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{{Infobox_gene}}
{{PBB_Controls
'''Ornithine decarboxylase antizyme''' is an [[enzyme]] that in humans is encoded by the ''OAZ1'' [[gene]].<ref name="pmid7811704">{{cite journal |vauthors=Tewari DS, Qian Y, Thornton RD, Pieringer J, Taub R, Mochan E, Tewari M | title = Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme | journal = Biochim Biophys Acta | volume = 1209 | issue = 2 | pages = 293–5 |date=Feb 1995 | pmid = 7811704 | pmc =  | doi =  10.1016/0167-4838(94)90199-6}}</ref><ref name="pmid8954789">{{cite journal |vauthors=Matsufuji S, Inazawa J, Hayashi T, Miyazaki Y, Ichiba T, Furusaka A, Matsufuji T, Atkins JF, Gesteland RF, Murakami Y, Hayashi S | title = Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization | journal = Genomics | volume = 38 | issue = 1 | pages = 102–104 |date=Mar 1997 | pmid = 8954789 | pmc =  | doi =10.1006/geno.1996.0601  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4946| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Ornithine decarboxylase antizyme 1
| HGNCid = 8095
| Symbol = OAZ1
| AltSymbols =; AZI; MGC138338; OAZ
| OMIM = 601579
| ECnumber =
| Homologene = 7455
| MGIid = 109433
  | GeneAtlas_image1 = PBB_GE_OAZ1_215952_s_at_tn.png
  | GeneAtlas_image2 = PBB_GE_OAZ1_200077_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008073 |text = ornithine decarboxylase inhibitor activity}}  
| Component =
| Process = {{GNF_GO|id=GO:0006596 |text = polyamine biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4946
    | Hs_Ensembl = ENSG00000104904
    | Hs_RefseqProtein = NP_004143
    | Hs_RefseqmRNA = NM_004152
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 2220520
    | Hs_GenLoc_end = 2224487
    | Hs_Uniprot = P54368
    | Mm_EntrezGene = 18245
    | Mm_Ensembl = ENSMUSG00000035242
    | Mm_RefseqmRNA = NM_008753
    | Mm_RefseqProtein = NP_032779
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 80229785
    | Mm_GenLoc_end = 80232414
    | Mm_Uniprot = Q52KL6
  }}
}}
'''Ornithine decarboxylase antizyme 1''', also known as '''OAZ1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4946| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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 and accelerates its degradation.<ref name="entrez">{{cite web | title = Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4946| accessdate = }}</ref>
| summary_text = 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 and accelerates its degradation.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Coffino P |title=Polyamines in spermiogenesis: not now, darling. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 9 |pages= 4421-3 |year= 2000 |pmid= 10781034 |doi=  }}
*{{cite journal  | author=Coffino P |title=Polyamines in spermiogenesis: not now, darling |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 9 |pages= 4421–4423 |year= 2000 |pmid= 10781034 |doi=10.1073/pnas.97.9.4421  | pmc=34313 }}
*{{cite journal  | author=Savage RE, Nofzinger K, Bedell C, ''et al.'' |title=Chloroform-induced multiple forms of ornithine decarboxylase: differential sensitivity of forms to enhancement by diethyl maleate and inhibition by ODC-antizyme. |journal=Journal of toxicology and environmental health |volume=27 |issue= 1 |pages= 57-64 |year= 1989 |pmid= 2724368 |doi= }}
*{{cite journal  | author=Savage RE |title=Chloroform-induced multiple forms of ornithine decarboxylase: differential sensitivity of forms to enhancement by diethyl maleate and inhibition by ODC-antizyme |journal=Journal of toxicology and environmental health |volume=27 |issue= 1 |pages= 57–64 |year= 1989 |pmid= 2724368 |doi=10.1080/15287398909531278 |name-list-format=vanc| author2=Nofzinger K  | author3=Bedell C  | display-authors=3  | last4=Deangelo  | first4=Anthony  | last5=Pereira  | first5=Michael }}
