SAT1 (gene)

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Spermidine/spermine N1-acetyltransferase 1
PDB rendering based on 2b3u.
Available structures: 2b3u, 2b3v, 2b4b, 2b4d, 2b58, 2b5g, 2f5i, 2fxf, 2g3t, 2jev
Identifiers
Symbol(s) SAT1; DC21; KFSD; SAT; SSAT; SSAT-1
External IDs OMIM: 313020 MGI98233 HomoloGene37716
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 6303 20229
Ensembl ENSG00000130066 n/a
Uniprot P21673 n/a
Refseq NM_002970 (mRNA)
NP_002961 (protein)
NM_009121 (mRNA)
NP_033147 (protein)
Location Chr X: 23.71 - 23.71 Mb n/a
Pubmed search [1] [2]

Spermidine/spermine N1-acetyltransferase 1, also known as SAT1, is a human gene.[1]

Spermidine/spermine N(1)-acetyltransferase (SPD/SPM acetyltransferase) is a rate-limiting enzyme in the catabolic pathway of polyamine metabolism. It catalyzes the N(1)-acetylation of spermidine and spermine and, by the successive activity of polyamine oxidase, spermine can be converted to spermidine and spermidine to putrescine.[supplied by OMIM][1]

[edit] References

[edit] Further reading

  • Lake JA, Carr J, Feng F, et al. (2003). "The role of Vif during HIV-1 infection: interaction with novel host cellular factors.". J. Clin. Virol. 26 (2): 143–52. PMID 12600646. 
  • Xiao L, Celano P, Mank AR, et al. (1992). "Structure of the human spermidine/spermine N1-acetyltransferase gene (exon/intron gene organization and localization to Xp22.1).". Biochem. Biophys. Res. Commun. 187 (3): 1493–502. PMID 1417826. 
  • Xiao L, Celano P, Mank AR, et al. (1991). "Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase.". Biochem. Biophys. Res. Commun. 179 (1): 407–15. PMID 1652956. 
  • Casero RA, Celano P, Ervin SJ, et al. (1991). "Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase.". J. Biol. Chem. 266 (2): 810–4. PMID 1985966. 
  • Libby PR, Ganis B, Bergeron RJ, Porter CW (1991). "Characterization of human spermidine/spermine N1-acetyltransferase purified from cultured melanoma cells.". Arch. Biochem. Biophys. 284 (2): 238–44. PMID 1989509. 
  • Casero RA, Celano P, Ervin SJ, et al. (1990). "High specific induction of spermidine/spermine N1-acetyltransferase in a human large cell lung carcinoma.". Biochem. J. 270 (3): 615–20. PMID 2241897. 
  • Casero RA, Gabrielson EW, Pegg AE (1994). "Immunohistochemical staining of human spermidine/spermine N1-acetyltransferase superinduced in response to treatment with antitumor polyamine analogues.". Cancer Res. 54 (15): 3955–8. PMID 8033120. 
  • Xiao L, Casero RA (1996). "Differential transcription of the human spermidine/spermine N1-acetyltransferase (SSAT) gene in human lung carcinoma cells.". Biochem. J. 313 ( Pt 2): 691–6. PMID 8573111. 
  • Coleman CS, Huang H, Pegg AE (1996). "Structure and critical residues at the active site of spermidine/spermine-N1-acetyltransferase.". Biochem. J. 316 ( Pt 3): 697–701. PMID 8670140. 
  • Bordin L, Vargiu C, Colombatto S, et al. (1997). "Casein kinase 2 phosphorylates recombinant human spermidine/spermine N1-acetyltransferase on both serine and threonine residues.". Biochem. Biophys. Res. Commun. 229 (3): 845–51. doi:10.1006/bbrc.1996.1890. PMID 8954982. 
  • Bettuzzi S, Davalli P, Astancolle S, et al. (2000). "Tumor progression is accompanied by significant changes in the levels of expression of polyamine metabolism regulatory genes and clusterin (sulfated glycoprotein 2) in human prostate cancer specimens.". Cancer Res. 60 (1): 28–34. PMID 10646846. 
  • Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMID 11256614. 
  • Coleman CS, Pegg AE (2001). "Polyamine analogues inhibit the ubiquitination of spermidine/spermine N1-acetyltransferase and prevent its targeting to the proteasome for degradation.". Biochem. J. 358 (Pt 1): 137–45. PMID 11485561. 
  • Bordin L, Vargiu C, Clari G, et al. (2002). "Phosphorylation of recombinant human spermidine/spermine N(1)-acetyltransferase by CK1 and modulation of its binding to mitochondria: a comparison with CK2.". Biochem. Biophys. Res. Commun. 290 (1): 463–8. doi:10.1006/bbrc.2001.6204. PMID 11779193. 
  • Nikiforova NN, Velikodvorskaja TV, Kachko AV, et al. (2002). "Induction of alternatively spliced spermidine/spermine N1-acetyltransferase mRNA in the human kidney cells infected by venezuelan equine encephalitis and tick-borne encephalitis viruses.". Virology 297 (2): 163–71. PMID 12083816. 
  • Gimelli G, Giglio S, Zuffardi O, et al. (2002). "Gene dosage of the spermidine/spermine N(1)-acetyltransferase ( SSAT) gene with putrescine accumulation in a patient with a Xp21.1p22.12 duplication and keratosis follicularis spinulosa decalvans (KFSD).". Hum. Genet. 111 (3): 235–41. doi:10.1007/s00439-002-0791-6. PMID 12215835. 
  • Tomitori H, Nenoi M, Mita K, et al. (2003). "Functional characterization of the human spermidine/spermine N(1)-acetyltransferase gene promoter.". Biochim. Biophys. Acta 1579 (2-3): 180–4. PMID 12427553. 
  • 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:10.1073/pnas.242603899. PMID 12477932. 
  • Izmailova E, Bertley FM, Huang Q, et al. (2003). "HIV-1 Tat reprograms immature dendritic cells to express chemoattractants for activated T cells and macrophages.". Nat. Med. 9 (2): 191–7. doi:10.1038/nm822. PMID 12539042.