AZIN1

Protein-coding gene in the species Homo sapiens
AZIN1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4ZGZ

Identifiers
AliasesAZIN1, AZI, AZIA1, OAZI, OAZIN, ODC1L, antizyme inhibitor 1, AZI1
External IDsOMIM: 607909; MGI: 1859169; HomoloGene: 22933; GeneCards: AZIN1; OMA:AZIN1 - orthologs
Gene location (Human)
Chromosome 8 (human)
Chr.Chromosome 8 (human)[1]
Chromosome 8 (human)
Genomic location for AZIN1
Genomic location for AZIN1
Band8q22.3Start102,826,111 bp[1]
End102,893,864 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for AZIN1
Genomic location for AZIN1
Band15|15 B3.1Start38,487,671 bp[2]
End38,519,510 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 15: 38.49 – 38.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000155096 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: AZIN1 antizyme inhibitor 1".

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.


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