AZIN1

Antizyme inhibitor 1 is a protein that in humans is encoded by the AZIN1 gene.^[5][6][7]

AZIN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4ZGZ
Identifiers
Aliases	AZIN1, AZI, AZIA1, OAZI, OAZIN, ODC1L, antizyme inhibitor 1, AZI1
External IDs	OMIM: 607909; MGI: 1859169; HomoloGene: 22933; GeneCards: AZIN1; OMA:AZIN1 - orthologs
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8q22.3 Start 102,826,111 bp[1] End 102,893,864 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 B3.1 Start 38,487,671 bp[2] End 38,519,510 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bronchial epithelial cell ventricular zone epithelium of nasopharynx ganglionic eminence epithelium of colon cartilage tissue placenta bone marrow cells jejunal mucosa body of pancreas Top expressed in fetal liver hematopoietic progenitor cell atrioventricular valve barrel cortex spermatocyte decidua lacrimal gland atrium epithelium of lens spermatid salivary gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ornithine decarboxylase activator activity protein binding catalytic activity ornithine decarboxylase activity Cellular component cytosol nucleus cytoplasm Biological process polyamine biosynthetic process positive regulation of polyamine transmembrane transport regulation of cellular amino acid metabolic process putrescine biosynthetic process from ornithine positive regulation of catalytic activity negative regulation of protein catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51582 54375 Ensembl ENSG00000155096 ENSMUSG00000037458 UniProt O14977 O35484 RefSeq (mRNA) NM_001301668 NM_015878 NM_148174 NM_001363010 NM_001363011 NM_001363012 NM_001363013 NM_001363014 NM_001363024 NM_001363083 NM_001102458 NM_001301688 NM_018745 RefSeq (protein) NP_001288597 NP_056962 NP_680479 NP_001349939 NP_001349940 NP_001349941 NP_001349942 NP_001349943 NP_001349953 NP_001350012 NP_001095928 NP_001288617 NP_061215 Location (UCSC) Chr 8: 102.83 – 102.89 Mb Chr 15: 38.49 – 38.52 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Ornithine decarboxylase (ODC) catalyzes the conversion of ornithine to putrescine in the first and apparently rate-limiting step in polyamine biosynthesis. Ornithine decarboxylase antizymes play a role in the regulation of polyamine synthesis by binding to and inhibiting ornithine decarboxylase. The protein encoded by this gene is highly similar to ODC. It binds to ODC antizyme and stabilizes ODC, thus inhibiting antizyme-mediated ODC degradation. Two alternatively spliced transcript variants have been found for this gene.^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000155096 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000037458 – 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. Koguchi K, Kobayashi S, Hayashi T, Matsufuji S, Murakami Y, Hayashi S (Nov 1997). "Cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme inhibitor". Biochim Biophys Acta. 1353 (3): 209–16. doi:10.1016/s0167-4781(97)00106-1. PMID 9349715.
6. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Jun 1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
7. "Entrez Gene: AZIN1 antizyme inhibitor 1".

External links

• Human AZIN1 genome location and AZIN1 gene details page in the UCSC Genome Browser.

Further reading

• Murakami Y, Matsufuji S, Hayashi S, et al. (2000). "Degradation of ornithine decarboxylase by the 26S proteasome". Biochem. Biophys. Res. Commun. 267 (1): 1–6. doi:10.1006/bbrc.1999.1706. PMID 10623564.
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• 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.
• Imabayashi H, Mori T, Gojo S, et al. (2003). "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis". Exp. Cell Res. 288 (1): 35–50. doi:10.1016/S0014-4827(03)00130-7. PMID 12878157.
• Reuter TY, Medhurst AL, Waisfisz Q, et al. (2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Exp. Cell Res. 289 (2): 211–21. doi:10.1016/S0014-4827(03)00261-1. PMID 14499622.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• 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.