OAZ2
From Wikipedia, the free encyclopedia
Ornithine decarboxylase antizyme 2
|
|||||||||||
Identifiers | |||||||||||
Symbol(s) | OAZ2; | ||||||||||
External IDs | OMIM: 604152 MGI: 109492 HomoloGene: 31094 | ||||||||||
|
|||||||||||
RNA expression pattern | |||||||||||
Orthologs | |||||||||||
Human | Mouse | ||||||||||
Entrez | 4947 | 18247 | |||||||||
Ensembl | ENSG00000180304 | ENSMUSG00000040652 | |||||||||
Uniprot | O95190 | O08608 | |||||||||
Refseq | NM_002537 (mRNA) NP_002528 (protein) |
NM_010952 (mRNA) NP_035082 (protein) |
|||||||||
Location | Chr 15: 62.77 - 62.77 Mb | Chr 9: 65.47 - 65.49 Mb | |||||||||
Pubmed search | [1] | [2] |
Ornithine decarboxylase antizyme 2, also known as OAZ2, is a human gene.[1]
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.[1]
[edit] References
[edit] Further reading
- Coffino P (2000). "Polyamines in spermiogenesis: not now, darling.". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4421-3. 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: 89. doi: . 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: . 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: . 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: . PMID 12359729.
- Zhou J, Atkins JF, Gesteland RF (1999). "Structure of human ornithine decarboxylase antizyme 2 gene.". Gene 232 (2): 165-71. PMID 10352227.
- Ivanov IP, Gesteland RF, Atkins JF (1998). "A second mammalian antizyme: conservation of programmed ribosomal frameshifting.". Genomics 52 (2): 119-29. doi: . PMID 9782076.
- 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. PMID 9428668.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791-806. PMID 8889548.