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NAT1 (N-acetyltransferase 1 (arylamine N-acetyltransferase))

Written2009-02Jhon D Ruiz, José AG Agúndez, Carmen Martínez, Elena García-Martín
Department of Pharmacology, Medical School, University of Extremadura, Badajoz, Spain (JDR, JAGA, CM); Department of Biochemistry & Molecular biology & Genetics, School of Biological Sciences, Badajoz, Spain (EGM)

(Note : for Links provided by Atlas : click)


Alias (NCBI)AAC1
HGNC (Hugo) NAT1
HGNC Alias namearylamine N-acetyltransferase 1
HGNC Previous nameAAC1
HGNC Previous nameN-acetyltransferase 1 (arylamine N-acetyltransferase)
LocusID (NCBI) 9
Atlas_Id 41497
Location 8p22  [Link to chromosome band 8p22]
Location_base_pair Starts at 18170467 and ends at 18223689 bp from pter ( according to hg19-Feb_2009)  [Mapping NAT1.png]
  Picture adapted from an original prepared by Genetics Home Reference; February 2009.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
NAT1 (8p22) / NAT1 (8p22)


Note In humans NAT1 is located in the NAT cluster that comprises 230 kb and includes two functional genes, NAT1 and NAT2. In other species the number of NAT genes range from 0 to 4.
  Structure of the human NAT1 gene and common NAT1 transcripts.
Transcription The human NAT1 gene has nine exons. The coding region is located in exon 9 and spans 870 bp. Diverse NAT1 transcripts have been reported and two promoters exist. The first promoter, designated as P1 is located in the 5' flanking region of exon 1 and controls two major (a1 and a2) transcripts. The second promoter is located upstream of exon 4 and give rise to at least five (b1 to b5) different transcripts. The different transcripts appear to have different translational efficiencies, although the biological significance of this is unknown (revised in Butcher et al., 2007).
Pseudogene In humans the NAT locus has a pseudogene designated as NATP.


Note NAT enzymes have been identified in several vertebrate and microorganism species, whereas NAT deficiency in the domestic and wild dog is due to complete absence of NAT genes.
Description The amino-terminal domain (residues 1-83) consists of five helices and one short beta-strand. The second domain comprises residues 85-192 and consists of nine beta-strands and two short helices. The third domain has a final helix which precedes the carboxy terminal region.
Expression NAT1 activity is expressed in liver and in many extrahepatic tissues. The transcripts originated from the first promoter, NATa, are expressed in kidney, liver, lung and trachea. However the most common transcripts are those designated as type b in the Figure above and have been detected in all tissues examinated.
Localisation Arylamine N-acetyltransferases are cytosolic enzymes.
Function NAT1 is a phase II enzyme that participates in the metabolism of numerous primary arylamines and hydrazine drugs and carcinogens. In addition to their N-acetylation catalytic activity, NAT enzymes have also O-acetylation activity towards N-hydroxyarylamines.
Homology NAT1 and NAT2 share 87% nucleotide homology in the coding region, whereas NAT1 and NAT2 proteins share 81% amino-acid sequence identity.


Note In humans NAT1 is highly polymorphic. Several polymorphisms, most of which are single nucleotide polymorphisms, and at least 26 different haplotypes have been described. The Figure below shows the positions of NAT1 polymorphisms, taking as a reference the start site in the open reading frame (ORF) in exon 9. Nonsynonymous polymorphisms are labeled in red font. The association of different haplotypes with phenotypes is summarized in the following link:

Implicated in

Entity Lung cancer
Note Two independent studies have observed a significant association of the NAT1 polymorphism with lung cancer risk (Bouchardy et al., 1998; Wikman et al., 2001). However these studies should be interpreted cautiously because these do not agree on the NAT1 risk genotype. Another study identified an increased risk among carriers of NAT1 plus NAT2 slow genotypes (Gemignani et al., 2007). In a meta-analysis carried out with smokers that suffered from non small-cell lung cancer a relevant association of the NAT1 rapid acetylation genotype was identified (Zienolddiny et al., 2008). Although negative associations have been reported (Perera et al., 2006 ), NAT1 is emerging as the NAT gene most likely related to lung cancer (McKay et al, 2008).