*{{cite journal | author=Tewari DS, Qian Y, Thornton RD, ''et al.'' |title=Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme. |journal=Biochim. Biophys. Acta |volume=1209 |issue= 2 |pages= 293-5 |year= 1995 |pmid= 7811704 |doi=  }}
*{{cite journal  | author=Matsufuji S |title=Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme |journal=Cell |volume=80 |issue= 1 |pages= 51–60 |year= 1995 |pmid= 7813017 |doi=10.1016/0092-8674(95)90450-6 |name-list-format=vanc| author2=Matsufuji T | author3=Miyazaki Y  | display-authors=3  | last4=Murakami  | first4=Y  | last5=Atkins  | first5=JF  | last6=Gesteland  | first6=RF  | last7=Hayashi  | first7=S }}
*{{cite journal  | author=Matsufuji S, Matsufuji T, Miyazaki Y, ''et al.'' |title=Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme. |journal=Cell |volume=80 |issue= 1 |pages= 51-60 |year= 1995 |pmid= 7813017 |doi=  }}
*{{cite journal  | author=Mamroud-Kidron E |title=A unified pathway for the degradation of ornithine decarboxylase in reticulocyte lysate requires interaction with the polyamine-induced protein, ornithine decarboxylase antizyme |journal=Eur. J. Biochem. |volume=226 |issue= 2 |pages= 547–554 |year= 1995 |pmid= 8001569 |doi=10.1111/j.1432-1033.1994.tb20079.x |name-list-format=vanc| author2=Omer-Itsicovich M  | author3=Bercovich Z  | display-authors=3  | last4=Tobias  | first4=Karin E. | last5=Rom  | first5=Eran  | last6=Kahana  | first6=Chaim  }}
*{{cite journal | author=Mamroud-Kidron E, Omer-Itsicovich M, Bercovich Z, ''et al.'' |title=A unified pathway for the degradation of ornithine decarboxylase in reticulocyte lysate requires interaction with the polyamine-induced protein, ornithine decarboxylase antizyme. |journal=Eur. J. Biochem. |volume=226 |issue= 2 |pages= 547-54 |year= 1995 |pmid= 8001569 |doi=  }}
*{{cite journal  | author=Ichiba T |title=Functional regions of ornithine decarboxylase antizyme |journal=Biochem. Biophys. Res. Commun. |volume=200 |issue= 3 |pages= 1721–1727 |year= 1994 |pmid= 8185631 |doi= 10.1006/bbrc.1994.1651 |name-list-format=vanc| author2=Matsufuji S | author3=Miyazaki Y  | display-authors=3  | last4=Murakami  | first4=Y  | last5=Tanaka  | first5=K  | last6=Ichihara  | first6=A  | last7=Hayashi | first7=S }}
*{{cite journal  | author=Ichiba T, Matsufuji S, Miyazaki Y, ''et al.'' |title=Functional regions of ornithine decarboxylase antizyme. |journal=Biochem. Biophys. Res. Commun. |volume=200 |issue= 3 |pages= 1721-7 |year= 1994 |pmid= 8185631 |doi= 10.1006/bbrc.1994.1651 }}
*{{cite journal  | author=Yang D |title=Molcecular cloning of human antizyme cDNA |journal=Biochem. Mol. Biol. Int. |volume=38 |issue= 5 |pages= 957–64 |year= 1997 |pmid= 9132164 |doi=  |name-list-format=vanc| author2=Takii T | author3=Hayashi H | display-authors=3  | last4=Itoh  | first4=S  | last5=Hayashi  | first5=M  | last6=Onozaki  | first6=K  }}
*{{cite journal | author=Matsufuji S, Inazawa J, Hayashi T, ''et al.'' |title=Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization. |journal=Genomics |volume=38 |issue= 1 |pages= 102-4 |year= 1997 |pmid= 8954789 |doi=  }}
*{{cite journal  |vauthors=Hayashi T, Matsufuji S, Hayashi S |title=Characterization of the human antizyme gene |journal=Gene |volume=203 |issue= 2 |pages= 131–139 |year= 1998 |pmid= 9426243 |doi=10.1016/S0378-1119(97)00504-0 }}
*{{cite journal  | author=Yang D, Takii T, Hayashi H, ''et al.'' |title=Molcecular cloning of human antizyme cDNA. |journal=Biochem. Mol. Biol. Int. |volume=38 |issue= 5 |pages= 957-64 |year= 1997 |pmid= 9132164 |doi= }}
