NAT8

NAT8
Identifiers
Aliases	NAT8, ATase2, CML1, GLA, Hcml1, TSC501, TSC510, CCNAT, N-acetyltransferase 8 (putative)
External IDs	OMIM: 606716 MGI: 1915646 HomoloGene: 9479 GeneCards: NAT8
EC number	2.3.1.80
Gene location (Human)
Chr.	Chromosome 2 (human)
End	73,642,422 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	85,809,064 bp
RNA expression pattern
	Top expressed in
	kidney tubule; ; renal cortex; ; kidney; ; metanephric glomerulus; ; glomerulus; ; liver; ; Right lobe of liver;
	More reference expression data
	n/a
Gene ontology
Molecular function	transferase activity; cysteine-S-conjugate N-acetyltransferase activity; acyltransferase activity; GO:0001948 protein binding; lysine N-acetyltransferase activity, acting on acetyl phosphate as donor;
Cellular component	integral component of membrane; endoplasmic reticulum-Golgi intermediate compartment membrane; endoplasmic reticulum membrane; membrane; endoplasmic reticulum-Golgi intermediate compartment; endoplasmic reticulum;
Biological process	peptidyl-lysine N6-acetylation; cellular protein metabolic process; positive regulation of gene expression; negative regulation of apoptotic process; amyloid-beta metabolic process; glutathione metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	9027
	68396
	ENSG00000144035
	ENSMUSG00000030004
	Q9UHE5
	Q9JIY7
	NM_003960
	NM_023455; NM_001362060
	NP_003951
	NP_075944; NP_001348989
	Wikidata
View/Edit Human	View/Edit Mouse

N-acetyltransferase 8 is a protein that in humans is encoded by the NAT8 gene.^[5]

Clinical relevance[]

Mutations in the NAT8 gene have been associated with chronic kidney disease.^[6]

References[]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000144035 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000030004 - 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.
^ "Entrez Gene: N-acetyltransferase 8 (GCN5-related".
^ Suhre K, Shin SY, Petersen AK, Mohney RP, Meredith D, Wägele B, Altmaier E, Deloukas P, Erdmann J, Grundberg E, Hammond CJ, de Angelis MH, Kastenmüller G, Köttgen A, Kronenberg F, Mangino M, Meisinger C, Meitinger T, Mewes HW, Milburn MV, Prehn C, Raffler J, Ried JS, Römisch-Margl W, Samani NJ, Small KS, Wichmann HE, Zhai G, Illig T, Spector TD, Adamski J, Soranzo N, Gieger C (September 2011). "Human metabolic individuality in biomedical and pharmaceutical research". Nature. 477 (7362): 54–60. doi:10.1038/nature10354. PMC 3832838. PMID 21886157.

Further reading[]

