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P22760

- AAAD_HUMAN

UniProt

P22760 - AAAD_HUMAN

Protein

Arylacetamide deacetylase

Gene

AADAC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 5 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly. Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity.5 Publications

    Catalytic activityi

    Triacylglycerol + H2O = diacylglycerol + a carboxylate.

    Kineticsi

    1. KM=0.8 mM for flutamide4 Publications
    2. KM=0.6 mM for flutamide4 Publications
    3. KM=0.472 mM for flutamide4 Publications
    4. KM=3.05 mM for phenacetin4 Publications
    5. KM=1.8 mM for phenacetin4 Publications
    6. KM=1.42 mM for phenacetin4 Publications
    7. KM=0.2 mM for rifampicin4 Publications
    8. KM=0.154 mM for rifampicin4 Publications

    Vmax=1.1 nmol/min/mg enzyme toward flutamide4 Publications

    Vmax=1.1 nmol/min/mg enzyme toward flutamide4 Publications

    Vmax=0.617 nmol/min/mg enzyme toward flutamide4 Publications

    Vmax=1.34 nmol/min/mg enzyme toward phenacetin4 Publications

    Vmax=6.4 nmol/min/mg enzyme toward phenacetin4 Publications

    Vmax=1.42 nmol/min/mg enzyme toward phenacetin4 Publications

    Vmax=0.149 nmol/min/mg enzyme toward rifampicin4 Publications

    Vmax=0.060 nmol/min/mg enzyme toward rifampicin4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei111 – 1111PROSITE-ProRule annotation
    Active sitei189 – 1891PROSITE-ProRule annotation

    GO - Molecular functioni

    1. catalytic activity Source: ProtInc
    2. deacetylase activity Source: UniProtKB
    3. lipase activity Source: UniProtKB
    4. serine hydrolase activity Source: UniProtKB
    5. triglyceride lipase activity Source: UniProtKB

    GO - Biological processi

    1. positive regulation of triglyceride catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    SABIO-RKP22760.

    Protein family/group databases

    MEROPSiS09.991.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arylacetamide deacetylase (EC:3.1.1.3)
    Gene namesi
    Name:AADAC
    Synonyms:DAC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:17. AADAC.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781N → Q: Abolishes glycosylation at this site and causes moderate decrease in activity. 1 Publication
    Mutagenesisi282 – 2821N → Q: Abolishes glycosylation at this site and causes substantial decrease in activity and reduced substrate affinity. 1 Publication

    Organism-specific databases

    PharmGKBiPA24363.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 399399Arylacetamide deacetylasePRO_0000071542Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi78 – 781N-linked (GlcNAc...)2 Publications
    Disulfide bondi116 ↔ 340By similarity
    Glycosylationi282 – 2821N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    Glycosylation is required for enzyme activity.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP22760.
    PRIDEiP22760.

    PTM databases

    PhosphoSiteiP22760.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level). Mainly expressed in liver, small intestine, colon, adrenal gland and bladder.3 Publications

    Inductioni

    Down-regulated following infection with hepatis C virus which results in impaired triacylglycerol lipolysis and impaired assembly of very low density lipoproteins. This may represent a cellular adaptation to infection that is aimed at limiting viral production.1 Publication

    Gene expression databases

    ArrayExpressiP22760.
    BgeeiP22760.
    CleanExiHS_AADAC.
    GenevestigatoriP22760.

    Organism-specific databases

    HPAiHPA002911.

    Interactioni

    Protein-protein interaction databases

    BioGridi106531. 1 interaction.
    STRINGi9606.ENSP00000232892.

    Structurei

    3D structure databases

    ProteinModelPortaliP22760.
    SMRiP22760. Positions 69-379.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 55CytoplasmicSequence Analysis
    Topological domaini24 – 399376LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei6 – 2318Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi111 – 1133Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

