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SAT2

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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]
Band	17p13.1	End	7,627,876 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11\|11 B3	Start	69,512,850 bp^[2]
Band	11\|11 B3	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

[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000141504 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000069835 – Ensembl, May 2017

^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ 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.

^ 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.

^ "Entrez Gene: SAT2 spermidine/spermine N1-acetyltransferase 2".

^ 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.

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.

v t e PDB gallery
2bei: X-ray structure of thialysine n-acetyltransferase (SSAT2) from homo sapiens

This article on a gene on human chromosome 17 is a stub. You can help Wikipedia by expanding it.

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