Arylamine N-acetyltransferase 2

Details

Name
Arylamine N-acetyltransferase 2
Synonyms
  • 2.3.1.5
  • AAC2
  • Arylamide acetylase 2
  • N-acetyltransferase type 2
  • NAT-2
  • PNAT
  • Polymorphic arylamine N-acetyltransferase
Gene Name
NAT2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0006940|Arylamine N-acetyltransferase 2
MDIEAYFERIGYKNSRNKLDLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIV
RRNRGGWCLQVNQLLYWALTTIGFQTTMLGGYFYIPPVNKYSTGMVHLLLQVTIDGRNYI
VDAGSGSSSQMWQPLELISGKDQPQVPCIFCLTEERGIWYLDQIRREQYITNKEFLNSHL
LPKKKHQKIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFILT
YRKFNYKDNTDLVEFKTLTEEEVEEVLKNIFKISLGRNLVPKPGDGSLTI
Number of residues
290
Molecular Weight
33542.235
Theoretical pI
5.67
GO Classification
Functions
arylamine N-acetyltransferase activity
Processes
small molecule metabolic process / xenobiotic metabolic process
Components
cytosol
General Function
Arylamine n-acetyltransferase activity
Specific Function
Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0012509|Arylamine N-acetyltransferase 2 (NAT2)
ATGGACATTGAAGCATATTTTGAAAGAATTGGCTATAAGAACTCTAGGAACAAATTGGAC
TTGGAAACATTAACTGACATTCTTGAGCACCAGATCCGGGCTGTTCCCTTTGAGAACCTT
AACATGCATTGTGGGCAAGCCATGGAGTTGGGCTTAGAGGCTATTTTTGATCACATTGTA
AGAAGAAACCGGGGTGGGTGGTGTCTCCAGGTCAATCAACTTCTGTACTGGGCTCTGACC
ACAATCGGTTTTCAGACCACAATGTTAGGAGGGTATTTTTACATCCCTCCAGTTAACAAA
TACAGCACTGGCATGGTTCACCTTCTCCTGCAGGTGACCATTGACGGCAGGAATTACATT
GTCGATGCTGGGTCTGGAAGCTCCTCCCAGATGTGGCAGCCTCTAGAATTAATTTCTGGG
AAGGATCAGCCTCAGGTGCCTTGCATTTTCTGCTTGACAGAAGAGAGAGGAATCTGGTAC
CTGGACCAAATCAGGAGAGAGCAGTATATTACAAACAAAGAATTTCTTAATTCTCATCTC
CTGCCAAAGAAGAAACACCAAAAAATATACTTATTTACGCTTGAACCTCGAACAATTGAA
GATTTTGAGTCTATGAATACATACCTGCAGACGTCTCCAACATCTTCATTTATAACCACA
TCATTTTGTTCCTTGCAGACCCCAGAAGGGGTTTACTGTTTGGTGGGCTTCATCCTCACC
TATAGAAAATTCAATTATAAAGACAATACAGATCTGGTCGAGTTTAAAACTCTCACTGAG
GAAGAGGTTGAAGAAGTGCTGAGAAATATATTTAAGATTTCCTTGGGGAGAAATCTCGTG
CCCAAACCTGGTGATGGATCCCTTACTATTTAG
Chromosome Location
8
Locus
8p22
External Identifiers
ResourceLink
UniProtKB IDP11245
UniProtKB Entry NameARY2_HUMAN
GenBank Protein ID219412
GenBank Gene IDD90040
HGNC IDHGNC:7646
General References
  1. Grant DM, Blum M, Demierre A, Meyer UA: Nucleotide sequence of an intronless gene for a human arylamine N-acetyltransferase related to polymorphic drug acetylation. Nucleic Acids Res. 1989 May 25;17(10):3978. [Article]
  2. Blum M, Grant DM, McBride W, Heim M, Meyer UA: Human arylamine N-acetyltransferase genes: isolation, chromosomal localization, and functional expression. DNA Cell Biol. 1990 Apr;9(3):193-203. [Article]
  3. Ohsako S, Deguchi T: Cloning and expression of cDNAs for polymorphic and monomorphic arylamine N-acetyltransferases from human liver. J Biol Chem. 1990 Mar 15;265(8):4630-4. [Article]
  4. Deguchi T: Sequences and expression of alleles of polymorphic arylamine N-acetyltransferase of human liver. J Biol Chem. 1992 Sep 5;267(25):18140-7. [Article]
  5. Ferguson RJ, Doll MA, Rustan TD, Gray K, Hein DW: Cloning, expression, and functional characterization of two mutant (NAT2(191) and NAT2(341/803)) and wild-type human polymorphic N-acetyltransferase (NAT2) alleles. Drug Metab Dispos. 1994 May-Jun;22(3):371-6. [Article]
  6. Patin E, Barreiro LB, Sabeti PC, Austerlitz F, Luca F, Sajantila A, Behar DM, Semino O, Sakuntabhai A, Guiso N, Gicquel B, McElreavey K, Harding RM, Heyer E, Quintana-Murci L: Deciphering the ancient and complex evolutionary history of human arylamine N-acetyltransferase genes. Am J Hum Genet. 2006 Mar;78(3):423-36. Epub 2006 Jan 13. [Article]
  7. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [Article]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  9. Ebisawa T, Deguchi T: Structure and restriction fragment length polymorphism of genes for human liver arylamine N-acetyltransferases. Biochem Biophys Res Commun. 1991 Jun 28;177(3):1252-7. [Article]
  10. Grant DM, Lottspeich F, Meyer UA: Evidence for two closely related isozymes of arylamine N-acetyltransferase in human liver. FEBS Lett. 1989 Feb 13;244(1):203-7. [Article]
  11. Wu H, Dombrovsky L, Tempel W, Martin F, Loppnau P, Goodfellow GH, Grant DM, Plotnikov AN: Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases. J Biol Chem. 2007 Oct 12;282(41):30189-97. Epub 2007 Jul 26. [Article]
  12. Vatsis KP, Martell KJ, Weber WW: Diverse point mutations in the human gene for polymorphic N-acetyltransferase. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6333-7. [Article]
  13. Abe M, Deguchi T, Suzuki T: The structure and characteristics of a fourth allele of polymorphic N-acetyltransferase gene found in the Japanese population. Biochem Biophys Res Commun. 1993 Mar 31;191(3):811-6. [Article]
  14. Lin HJ, Han CY, Lin BK, Hardy S: Ethnic distribution of slow acetylator mutations in the polymorphic N-acetyltransferase (NAT2) gene. Pharmacogenetics. 1994 Jun;4(3):125-34. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00250Dapsoneapproved, investigationalunknownsubstrateDetails
DB01015SulfamethoxazoleapprovedunknownsubstrateDetails
DB00951Isoniazidapproved, investigationalunknownsubstrateDetails
DB04953Ezogabineapproved, investigationalunknownsubstrateDetails
DB00316AcetaminophenapprovedunknowninhibitorDetails
DB01068Clonazepamapproved, illicitunknownsubstrateDetails
DB11640Amifampridineapproved, investigationalnosubstrateDetails
DB09288PropacetamolexperimentalnoinhibitorDetails
DB00945Acetylsalicylic acidapproved, vet_approvedunknownsubstrateDetails
DB12612Ozanimodapproved, investigationalunknownsubstrateDetails