Entity Head and neck cancer
Note Since chemical compounds present in tobacco are inactivated by phase II enzymes, it has been proposed that head and neck cancer risk could be modified by NAT genotypes. Head and neck cancers are strongly associated with smoking, and a few studies have explored the role of NAT1 polymorphisms in the risk of developing head and neck cancer in smokers. However overall findings are inconsistent and associations if present are weak, and indicate either a decreased risk in carriers of the variant NAT1*10 (McKay et al., 2008), an increased risk (Katoh et al., 1998) or a lack of association (Fronhoffs et al., 2001; Henning et al., 1999; Agúndez, 2008).
Entity Breast cancer
Note The NAT1*10 variant allele was associated to increased breast cancer risk among women who consumed well-done meat, although the statistical significance of this finding is low (Krajinovic et al., 2001). Several studies, however, indicate that no major association of NAT polymorphisms and breast cancer risk exists (Agúndez, 2008).
Entity Colorectal cancer
Note A biologically plausible mechanistic hypothesis suggest that rapid NAT1 and/or NAT2 acetylators should more activate heterocyclic amine carcinogens within the colon to their ultimate carcinogenic forms, thereby predisposing them to colorectal cancer. However sufficient evidence is available to rule out a relevant association of NAT genotypes alone with colorectal cancer risk. This evidence is based in nearly thirty studies failed to detect a statistically significant association for NAT1 genotypes both with colorectal cancer or adenomas. In addition meta-analyses (Chen et al., 2005; Ye et al., 2002; Houlston et al., 2001) consistently confirm a lack of a relevant association of NAT1 rapid acetylator genotypes and colorectal cancer risk (revised in Agúndez, 2008).
Entity Bladder cancer
Note No significant association of the NAT1 genotype with bladder cancer risk has been observed in a recent meta-analysis, although the authors found a joint effect of NAT1 rapid genotypes, slow NAT2 genotypes and smoking as factors increasing cancer risk (Sanderson et al., 2007). Overall findings are negative (Okkels et al., 1997), although a significant risk has been described in smokers (Taylor et al., 1998; Hsieh et al., 1999; Cascorbi et al., 2001) and a nearly significant association was observed in individuals exposed to benzidine (Carreon et al., 2006).


Polymorphisms of human N-acetyltransferases and cancer risk.
Agundez JA.
Curr Drug Metab. 2008 Jul;9(6):520-31.
PMID 18680472
Functional properties of an alternative, tissue-specific promoter for human arylamine N-acetyltransferase 1.
Barker DF, Husain A, Neale JR, Martini BD, Zhang X, Doll MA, States JC, Hein DW.
Pharmacogenet Genomics. 2006 Jul;16(7):515-25.
PMID 16788383
Human arylamine N-acetyltransferase genes: isolation, chromosomal localization, and functional expression.
Blum M, Grant DM, McBride W, Heim M, Meyer UA.
DNA Cell Biol. 1990 Apr;9(3):193-203.
PMID 2340091
N-acetyltransferase NAT1 and NAT2 genotypes and lung cancer risk.
Bouchardy C, Mitrunen K, Wikman H, Husgafvel-Pursiainen K, Dayer P, Benhamou S, Hirvonen A.
Pharmacogenetics. 1998 Aug;8(4):291-8.
PMID 9731715
Induction of human arylamine N-acetyltransferase type I by androgens in human prostate cancer cells.
Butcher NJ, Tetlow NL, Cheung C, Broadhurst GM, Minchin RF.
Cancer Res. 2007 Jan 1;67(1):85-92.