    Sequence similaritiesi

    Belongs to the 'GDXG' lipolytic enzyme family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0657.
    HOGENOMiHOG000033738.
    HOVERGENiHBG058974.
    InParanoidiP22760.
    KOiK13616.
    OMAiYVYEPIP.
    OrthoDBiEOG7HB599.
    PhylomeDBiP22760.
    TreeFamiTF314978.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR017157. Arylacetamide_deacetylase.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view]
    PfamiPF07859. Abhydrolase_3. 2 hits.
    [Graphical view]
    PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22760-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRKSLYLLI VGILIAYYIY TPLPDNVEEP WRMMWINAHL KTIQNLATFV    50
    ELLGLHHFMD SFKVVGSFDE VPPTSDENVT VTETKFNNIL VRVYVPKRKS 100
    EALRRGLFYI HGGGWCVGSA ALSGYDLLSR WTADRLDAVV VSTNYRLAPK 150
    YHFPIQFEDV YNALRWFLRK KVLAKYGVNP ERIGISGDSA GGNLAAAVTQ 200
    QLLDDPDVKI KLKIQSLIYP ALQPLDVDLP SYQENSNFLF LSKSLMVRFW 250
    SEYFTTDRSL EKAMLSRQHV PVESSHLFKF VNWSSLLPER FIKGHVYNNP 300
    NYGSSELAKK YPGFLDVRAA PLLADDNKLR GLPLTYVITC QYDLLRDDGL 350
    MYVTRLRNTG VQVTHNHVED GFHGAFSFLG LKISHRLINQ YIEWLKENL 399
    Length:399
    Mass (Da):45,734
    Last modified:January 11, 2011 - v5
    Checksum:i34F9CB717DD7417A
    GO

    Sequence cautioni

    The sequence AAA35551.1 differs from that shown. Reason: Frameshift at positions 53 and 56.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31R → M AA sequence (PubMed:2043131)Curated
    Sequence conflicti55 – 573LHH → VHI in AAA35551. (PubMed:8063807)Curated

    Polymorphismi

    Three alleles are known: AADAC*1, AADAC*2 and AADAC*3. The sequence shown is that of AADAC*1 which is found in European American, African American, Japanese and Korean populations at allelic frequencies of 39.3 to 47.4%. The AADAC*2 allele is found in European American, African American, Korean, and Japanese populations at allelic frequencies of 52.6 to 63.5% whereas the AADAC*3 allele is found in European American (1.3%) and African American (2.0%) samples but not in Japanese or Korean samples.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti281 – 2811V → I in alleles AADAC*2 and AADAC*3; mildly decreased enzyme activity. 5 Publications
    Corresponds to variant rs1803155 [ dbSNP | Ensembl ].
    VAR_014798
    Natural varianti399 – 3991L → LQ in allele AADAC*3; decreased enzyme activity.
    VAR_070543

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L32179 mRNA. Translation: AAA35551.1. Frameshift.
    AK290628 mRNA. Translation: BAF83317.1.
    AC068647 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78791.1.
    CH471052 Genomic DNA. Translation: EAW78792.1.
    BC032309 mRNA. Translation: AAH32309.1.
    CCDSiCCDS33877.1.
    PIRiA53856.
    RefSeqiNP_001077.2. NM_001086.2.
    XP_005247160.1. XM_005247103.2.
    UniGeneiHs.506908.

    Genome annotation databases

    EnsembliENST00000232892; ENSP00000232892; ENSG00000114771.
    GeneIDi13.
    KEGGihsa:13.
    UCSCiuc003eze.3. human.

    Polymorphism databases

    DMDMi317373587.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L32179 mRNA. Translation: AAA35551.1 . Frameshift.
    AK290628 mRNA. Translation: BAF83317.1 .
    AC068647 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78791.1 .
    CH471052 Genomic DNA. Translation: EAW78792.1 .
    BC032309 mRNA. Translation: AAH32309.1 .
    CCDSi CCDS33877.1.
    PIRi A53856.
    RefSeqi NP_001077.2. NM_001086.2.
    XP_005247160.1. XM_005247103.2.
    UniGenei Hs.506908.

    3D structure databases

    ProteinModelPortali P22760.
    SMRi P22760. Positions 69-379.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106531. 1 interaction.
    STRINGi 9606.ENSP00000232892.

    Protein family/group databases

    MEROPSi S09.991.

    PTM databases

    PhosphoSitei P22760.

    Polymorphism databases

    DMDMi 317373587.

    Proteomic databases

    PaxDbi P22760.
    PRIDEi P22760.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000232892 ; ENSP00000232892 ; ENSG00000114771 .
    GeneIDi 13.
    KEGGi hsa:13.
    UCSCi uc003eze.3. human.

