OAZ2

OAZ2
Identifiers
AliasesOAZ2, AZ2, ornithine decarboxylase antizyme 2
External IDsMGI: 109492 HomoloGene: 31094 GeneCards: OAZ2
Gene location (Human)
Chr.Chromosome 15 (human)[1]
Band15q22.31Start64,687,573 bp[1]
End64,703,281 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

4947

18247

Ensembl

ENSG00000180304

ENSMUSG00000040652

UniProt

O95190

O08608

RefSeq (mRNA)

NM_002537
NM_001301302

NM_001301307
NM_010952

RefSeq (protein)

NP_001288231
NP_002528

NP_001288236
NP_035082

Location (UCSC)Chr 15: 64.69 – 64.7 MbChr 9: 65.67 – 65.69 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ornithine decarboxylase antizyme 2 is an enzyme that in humans is encoded by the OAZ2 gene.[5][6][7]

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.[7]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000180304 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000040652 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ 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.
  6. ↑ 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.
  7. 1 2 "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.


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