PMID 17210686
NAT2 slow acetylation and bladder cancer in workers exposed to benzidine.
Carreon T, Ruder AM, Schulte PA, Hayes RB, Rothman N, Waters M, Grant DJ, Boissy R, Bell DA, Kadlubar FF, Hemstreet GP 3rd, Yin S, LeMasters GK.
Int J Cancer. 2006 Jan 1;118(1):161-8.
PMID 16003747
Association of NAT1 and NAT2 polymorphisms to urinary bladder cancer: significantly reduced risk in subjects with NAT1*10.
Cascorbi I, Roots I, Brockmoller J.
Cancer Res. 2001 Jul 1;61(13):5051-6.
PMID 11431340
Relationship between metabolic enzyme polymorphism and colorectal cancer.
Chen K, Jiang QT, He HQ.
World J Gastroenterol. 2005 Jan 21;11(3):331-5.
PMID 15637738
Classification of breast cancer using genetic algorithms and tissue microarrays.
Dolled-Filhart M, Ryden L, Cregger M, Jirstrom K, Harigopal M, Camp RL, Rimm DL.
Clin Cancer Res. 2006 Nov 1;12(21):6459-68.
PMID 17085660
Real-time PCR analysis of the N-acetyltransferase NAT1 allele *3, *4, *10, *11, *14 and *17 polymorphism in squamous cell cancer of head and neck.
Fronhoffs S, Bruning T, Ortiz-Pallardo E, Brode P, Koch B, Harth V, Sachinidis A, Bolt HM, Herberhold C, Vetter H, Ko Y.
Carcinogenesis. 2001 Sep;22(9):1405-12.
PMID 11532862
Development of lung cancer before the age of 50: the role of xenobiotic metabolizing genes.
Gemignani F, Landi S, Szeszenia-Dabrowska N, Zaridze D, Lissowska J, Rudnai P, Fabianova E, Mates D, Foretova L, Janout V, Bencko V, Gaborieau V, Gioia-Patricola L, Bellini I, Barale R, Canzian F, Hall J, Boffetta P, Hung RJ, Brennan P.
Carcinogenesis. 2007 Jun;28(6):1287-93. Epub 2007 Jan 27.
PMID 17259654
Monomorphic and polymorphic human arylamine N-acetyltransferases: a comparison of liver isozymes and expressed products of two cloned genes.
Grant DM, Blum M, Beer M, Meyer UA.
Mol Pharmacol. 1991 Feb;39(2):184-91.
PMID 1996083
Effects of N-acetyl transferase 1 and 2 polymorphisms on bladder cancer risk in Caucasians.
Gu J, Liang D, Wang Y, Lu C, Wu X.
Mutat Res. 2005 Mar 7;581(1-2):97-104. Epub 2004 Dec 16.
PMID 15725609
Molecular genetics and epidemiology of the NAT1 and NAT2 acetylation polymorphisms.
Hein DW, Doll MA, Fretland AJ, Leff MA, Webb SJ, Xiao GH, Devanaboyina US, Nangju NA, Feng Y.
Cancer Epidemiol Biomarkers Prev. 2000 Jan;9(1):29-42.
PMID 10667461
Molecular genetics and function of NAT1 and NAT2: role in aromatic amine metabolism and carcinogenesis.
Hein DW.
Mutat Res. 2002 Sep 30;506-507:65-77.
PMID 12351146
Association of arylamine N-acetyltransferases NAT1 and NAT2 genotypes to laryngeal cancer risk.
Henning S, Cascorbi I, Munchow B, Jahnke V, Roots I.
Pharmacogenetics. 1999 Feb;9(1):103-11.
PMID 10208649
Polymorphisms and colorectal tumor risk.
Houlston RS, Tomlinson IP.
Gastroenterology. 2001 Aug;121(2):282-301.
PMID 11487538.
Genetic polymorphisms of N-acetyltransferase 1 and 2 and risk of cigarette smoking-related bladder cancer.