*{{cite journal  |vauthors=Zhu C, Lang DW, Coffino P |title=Antizyme2 is a negative regulator of ornithine decarboxylase and polyamine transport |journal=J. Biol. Chem. |volume=274 |issue= 37 |pages= 26425–26430 |year= 1999 |pmid= 10473601 |doi=10.1074/jbc.274.37.26425  }}
*{{cite journal | author=Hayashi T, Matsufuji S, Hayashi S |title=Characterization of the human antizyme gene. |journal=Gene |volume=203 |issue= 2 |pages= 131-9 |year= 1998 |pmid= 9426243 |doi=  }}
*{{cite journal  |vauthors=Chen H, MacDonald A, Coffino P |title=Structural elements of antizymes 1 and 2 are required for proteasomal degradation of ornithine decarboxylase |journal=J. Biol. Chem. |volume=277 |issue= 48 |pages= 45957–45961 |year= 2003 |pmid= 12359729 |doi= 10.1074/jbc.M206799200 }}
*{{cite journal  | author=Zhu C, Lang DW, Coffino P |title=Antizyme2 is a negative regulator of ornithine decarboxylase and polyamine transport. |journal=J. Biol. Chem. |volume=274 |issue= 37 |pages= 26425-30 |year= 1999 |pmid= 10473601 |doi=  }}
*{{cite journal  | author=Ike A |title=Structure and promoter activity of the gene encoding ornithine decarboxylase antizyme expressed exclusively in haploid germ cells in testis (OAZt/Oaz3) |journal=Gene |volume=298 |issue= 2 |pages= 183–193 |year= 2003 |pmid= 12426106 |doi=10.1016/S0378-1119(02)00978-2 |name-list-format=vanc| author2=Yamada S  | author3=Tanaka H  | display-authors=3  | last4=Nishimune  | first4=Y  | last5=Nozaki  | first5=M  }}
*{{cite journal | author=Chen H, MacDonald A, Coffino P |title=Structural elements of antizymes 1 and 2 are required for proteasomal degradation of ornithine decarboxylase. |journal=J. Biol. Chem. |volume=277 |issue= 48 |pages= 45957-61 |year= 2003 |pmid= 12359729 |doi= 10.1074/jbc.M206799200 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Ike A, Yamada S, Tanaka H, ''et al.'' |title=Structure and promoter activity of the gene encoding ornithine decarboxylase antizyme expressed exclusively in haploid germ cells in testis (OAZt/Oaz3). |journal=Gene |volume=298 |issue= 2 |pages= 183-93 |year= 2003 |pmid= 12426106 |doi=  }}
*{{cite journal  | author=Grimwood J |title=The DNA sequence and biology of human chromosome 19 |journal=Nature |volume=428 |issue= 6982 |pages= 529–535 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399  |name-list-format=vanc| author2=Gordon LA  | author3=Olsen A  | display-authors=3  | last4=Terry  | first4=Astrid  | last5=Schmutz  | first5=Jeremy  | last6=Lamerdin  | first6=Jane  | last7=Hellsten  | first7=Uffe  | last8=Goodstein  | first8=David  | last9=Couronne  | first9=Olivier }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Mangold U, Leberer E |title=Regulation of all members of the antizyme family by antizyme inhibitor |journal=Biochem. J. |volume=385 |issue= Pt 1 |pages= 21–8 |year= 2005 |pmid= 15355308 |doi= 10.1042/BJ20040547  | pmc=1134669 }}
*{{cite journal  | author=Grimwood J, Gordon LA, Olsen A, ''et al.'' |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529-35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 }}
*{{cite journal  | author=Choi KS |title=Stable siRNA-mediated silencing of antizyme inhibitor: regulation of ornithine decarboxylase activity |journal=Biochem. Biophys. Res. Commun. |volume=328 |issue= 1 |pages= 206–212 |year= 2005 |pmid= 15670771 |doi= 10.1016/j.bbrc.2004.11.172  |name-list-format=vanc| author2=Suh YH  | author3=Kim WH  | display-authors=3  | last4=Lee  | first4=T  | last5=Jung  | first5=M }}
