizyme". Biochem. Biophys. Res. Commun. 200 (3): 1721–7. doi:10.1006/bbrc.1994.1651. PMID 8185631.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Matsufuji S, Inazawa J, Hayashi T; et al. (1997). "Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization". Genomics. 38 (1): 102–4. PMID 8954789.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yang D, Takii T, Hayashi H; et al. (1997). "Molcecular cloning of human antizyme cDNA". Biochem. Mol. Biol. Int. 38 (5): 957–64. PMID 9132164.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hayashi T, Matsufuji S, Hayashi S (1998). "Characterization of the human antizyme gene". Gene. 203 (2): 131–9. PMID 9426243.CS1 maint: Multiple names: authors list (link)
• Zhu C, Lang DW, Coffino P (1999). "Antizyme2 is a negative regulator of ornithine decarboxylase and polyamine transport". J. Biol. Chem. 274 (37): 26425–30. PMID 10473601.CS1 maint: Multiple names: authors list (link)
• Chen H, MacDonald A, Coffino P (2003). "Structural elements of antizymes 1 and 2 are required for proteasomal degradation of ornithine decarboxylase". J. Biol. Chem. 277 (48): 45957–61. doi:10.1074/jbc.M206799200. PMID 12359729.CS1 maint: Multiple names: authors list (link)
• Ike A, Yamada S, Tanaka H; et al. (2003). "Structure and promoter activity of the gene encoding ornithine decarboxylase antizyme expressed exclusively in haploid germ cells in testis (OAZt/Oaz3)". Gene. 298 (2): 183–93. PMID 12426106.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Grimwood J, Gordon LA, Olsen A; et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature. 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mangold U, Leberer E (2005). "Regulation of all members of the antizyme family by antizyme inhibitor". Biochem. J. 385 (Pt 1): 21–8. doi:10.1042/BJ20040547. PMID 15355308.
• Choi KS, Suh YH, Kim WH; et al. (2005). "Stable siRNA-mediated silencing of antizyme inhibitor: regulation of ornithine decarboxylase activity". Biochem. Biophys. Res. Commun. 328 (1): 206–12. doi:10.1016/j.bbrc.2004.11.172. PMID 15670771.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ku M, Howard S, Ni W; et al. (2006). "OAZ regulates bone morphogenetic protein signaling through Smad6 activation". J. Biol. Chem. 281 (8): 5277–87. doi:10.1074/jbc.M510004200. PMID 16373339.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lim J, Hao T, Shaw C; et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tsuji T, Katsurano M, Ibaragi S; et al. (2007). "Ornithine decarboxylase antizyme upregulates DNA-dependent protein kinase and enhances the nonhomologous end-joining repair of DNA double-strand breaks in human oral cancer cells". Biochemistry. 46 (31): 8920–32. doi:10.1021/bi7000328. PMID 17630775.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)