Hsieh FI, Pu YS, Chern HD, Hsu LI, Chiou HY, Chen CJ.
Br J Cancer. 1999 Oct;81(3):537-41.
PMID 10507782
Identification and characterization of variant alleles of human acetyltransferase NAT1 with defective function using p-aminosalicylate as an in-vivo and in-vitro probe.
Hughes NC, Janezic SA, McQueen KL, Jewett MA, Castranio T, Bell DA, Grant DM.
Pharmacogenetics. 1998 Feb;8(1):55-66.
PMID 9511182
Identification of the major promoter and non-coding exons of the human arylamine N-acetyltransferase 1 gene (NAT1).
Husain A, Barker DF, States JC, Doll MA, Hein DW.
Pharmacogenetics. 2004 Jul;14(7):397-406.
PMID 15226672
Functional analysis of the human N-acetyltransferase 1 major promoter: quantitation of tissue expression and identification of critical sequence elements.
Husain A, Zhang X, Doll MA, States JC, Barker DF, Hein DW.
Drug Metab Dispos. 2007 Sep;35(9):1649-56. Epub 2007 Jun 25.
PMID 17591675
1998 International Meeting on the Arylamine N-Acetyltransferases: synopsis of the workshop on nomenclature, biochemistry, molecular biology, interspecies comparisons, and role in human disease risk.
Ilett KF, Kadlubar FF, Minchin RF.
Drug Metab Dispos. 1999 Sep;27(9):957-9.
PMID 10460790
Loss of function polymorphisms in NAT1 protect against spina bifida.
Jensen LE, Hoess K, Mitchell LE, Whitehead AS.
Hum Genet. 2006 Aug;120(1):52-7. Epub 2006 May 6.
PMID 16680433
Role of arylamine N-acetyltransferase 1 and 2 (NAT1 and NAT2) genotypes in susceptibility to oral/pharyngeal and laryngeal cancers.
Jourenkova-Mironova N, Wikman H, Bouchardy C, Mitrunen K, Dayer P, Benhamou S, Hirvonen A.
Pharmacogenetics. 1999 Aug;9(4):533-7.
PMID 10780274
Quantitation of three-month intraindividual variability and influence of sex and menstrual cycle phase on CYP1A2, N-acetyltransferase-2, and xanthine oxidase activity determined with caffeine phenotyping.
Kashuba AD, Bertino JS Jr, Kearns GL, Leeder JS, James AW, Gotschall R, Nafziger AN.
Clin Pharmacol Ther. 1998 May;63(5):540-51.
PMID 9630827
A pilot study testing the association between N-acetyltransferases 1 and 2 and risk of oral squamous cell carcinoma in Japanese people.
Katoh T, Kaneko S, Boissy R, Watson M, Ikemura K, Bell DA.
Carcinogenesis. 1998 Oct;19(10):1803-7.
PMID 9806162
Genetic susceptibility to breast cancer in French-Canadians: role of carcinogen-metabolizing enzymes and gene-environment interactions.
Krajinovic M, Ghadirian P, Richer C, Sinnett H, Gandini S, Perret C, Lacroix A, Labuda D, Sinnett D.
Int J Cancer. 2001 Apr 15;92(2):220-5.
PMID 11291049
Variants of N-acetyltransferase NAT1 and a case-control study of colorectal adenomas.
Lin HJ, Probst-Hensch NM, Hughes NC, Sakamoto GT, Louie AD, Kau IH, Lin BK, Lee DB, Lin J, Frankl HD, Lee ER, Hardy S, Grant DM, Haile RW.
Pharmacogenetics. 1998 Jun;8(3):269-81.
PMID 9682272
Arylamine N-acetyltransferase aggregation and constitutive ubiquitylation.
Liu F, Zhang N, Zhou X, Hanna PE, Wagner CR, Koepp DM, Walters KJ.
J Mol Biol. 2006 Aug 18;361(3):482-92. Epub 2006 Jun 30.