*{{cite journal  | author=Mangold U, Leberer E |title=Regulation of all members of the antizyme family by antizyme inhibitor. |journal=Biochem. J. |volume=385 |issue= Pt 1 |pages= 21-8 |year= 2005 |pmid= 15355308 |doi= 10.1042/BJ20040547 }}
*{{cite journal  | author=Ku M |title=OAZ regulates bone morphogenetic protein signaling through Smad6 activation |journal=J. Biol. Chem. |volume=281 |issue= 8 |pages= 5277–5287 |year= 2006 |pmid= 16373339 |doi= 10.1074/jbc.M510004200  |name-list-format=vanc| author2=Howard S  | author3=Ni W  | display-authors=3  | last4=Lagna  | first4=G  | last5=Hata  | first5=A }}
*{{cite journal | author=Choi KS, Suh YH, Kim WH, ''et al.'' |title=Stable siRNA-mediated silencing of antizyme inhibitor: regulation of ornithine decarboxylase activity. |journal=Biochem. Biophys. Res. Commun. |volume=328 |issue= 1 |pages= 206-12 |year= 2005 |pmid= 15670771 |doi= 10.1016/j.bbrc.2004.11.172 }}
*{{cite journal  | author=Lim J |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration |journal=Cell |volume=125 |issue= 4 |pages= 801–814 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032  |name-list-format=vanc| author2=Hao T  | author3=Shaw C  | display-authors=3  | last4=Patel  | first4=Akash J.  | last5=Szabó  | first5=Gábor  | last6=Rual  | first6=Jean-François  | last7=Fisk  | first7=C. Joseph  | last8=Li  | first8=Ning  | last9=Smolyar  | first9=Alex }}
*{{cite journal  | author=Ku M, Howard S, Ni W, ''et al.'' |title=OAZ regulates bone morphogenetic protein signaling through Smad6 activation. |journal=J. Biol. Chem. |volume=281 |issue= 8 |pages= 5277-87 |year= 2006 |pmid= 16373339 |doi= 10.1074/jbc.M510004200 }}
*{{cite journal  | author=Tsuji T |title=Ornithine decarboxylase antizyme upregulates DNA-dependent protein kinase and enhances the nonhomologous end-joining repair of DNA double-strand breaks in human oral cancer cells |journal=Biochemistry |volume=46 |issue= 31 |pages= 8920–8932 |year= 2007 |pmid= 17630775 |doi= 10.1021/bi7000328  |name-list-format=vanc| author2=Katsurano M  | author3=Ibaragi S  | display-authors=3  | last4=Shima  | first4=Kaori  | last5=Sasaki  | first5=Akira  | last6=Hu  | first6=Guo-fu }}
*{{cite journal | author=Lim J, Hao T, Shaw C, ''et al.'' |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801-14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }}
*{{cite journal | author=Tsuji T, Katsurano M, Ibaragi S, ''et al.'' |title=Ornithine decarboxylase antizyme upregulates DNA-dependent protein kinase and enhances the nonhomologous end-joining repair of DNA double-strand breaks in human oral cancer cells. |journal=Biochemistry |volume=46 |issue= 31 |pages= 8920-32 |year= 2007 |pmid= 17630775 |doi= 10.1021/bi7000328 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 00:20, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Ornithine decarboxylase antizyme is an enzyme that in humans is encoded by the OAZ1 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 and accelerates its degradation.[3]

References

  1. ↑ Tewari DS, Qian Y, Thornton RD, Pieringer J, Taub R, Mochan E, Tewari M (Feb 1995). "Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme". Biochim Biophys Acta. 1209 (2): 293–5. doi:10.1016/0167-4838(94)90199-6. PMID 7811704.
  2. ↑ Matsufuji S, Inazawa J, Hayashi T, Miyazaki Y, Ichiba T, Furusaka A, Matsufuji T, Atkins JF, Gesteland RF, Murakami Y, Hayashi S (Mar 1997). "Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization". Genomics. 38 (1): 102–104. doi:10.1006/geno.1996.0601. PMID 8954789.
  3. ↑ 3.0 3.1 "Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1".

Further reading



Retrieved from "https://www.wikidoc.org/index.php?title=OAZ1&oldid=1418908"