NAT8

N-acetyltransferase 8 (GCN5-related, putative)

Identifiers

NAT8 ; ATase2; CCNAT; CML1; GLA; Hcml1; TSC501; TSC510

External IDs

OMIM: 606716 MGI: 1915646 HomoloGene: 9479 GeneCards: NAT8 Gene

2.3.1.80

Gene ontology
Molecular function	• lysine N-acetyltransferase activity, acting on acetyl phosphate as donor • protein binding • cysteine-S-conjugate N-acetyltransferase activity
Cellular component	• endoplasmic reticulum membrane • endoplasmic reticulum-Golgi intermediate compartment • integral component of membrane • endoplasmic reticulum-Golgi intermediate compartment membrane • extracellular exosome
Biological process	• glutathione metabolic process • positive regulation of gene expression • peptidyl-lysine N6-acetylation • response to drug • negative regulation of apoptotic process • beta-amyloid metabolic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
73.64 – 73.64 Mb

Chr 6:
85.83 – 85.83 Mb

PubMed search

N-acetyltransferase 8 is a protein that in humans is encoded by the NAT8 gene.^[1]

Clinical relevance

Mutations in the NAT8 gene have been associated with chronic kidney disease.^[2]

References

↑ "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. PMID 21886157.

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.
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.
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. PMID 20383145.

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 ATP citrate lyase HMG-CoA synthase Malate synthase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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NAT8

Clinical relevance

References

Further reading