PMID 16857211
Sequence variants of NAT1 and NAT2 and other xenometabolic genes and risk of lung and aerodigestive tract cancers in Central Europe.
McKay JD, Hashibe M, Hung RJ, Wakefield J, Gaborieau V, Szeszenia-Dabrowska N, Zaridze D, Lissowska J, Rudnai P, Fabianova E, Mates D, Foretova L, Janout V, Bencko V, Chabrier A, Hall J, Boffetta P, Canzian F, Brennan P.
Cancer Epidemiol Biomarkers Prev. 2008 Jan;17(1):141-7.
PMID 18199719
Arylamine N-acetyltransferase I.
Minchin RF, Hanna PE, Dupret JM, Wagner CR, Rodrigues-Lima F, Butcher NJ.
Int J Biochem Cell Biol. 2007;39(11):1999-2005. Epub 2007 Jan 20.
PMID 17392017
Acetylation of p-aminobenzoylglutamate, a folic acid catabolite, by recombinant human arylamine N-acetyltransferase and U937 cells.
Minchin RF.
Biochem J. 1995 Apr 1;307 ( Pt 1):1-3.
PMID 7717963
Arylamine N-acetyltransferase 1 (NAT1) and 2 (NAT2) polymorphisms in susceptibility to bladder cancer: the influence of smoking.
Okkels H, Sigsgaard T, Wolf H, Autrup H.
Cancer Epidemiol Biomarkers Prev. 1997 Apr;6(4):225-31.
PMID 9107426
Lack of associations among cancer and albumin adducts, ras p21 oncoprotein levels, and CYP1A1, CYP2D6, NAT1, and NAT2 in a nested case-control study of lung cancer within the physicians' health study.
Perera FP, Tang D, Brandt-Rauf P, Santella RM, Mooney LV, Tu YH, Bendkowska I, Bell DA.
Cancer Epidemiol Biomarkers Prev. 2006 Jul;15(7):1417-9.
PMID 16835348
Novel prognostic immunohistochemical biomarker panel for estrogen receptor-positive breast cancer.
Ring BZ, Seitz RS, Beck R, Shasteen WJ, Tarr SM, Cheang MC, Yoder BJ, Budd GT, Nielsen TO, Hicks DG, Estopinal NC, Ross DT.
J Clin Oncol. 2006 Jul 1;24(19):3039-47.
PMID 16809728
Homology modelling and structural analysis of human arylamine N-acetyltransferase NAT1: evidence for the conservation of a cysteine protease catalytic domain and an active-site loop.
Rodrigues-Lima F, Delomenie C, Goodfellow GH, Grant DM, Dupret JM.
Biochem J. 2001 Jun 1;356(Pt 2):327-34.
PMID 11368758
Joint effects of the N-acetyltransferase 1 and 2 (NAT1 and NAT2) genes and smoking on bladder carcinogenesis: a literature-based systematic HuGE review and evidence synthesis.
Sanderson S, Salanti G, Higgins J.
Am J Epidemiol. 2007 Oct 1;166(7):741-51. Epub 2007 Aug 4.
PMID 17675654
The role of N-acetylation polymorphisms in smoking-associated bladder cancer: evidence of a gene-gene-exposure three-way interaction.
Taylor JA, Umbach DM, Stephens E, Castranio T, Paulson D, Robertson C, Mohler JL, Bell DA.
Cancer Res. 1998 Aug 15;58(16):3603-10.
PMID 9721868
Cytosolic arylamine N-acetyltransferase (NAT) deficiency in the dog and other canids due to an absence of NAT genes.
Trepanier LA, Ray K, Winand NJ, Spielberg SP, Cribb AE.
Biochem Pharmacol. 1997 Jul 1;54(1):73-80.
PMID 9296352
Arylamine N-acetyltransferases - of mice, men and microorganisms.
Upton A, Johnson N, Sandy J, Sim E.
