OAZ2

OAZ2
Identifiers
Aliases	OAZ2, AZ2, ornithine decarboxylase antizyme 2
External IDs	OMIM: 604152 MGI: 109492 HomoloGene: 31094 GeneCards: OAZ2
Gene location (Human)
Chr.	Chromosome 15 (human)
End	64,703,281 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	65,597,582 bp
RNA expression pattern
	Top expressed in
	monocyte; ; prefrontal cortex; ; amygdala; ; nucleus accumbens; ; gastrocnemius muscle; ; cingulate gyrus; ; caudate nucleus; ; hypothalamus; ; putamen; ; smooth muscle tissue;
	Top expressed in
	lung; ; quadriceps femoris muscle; ; skeletal muscle tissue; ; neural tube; ; mesencephalon; ; hypothalamus; ; heart; ; superior frontal gyrus; ; hippocampus proper; ; rhombencephalon;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	ornithine decarboxylase inhibitor activity; protein binding;
Cellular component	cytosol; nucleus; cytoplasm;
Biological process	positive regulation of intracellular protein transport; polyamine biosynthetic process; polyamine metabolic process; negative regulation of polyamine transmembrane transport; negative regulation of catalytic activity; regulation of cellular amino acid metabolic process; positive regulation of protein catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	4947
	18247
	ENSG00000180304
	ENSMUSG00000040652
	O95190
	O08608
	NM_002537; NM_001301302
	NM_001301307; NM_010952
	NP_001288231; NP_002528
	NP_001288236; NP_035082
	Wikidata
View/Edit Human	View/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 2 3 GRCh38: Ensembl release 89: ENSG00000180304 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000040652 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 "Entrez Gene: OAZ2 ornithine decarboxylase antizyme 2".

Coffino P (2000). "Polyamines in spermiogenesis: not now, darling". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4421–3. Bibcode:2000PNAS...97.4421C. 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. Bibcode:2002PNAS...9916899M. 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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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000180304 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000040652 - 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.

[pmid9782076-5] 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.

[pmid10352227-6] 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.

[entrez-7] 1 2 "Entrez Gene: OAZ2 ornithine decarboxylase antizyme 2".

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References

Further reading