| 释义 |
- References
- Further reading
{{About|the human gene|the submarine communications cable|SAT-2|the SAT II tests|SAT Subject Tests}}{{Infobox_gene}}Diamine acetyltransferase 2 is an enzyme that in humans is encoded by the SAT2 gene.[1][2][3]SAT2 maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate.[4] {{PBB_Summary
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}}References1. ^{{cite journal | vauthors = Coleman CS, Stanley BA, Jones AD, Pegg AE | title = Spermidine/spermine-N1-acetyltransferase-2 (SSAT2) acetylates thialysine and is not involved in polyamine metabolism | journal = Biochem J | volume = 384 | issue = Pt 1 | pages = 139–48 |date=Nov 2004 | pmid = 15283699 | pmc = 1134097 | doi = 10.1042/BJ20040790 }}
2. ^{{cite journal | vauthors = Baek JH, Liu YV, McDonald KR, Wesley JB, Hubbi ME, Byun H, Semenza GL | title = Spermidine/spermine-N1-acetyltransferase 2 is an essential component of the ubiquitin ligase complex that regulates hypoxia-inducible factor 1alpha | journal = J Biol Chem | volume = 282 | issue = 32 | pages = 23572–80 |date=Aug 2007 | pmid = 17558023 | pmc = | doi = 10.1074/jbc.M703504200 }}
3. ^{{cite web | title = Entrez Gene: SAT2 spermidine/spermine N1-acetyltransferase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=112483| accessdate = }}
4. ^{{cite journal | vauthors = Jenstad M, Quazi AZ, Zilberter M, Haglerød C, Berghuis P, Saddique N, Goiny M, Buntup D, Davanger S, S Haug FM, Barnes CA, McNaughton BL, Ottersen OP, Storm-Mathisen J, Harkany T, Chaudhry FA | title = System A transporter SAT2 mediates replenishment of dendritic glutamate pools controlling retrograde signaling by glutamate. | journal = Cereb Cortex | volume = 19 | issue = 5 | pages = 1092–106 |date=May 2009 | pmid = 18832333 | pmc = | doi = 10.1093/cercor/bhn151}}
Further reading{{refbegin | 2}}- {{cite journal |vauthors=Baek JH, Liu YV, McDonald KR, etal |title=Spermidine/spermine N(1)-acetyltransferase-1 binds to hypoxia-inducible factor-1alpha (HIF-1alpha) and RACK1 and promotes ubiquitination and degradation of HIF-1alpha. |journal=J. Biol. Chem. |volume=282 |issue= 46 |pages= 33358–66 |year= 2008 |pmid= 17875644 |doi= 10.1074/jbc.M705627200 }}
- {{cite journal |vauthors=Gornati R, Chini V, Rimoldi S, etal |title=Evaluation of SAT-1, SAT-2 and GalNAcT-1 mRNA in colon cancer by real-time PCR. |journal=Mol. Cell. Biochem. |volume=298 |issue= 1–2 |pages= 59–68 |year= 2007 |pmid= 17119850 |doi= 10.1007/s11010-006-9350-0 }}
- {{cite journal | vauthors=Han BW, Bingman CA, Wesenberg GE, Phillips GN |title=Crystal structure of Homo sapiens thialysine Nepsilon-acetyltransferase (HsSSAT2) in complex with acetyl coenzyme A |journal=Proteins |volume=64 |issue= 1 |pages= 288–93 |year= 2006 |pmid= 16596569 |doi= 10.1002/prot.20967 }}
- {{cite journal |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
- {{cite journal |vauthors=Barrios-Rodiles M, Brown KR, Ozdamar B, etal |title=High-throughput mapping of a dynamic signaling network in mammalian cells |journal=Science |volume=307 |issue= 5715 |pages= 1621–5 |year= 2005 |pmid= 15761153 |doi= 10.1126/science.1105776 }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
- {{cite journal |vauthors=Chen Y, Vujcic S, Liang P, etal |title=Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase |journal=Biochem. J. |volume=373 |issue= Pt 3 |pages= 661–7 |year= 2003 |pmid= 12803540 |doi= 10.1042/BJ20030734 | pmc=1223561 }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }}
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