Trends Pharmacol Sci. 2001 Mar;22(3):140-6.
PMID 11239577
Purification of recombinant human N-acetyltransferase type 1 (NAT1) expressed in E. coli and characterization of its potential role in folate metabolism.
Ward A, Summers MJ, Sim E.
Biochem Pharmacol. 1995 Jun 16;49(12):1759-67.
PMID 7598738
Relevance of N-acetyltransferase 1 and 2 (NAT1, NAT2) genetic polymorphisms in non-small cell lung cancer susceptibility.
Wikman H, Thiel S, Jager B, Schmezer P, Spiegelhalder B, Edler L, Dienemann H, Kayser K, Schulz V, Drings P, Bartsch H, Risch A.
Pharmacogenetics. 2001 Mar;11(2):157-68.
PMID 11266080
Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases.
Wu H, Dombrovsky L, Tempel W, Martin F, Loppnau P, Goodfellow GH, Grant DM, Plotnikov AN.
J Biol Chem. 2007 Oct 12;282(41):30189-97. Epub 2007 Jul 26.
PMID 17656365
Meta-analysis of 20 case-control studies on the N-acetyltransferase 2 acetylation status and colorectal cancer risk.
Ye Z, Parry JM.
Med Sci Monit. 2002 Aug;8(8):CR558-65.
PMID 12165742
A comprehensive analysis of phase I and phase II metabolism gene polymorphisms and risk of non-small cell lung cancer in smokers.
Zienolddiny S, Campa D, Lind H, Ryberg D, Skaug V, Stangeland LB, Canzian F, Haugen A.
Carcinogenesis. 2008 Jun;29(6):1164-9. Epub 2008 Feb 6.
PMID 18258609


This paper should be referenced as such :
Ruiz, JD ; Agúndez, JAG ; Martinez, C ; Garcia-Martin, E
NAT1 (N-acetyltransferase 1 (arylamine N-acetyltransferase))
Atlas Genet Cytogenet Oncol Haematol. 2010;14(1):39-43.
Free journal version : [ pdf ]   [ DOI ]
On line version :

External links

HGNC (Hugo)NAT1   7645
Entrez_Gene (NCBI)NAT1  9  N-acetyltransferase 1
AliasesAAC1; MNAT; NAT-1; NATI
GeneCards (Weizmann)NAT1
Ensembl hg19 (Hinxton)ENSG00000171428 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000171428 [Gene_View]  ENSG00000171428 [Sequence]  chr8:18170467-18223689 [Contig_View]  NAT1 [Vega]
ICGC DataPortalENSG00000171428
TCGA cBioPortalNAT1
AceView (NCBI)NAT1
Genatlas (Paris)NAT1
SOURCE (Princeton)NAT1
Genetics Home Reference (NIH)NAT1
Genomic and cartography
GoldenPath hg38 (UCSC)NAT1  -     chr8:18170467-18223689 +  8p22   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)NAT1  -     8p22   [Description]    (hg19-Feb_2009)
GoldenPathNAT1 - 8p22 [CytoView hg19]  NAT1 - 8p22 [CytoView hg38]
genome Data Viewer NCBINAT1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AJ581135 AJ581136 AJ581137 AJ581138 AJ581139
RefSeq transcript (Entrez)NM_000662 NM_001160170 NM_001160171 NM_001160172 NM_001160173 NM_001160174 NM_001160175 NM_001160176 NM_001160179 NM_001291962
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)NAT1
Alternative Splicing GalleryENSG00000171428
Gene ExpressionNAT1 [ NCBI-GEO ]   NAT1 [ EBI - ARRAY_EXPRESS ]   NAT1 [ SEEK ]   NAT1 [ MEM ]
Gene Expression Viewer (FireBrowse)NAT1 [ Firebrowse - Broad ]
GenevisibleExpression of NAT1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)9
GTEX Portal (Tissue expression)NAT1
Human Protein AtlasENSG00000171428-NAT1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP18440   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP18440  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP18440
