OAZ2
Ornithine decarboxylase antizyme 2 | |||||||||||||
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Identifiers | |||||||||||||
Symbols | OAZ2 ; AZ2 | ||||||||||||
External IDs | OMIM: 604152 MGI: 109492 HomoloGene: 31094 GeneCards: OAZ2 Gene | ||||||||||||
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RNA expression pattern | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 4947 | 18247 | |||||||||||
Ensembl | ENSG00000180304 | ENSMUSG00000040652 | |||||||||||
UniProt | O95190 | O08608 | |||||||||||
RefSeq (mRNA) | NM_001301302 | NM_001301307 | |||||||||||
RefSeq (protein) | NP_001288231 | NP_001288236 | |||||||||||
Location (UCSC) | Chr 15: 64.98 – 65 Mb | Chr 9: 65.67 – 65.69 Mb | |||||||||||
PubMed search | |||||||||||||
Ornithine decarboxylase antizyme 2 is an enzyme that in humans is encoded by the OAZ2 gene.[1][2][3]
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 but does not accelerate its degradation.[3]
References
- ↑ Ivanov IP, Gesteland RF, Atkins JF (Dec 1998). "A second mammalian antizyme: conservation of programmed ribosomal frameshifting". Genomics 52 (2): 119–29. doi:10.1006/geno.1998.5434. PMID 9782076.
- ↑ Zhou J, Atkins JF, Gesteland RF (Jul 1999). "Structure of human ornithine decarboxylase antizyme 2 gene". Gene 232 (2): 165–71. doi:10.1016/S0378-1119(99)00128-6. PMID 10352227.
- ↑ 3.0 3.1 "Entrez Gene: OAZ2 ornithine decarboxylase antizyme 2".
Further reading
- Coffino P (2000). "Polyamines in spermiogenesis: not now, darling.". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4421–3. doi:10.1073/pnas.97.9.4421. PMC 34313. PMID 10781034.
- Ewing RM, Chu P, Elisma F et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
- 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. PMC 1134669. PMID 15355308.
- 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.
- 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.
- Nilsson J, Koskiniemi S, Persson K et al. (1998). "Polyamines regulate both transcription and translation of the gene encoding ornithine decarboxylase antizyme in mouse.". Eur. J. Biochem. 250 (2): 223–31. doi:10.1111/j.1432-1033.1997.0223a.x. PMID 9428668.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.