NAT8

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

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)[1] Band 2p13.1 Start 73,640,723 bp[1] End 73,642,422 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6|6 C3 Start 85,830,388 bp[2] End 85,832,082 bp[2]
Gene ontology Molecular function • transferase activity • cysteine-S-conjugate N-acetyltransferase activity • transferase activity, transferring acyl groups • 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 • response to drug Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9027	68396
Ensembl	ENSG00000144035	ENSMUSG00000030004
UniProt	Q9UHE5	Q9JIY7
RefSeq (mRNA)	NM_003960	NM_023455 NM_001362060
RefSeq (protein)	NP_003951	NP_075944 NP_001348989
Location (UCSC)	Chr 2: 73.64 – 73.64 Mb	Chr 6: 85.83 – 85.83 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Clinical relevance

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

References

1. GRCh38: Ensembl release 89: ENSG00000144035 - Ensembl, May 2017
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.
5. "Entrez Gene: N-acetyltransferase 8 (GCN5-related".
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.

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.
• 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. PMC 3748585. PMID 20383145.