Splice isoforms : SwissVarP18440
Catalytic activity : Enzyme2.3.1.5 [ Enzyme-Expasy ] [ IntEnz-EBI ] [ BRENDA ] [ KEGG ]   [ MEROPS ]
Domains : Interpro (EBI)Arylamine_N-AcTrfase    Papain-like_cys_pep_sf   
Domain families : Pfam (Sanger)Acetyltransf_2 (PF00797)   
Domain families : Pfam (NCBI)pfam00797   
Conserved Domain (NCBI)NAT1
DMDM Disease mutations9
Blocks (Seattle)NAT1
PDB (RSDB)2DSS    2GWU    2IJA    2PQT   
PDB Europe2DSS    2GWU    2IJA    2PQT   
PDB (PDBSum)2DSS    2GWU    2IJA    2PQT   
PDB (IMB)2DSS    2GWU    2IJA    2PQT   
Structural Biology KnowledgeBase2DSS    2GWU    2IJA    2PQT   
SCOP (Structural Classification of Proteins)2DSS    2GWU    2IJA    2PQT   
CATH (Classification of proteins structures)2DSS    2GWU    2IJA    2PQT   
Human Protein Atlas [tissue]ENSG00000171428-NAT1 [tissue]
Peptide AtlasP18440
IPIIPI00644361   IPI00930394   
Protein Interaction databases
IntAct (EBI)P18440
Ontologies - Pathways
Ontology : AmiGOarylamine N-acetyltransferase activity  arylamine N-acetyltransferase activity  cytosol  xenobiotic metabolic process  
Ontology : EGO-EBIarylamine N-acetyltransferase activity  arylamine N-acetyltransferase activity  cytosol  xenobiotic metabolic process  
Pathways : KEGGCaffeine metabolism    Drug metabolism - other enzymes    Chemical carcinogenesis   
REACTOMEP18440 [protein]
REACTOME PathwaysR-HSA-156582 [pathway]   
NDEx NetworkNAT1
Atlas of Cancer Signalling NetworkNAT1
Wikipedia pathwaysNAT1
Orthology - Evolution
GeneTree (enSembl)ENSG00000171428
Phylogenetic Trees/Animal Genes : TreeFamNAT1
Homologs : HomoloGeneNAT1
Homology/Alignments : Family Browser (UCSC)NAT1
Gene fusions - Rearrangements
Fusion : FusionGDB2.3.1.5   
Fusion : Fusion_HubDDHD2--NAT1    NAT1--NAT1    NAT1--NATP    NAT1--RP11-685B14.1    PSD3--NAT1    UGT3A1--NAT1   
Fusion : QuiverNAT1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerNAT1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)NAT1
Exome Variant ServerNAT1
GNOMAD BrowserENSG00000171428
Varsome BrowserNAT1
Genetic variants : HAPMAP9
Genomic Variants (DGV)NAT1 [DGVbeta]
DECIPHERNAT1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisNAT1 
ICGC Data PortalNAT1 
TCGA Data PortalNAT1 
Broad Tumor PortalNAT1
OASIS PortalNAT1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICNAT1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DNAT1
Mutations and Diseases : HGMDNAT1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch NAT1
DgiDB (Drug Gene Interaction Database)NAT1
DoCM (Curated mutations)NAT1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)NAT1 (select a term)
NCG6 (London) select NAT1
Cancer3DNAT1(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry NAT1
NextProtP18440 [Medical]
Target ValidationNAT1
Huge Navigator NAT1 [HugePedia]
snp3D : Map Gene to Disease9
BioCentury BCIQNAT1
Clinical trials, drugs, therapy
Protein Interactions : CTD9
Pharm GKB GenePA17
Pharm GKB PathwaysPA165374494   
Clinical trialNAT1
canSAR (ICR)NAT1 (select the gene name)
DataMed IndexNAT1
PubMed243 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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