    Organism-specific databases

    CTDi 13.
    GeneCardsi GC03P151531.
    HGNCi HGNC:17. AADAC.
    HPAi HPA002911.
    MIMi 600338. gene.
    neXtProti NX_P22760.
    PharmGKBi PA24363.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0657.
    HOGENOMi HOG000033738.
    HOVERGENi HBG058974.
    InParanoidi P22760.
    KOi K13616.
    OMAi YVYEPIP.
    OrthoDBi EOG7HB599.
    PhylomeDBi P22760.
    TreeFami TF314978.

    Enzyme and pathway databases

    SABIO-RK P22760.

    Miscellaneous databases

    GeneWikii AADAC.
    GenomeRNAii 13.
    NextBioi 27.
    PROi P22760.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22760.
    Bgeei P22760.
    CleanExi HS_AADAC.
    Genevestigatori P22760.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR017157. Arylacetamide_deacetylase.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view ]
    Pfami PF07859. Abhydrolase_3. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF037251. Arylacetamide_deacetylase. 1 hit.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human liver arylacetamide deacetylase. Molecular cloning of a novel esterase involved in the metabolic activation of arylamine carcinogens with high sequence similarity to hormone-sensitive lipase."
      Probst M.R., Beer M., Beer D., Jenoe P., Meyer U.A., Gasser R.
      J. Biol. Chem. 269:21650-21656(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT ILE-281.
      Tissue: Liver.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-281.
      Tissue: Heart.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-281.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.
    6. "Purification and characterization of a human liver arylacetamide deacetylase."
      Probst M.R., Jenoe P., Meyer U.A.
      Biochem. Biophys. Res. Commun. 177:453-459(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
      Tissue: Liver.
    7. "Human carboxylesterases and their role in xenobiotic and endobiotic metabolism."
      Ross M.K., Crow J.A.
      J. Biochem. Mol. Toxicol. 21:187-196(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Human arylacetamide deacetylase is a principal enzyme in flutamide hydrolysis."
      Watanabe A., Fukami T., Nakajima M., Takamiya M., Aoki Y., Yokoi T.
      Drug Metab. Dispos. 37:1513-1520(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78 AND ASN-282.
      Tissue: Liver.
    10. "Species differences in tissue distribution and enzyme activities of arylacetamide deacetylase in human, rat, and mouse."
      Kobayashi Y., Fukami T., Nakajima A., Watanabe A., Nakajima M., Yokoi T.
      Drug Metab. Dispos. 40:671-679(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, TISSUE SPECIFICITY.
    11. "A novel polymorphic allele of human arylacetamide deacetylase leads to decreased enzyme activity."
      Shimizu M., Fukami T., Kobayashi Y., Takamiya M., Aoki Y., Nakajima M., Yokoi T.
      Drug Metab. Dispos. 40:1183-1190(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, VARIANTS ILE-281 AND GLN-399 EXT, CHARACTERIZATION OF VARIANTS ILE-281 AND GLN-399 EXT.
    12. "N-Glycosylation during translation is essential for human arylacetamide deacetylase enzyme activity."
      Muta K., Fukami T., Nakajima M., Yokoi T.
      Biochem. Pharmacol. 87:352-359(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-78 AND ASN-282, MUTAGENESIS OF ASN-78 AND ASN-282.
    13. "Arylacetamide deacetylase: a novel host factor with important roles in the lipolysis of cellular triacylglycerol stores, VLDL assembly and HCV production."
      Nourbakhsh M., Douglas D.N., Pu C.H., Lewis J.T., Kawahara T., Lisboa L.F., Wei E., Asthana S., Quiroga A.D., Law L.M., Chen C., Addison W.R., Nelson R., Houghton M., Lehner R., Kneteman N.M.
      J. Hepatol. 59:336-343(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    14. "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population."
      Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., Nakamura Y.
      J. Hum. Genet. 48:249-270(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ILE-281.

    Entry informationi

    Entry nameiAAAD_HUMAN
    AccessioniPrimary (citable) accession number: P22760
    Secondary accession number(s): A8K3L3, D3DNJ6, Q8N1A9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 134 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Can hydrolyze a number of clinical drugs such as flutamide, an antiandrogen drug used for the treatment of prostate cancer; phenacetin, an analgesic antipyretic which has been withdrawn from the market due to its links with renal failure; and rifamycins which have been used as antituberculosis drugs.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3