OAZ2

OAZ2
Identifiers
Aliases	OAZ2 , AZ2, ornithine decarboxylase antizyme 2
External IDs	OMIM: 604152; MGI: 109492; HomoloGene: 31094; GeneCards: OAZ2; OMA:OAZ2 - orthologs
Gene location (Human) Chr. Chromosome 15 (human) [1] Band 15q22.31 Start 64,687,573 bp [1] End 64,703,281 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9|9 C Start 65,575,283 bp [2] End 65,597,582 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left testis right testis monocyte C1 segment prefrontal cortex amygdala nucleus accumbens gastrocnemius muscle cingulate gyrus right frontal lobe Top expressed in lung muscle of thigh quadriceps femoris muscle skeletal muscle tissue neural tube dentate gyrus of hippocampal formation granule cell mesencephalon hypothalamus heart superior frontal gyrus More reference expression data BioGPS 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 Species Human Mouse 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 Mb Chr 9: 65.58 – 65.6 Mb PubMed search [3] [4]
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. GRCh38: Ensembl release 89: ENSG00000180304 – Ensembl, May 2017
2. 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.
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. "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. 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.