Arylamine N-acetyltransferase 2
Details
- Name
- Arylamine N-acetyltransferase 2
- Synonyms
- 2.3.1.5
- AAC2
- Arylamide acetylase 2
- N-acetyltransferase type 2
- N-hydroxyarylamine O-acetyltransferase
- NAT-2
- PNAT
- Polymorphic arylamine N-acetyltransferase
- Gene Name
- NAT2
- UniProtKB Entry
- P11245Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0055944|Arylamine N-acetyltransferase 2 MDIEAYFERIGYKNSRNKLDLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIV RRNRGGWCLQVNQLLYWALTTIGFQTTMLGGYFYIPPVNKYSTGMVHLLLQVTIDGRNYI VDAGSGSSSQMWQPLELISGKDQPQVPCIFCLTEERGIWYLDQIRREQYITNKEFLNSHL LPKKKHQKIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFILT YRKFNYKDNTDLVEFKTLTEEEVEEVLRNIFKISLGRNLVPKPGDGSLTI
- Number of residues
- 290
- Molecular Weight
- 33570.245
- Theoretical pI
- 5.67
- GO Classification
- FunctionsN-hydroxyarylamine O-acetyltransferase activity
- General Function
- Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates (PubMed:12222688, PubMed:7915226). Participates in the detoxification of a plethora of hydrazine and arylamine drugs, and is able to bioactivate several known carcinogens
- Specific Function
- arylamine N-acetyltransferase activity
- Pfam Domain Function
- Acetyltransf_2 (PF00797)
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P11245 UniProtKB Entry Name ARY2_HUMAN GenBank Protein ID 219412 GenBank Gene ID D90040 GeneCard ID NAT2 HGNC ID HGNC:7646 PDB ID(s) 2PFR KEGG ID hsa:10 NCBI Gene ID 10 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Bio-Entities
Bio-Entity Type Arylamine N-acetyltransferase 2 (Humans) protein primary- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Dapsone approved, investigational unknown enzyme substrate Details Sulfamethoxazole approved unknown enzyme substrate Details Isoniazid approved, investigational unknown enzyme substrate Details Ezogabine approved, investigational unknown enzyme substrate Details Acetaminophen approved unknown enzyme inhibitor Details Clonazepam approved, illicit unknown enzyme substrate Details Amifampridine approved, investigational no enzyme substrate Details Propacetamol experimental no enzyme inhibitor Details Acetylsalicylic acid approved, vet_approved unknown enzyme substrate Details Ozanimod approved, investigational unknown enzyme substrate Details