SAT2

In this article we are going to address the topic of SAT2 from different perspectives, with the aim of delving into its importance and relevance today. SAT2 is a topic that has generated great interest in different areas, since its influence extends to numerous areas of society. Throughout this article, we will analyze the different facets of SAT2, exploring its impact on everyday life, its evolution over time, and possible future implications. In addition, we will examine the opinions and reflections of experts in the field, as well as the experiences of people who have closely experienced the influence of SAT2 in their lives. In short, this article aims to offer a deep and complete vision of SAT2, in order to enrich knowledge and understanding of this exciting topic.

Protein-coding gene in the species Homo sapiens

This article is about the human gene. For the submarine communications cable, see SAT-2. For the SAT II tests, see SAT Subject Tests.

SAT2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2BEI, 2Q4V
Identifiers
Aliases	SAT2, Sspermidine/spermine N1-acetyltransferase family member 2, SSAT-2
External IDs	OMIM: 611463; MGI: 1916465; HomoloGene: 44215; GeneCards: SAT2; OMA:SAT2 - orthologs
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p13.1 Start 7,626,234 bp[1] End 7,627,876 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B3 Start 69,512,850 bp[2] End 69,514,696 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal cortex left adrenal cortex jejunal mucosa right lobe of liver mucosa of ileum duodenum human kidney left ovary right ovary anterior pituitary Top expressed in otolith organ utricle retinal pigment epithelium right kidney proximal tubule otic vesicle Rostral migratory stream internal carotid artery external carotid artery epithelium of lens More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity N-acetyltransferase activity acyltransferase activity diamine N-acetyltransferase activity protein binding identical protein binding spermidine binding Cellular component cytoplasm extracellular exosome Biological process putrescine acetylation spermine acetylation nor-spermidine metabolic process spermidine acetylation putrescine catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 112483 69215 Ensembl ENSG00000141504 ENSMUSG00000069835 UniProt Q96F10 Q6P8J2 RefSeq (mRNA) NM_133491 NM_001320845 NM_001320846 NM_001320847 NM_026991 NM_001356468 NM_001356469 RefSeq (protein) NP_001307774 NP_001307775 NP_001307776 NP_597998 NP_081267 NP_001343397 NP_001343398 Location (UCSC) Chr 17: 7.63 – 7.63 Mb Chr 11: 69.51 – 69.51 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Diamine acetyltransferase 2 is an enzyme that in humans is encoded by the SAT2 gene.^[5][6][7] SAT2 maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate.^[8]

References

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000141504 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000069835 – 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. ^ Coleman CS, Stanley BA, Jones AD, Pegg AE (Nov 2004). "Spermidine/spermine-N1-acetyltransferase-2 (SSAT2) acetylates thialysine and is not involved in polyamine metabolism". Biochem J. 384 (Pt 1): 139–48. doi:10.1042/BJ20040790. PMC 1134097. PMID 15283699.
6. ^ Baek JH, Liu YV, McDonald KR, Wesley JB, Hubbi ME, Byun H, Semenza GL (Aug 2007). "Spermidine/spermine-N1-acetyltransferase 2 is an essential component of the ubiquitin ligase complex that regulates hypoxia-inducible factor 1alpha". J Biol Chem. 282 (32): 23572–80. doi:10.1074/jbc.M703504200. PMID 17558023.
7. ^ "Entrez Gene: SAT2 spermidine/spermine N1-acetyltransferase 2".
8. ^ 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 (May 2009). "System A transporter SAT2 mediates replenishment of dendritic glutamate pools controlling retrograde signaling by glutamate". Cereb Cortex. 19 (5): 1092–106. doi:10.1093/cercor/bhn151. PMID 18832333.

Further reading

• Baek JH, Liu YV, McDonald KR, et al. (2008). "Spermidine/spermine N(1)-acetyltransferase-1 binds to hypoxia-inducible factor-1alpha (HIF-1alpha) and RACK1 and promotes ubiquitination and degradation of HIF-1alpha". J. Biol. Chem. 282 (46): 33358–66. doi:10.1074/jbc.M705627200. PMID 17875644.
• Gornati R, Chini V, Rimoldi S, et al. (2007). "Evaluation of SAT-1, SAT-2 and GalNAcT-1 mRNA in colon cancer by real-time PCR". Mol. Cell. Biochem. 298 (1–2): 59–68. doi:10.1007/s11010-006-9350-0. hdl:11383/1672116. PMID 17119850. S2CID 29889795.
• Han BW, Bingman CA, Wesenberg GE, Phillips GN (2006). "Crystal structure of Homo sapiens thialysine Nepsilon-acetyltransferase (HsSSAT2) in complex with acetyl coenzyme A". Proteins. 64 (1): 288–93. doi:10.1002/prot.20967. PMID 16596569.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Barrios-Rodiles M, Brown KR, Ozdamar B, et al. (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
• 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.
• Chen Y, Vujcic S, Liang P, et al. (2003). "Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase". Biochem. J. 373 (Pt 3): 661–7. doi:10.1042/BJ20030734. PMC 1223561. PMID 12803540.
• 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.

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