Ko MH, Puglielli L (2009). "Two endoplasmic reticulum (ER)/ER Golgi intermediate compartment-based lysine acetyltransferases post-translationally regulate BACE1 levels". J. Biol. Chem. 284 (4): 2482–92. doi:10.1074/jbc.M804901200. PMC 2629114. PMID 19011241.
Ozaki K, Fujiwara T, Nakamura Y, Takahashi E (1998). "Isolation and mapping of a novel human kidney- and liver-specific gene homologous to the bacterial acetyltransferases". J. Hum. Genet. 43 (4): 255–8. doi:10.1007/s100380050084. PMID 9852678.
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. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
Veiga-da-Cunha M, Tyteca D, Stroobant V, et al. (2010). "Molecular identification of NAT8 as the enzyme that acetylates cysteine S-conjugates to mercapturic acids". J. Biol. Chem. 285 (24): 18888–98. doi:10.1074/jbc.M110.110924. PMC 2881811. PMID 20392701.
Ariyannur PS, Moffett JR, Manickam P, et al. (2010). "Methamphetamine-induced neuronal protein NAT8L is the NAA biosynthetic enzyme: implications for specialized acetyl coenzyme A metabolism in the CNS". Brain Res. 1335: 1–13. doi:10.1016/j.brainres.2010.04.008. PMID 20385109. S2CID 206324237.
Popsueva AE, Luchinskaya NN, Ludwig AV, et al. (2001). "Overexpression of camello, a member of a novel protein family, reduces blastomere adhesion and inhibits gastrulation in Xenopus laevis". Dev. Biol. 234 (2): 483–96. doi:10.1006/dbio.2001.0261. PMID 11397015.
Juhanson P, Kepp K, Org E, et al. (2008). "N-acetyltransferase 8, a positional candidate for blood pressure and renal regulation: resequencing, association and in silico study". BMC Med. Genet. 9: 25. doi:10.1186/1471-2350-9-25. PMC 2330028. PMID 18402670.
Veréb J, Démant F, Pavkovceková O, Tischler V (1975). "[Agenesis and aplasia of the kidney in children in the x-ray diagnostic picture]". Cesk Pediatr. 30 (3): 94–7. PMID 1139715.
Köttgen A, Pattaro C, Böger CA, et al. (2010). "New loci associated with kidney function and chronic kidney disease". Nat. Genet. 42 (5): 376–84. doi:10.1038/ng.568. PMC 2997674. PMID 20383146.
Chambers JC, Zhang W, Lord GM, et al. (2010). "Genetic loci influencing kidney function and chronic kidney disease". Nat. Genet. 42 (5): 373–5. doi:10.1038/ng.566. PMC 3748585. PMID 20383145.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000144035 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000030004 - 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.

[entrez-5] "Entrez Gene: N-acetyltransferase 8 (GCN5-related".

[pmid21886157-6] Suhre K, Shin SY, Petersen AK, Mohney RP, Meredith D, Wägele B, Altmaier E, Deloukas P, Erdmann J, Grundberg E, Hammond CJ, de Angelis MH, Kastenmüller G, Köttgen A, Kronenberg F, Mangino M, Meisinger C, Meitinger T, Mewes HW, Milburn MV, Prehn C, Raffler J, Ried JS, Römisch-Margl W, Samani NJ, Small KS, Wichmann HE, Zhai G, Illig T, Spector TD, Adamski J, Soranzo N, Gieger C (September 2011). "Human metabolic individuality in biomedical and pharmaceutical research". Nature. 477 (7362): 54–60. doi:10.1038/nature10354. PMC 3832838. PMID 21886157.

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v t Transferases: acyltransferases (EC 2.3)
2.3.1: other than amino-acyl groups	acetyltransferases: Acetyl-Coenzyme A acetyltransferase N-Acetylglutamate synthase Choline acetyltransferase Dihydrolipoyl transacetylase Acetyl-CoA C-acyltransferase Beta-galactoside transacetylase Chloramphenicol acetyltransferase N-acetyltransferase Serotonin N-acetyl transferase HGSNAT ARD1A Histone acetyltransferase P300/CBP NAT2 palmitoyltransferases: Carnitine O-palmitoyltransferase CPT1 CPT2 Serine C-palmitoyltransferase SPTLC1 SPTLC2 other: Acyltransferase like 2 Aminolevulinic acid synthase Beta-ketoacyl-ACP synthase Glyceronephosphate O-acyltransferase Lecithin—cholesterol acyltransferase Glycerol-3-phosphate O-acyltransferase 1-acylglycerol-3-phosphate O-acyltransferase 2-acylglycerol-3-phosphate O-acyltransferase ABHD5
2.3.2: Aminoacyltransferases	Gamma-glutamyl transpeptidase Peptidyl transferase Transglutaminase Tissue transglutaminase Keratinocyte transglutaminase Factor XIII
2.3.3: converted into alkyl on transfer	Citrate synthase Decylcitrate synthase Citrate (Re)-synthase Decylhomocitrate synthase 2-methylcitrate synthase 2-ethylmalate synthase 3-ethylmalate synthase ATP citrate lyase Malate synthase HMG-CoA synthase HMGCS2 2-hydroxyglutarate synthase 3-propylmalate synthase 2-isopropylmalate synthase Homocitrate synthase Sulfoacetaldehyde acetyltransferase

v t Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)