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P22760

- AAAD_HUMAN

UniProt

P22760 - AAAD_HUMAN

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Protein

Arylacetamide deacetylase

Gene

AADAC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55CytoplasmicSequence Analysis
Transmembranei6 – 2318Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini24 – 399376LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiP22760.
CleanExiHS_AADAC.
ExpressionAtlasiP22760. baseline and differential.
GenevestigatoriP22760.

Organism-specific databases

HPAiHPA002911.

Interactioni

Protein-protein interaction databases

BioGridi106531. 1 interaction.
STRINGi9606.ENSP00000232892.

Structurei

3D structure databases

ProteinModelPortaliP22760.
SMRiP22760. Positions 70-381.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00550000074556.
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

        10         20         30         40         50
MGRKSLYLLI VGILIAYYIY TPLPDNVEEP WRMMWINAHL KTIQNLATFV
60 70 80 90 100
ELLGLHHFMD SFKVVGSFDE VPPTSDENVT VTETKFNNIL VRVYVPKRKS
110 120 130 140 150
EALRRGLFYI HGGGWCVGSA ALSGYDLLSR WTADRLDAVV VSTNYRLAPK
160 170 180 190 200
YHFPIQFEDV YNALRWFLRK KVLAKYGVNP ERIGISGDSA GGNLAAAVTQ
210 220 230 240 250
QLLDDPDVKI KLKIQSLIYP ALQPLDVDLP SYQENSNFLF LSKSLMVRFW
260 270 280 290 300
SEYFTTDRSL EKAMLSRQHV PVESSHLFKF VNWSSLLPER FIKGHVYNNP
310 320 330 340 350
NYGSSELAKK YPGFLDVRAA PLLADDNKLR GLPLTYVITC QYDLLRDDGL
360 370 380 390
MYVTRLRNTG VQVTHNHVED GFHGAFSFLG LKISHRLINQ YIEWLKENL
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 70-381.
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.
GeneTreei ENSGT00550000074556.
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

Bgeei P22760.
CleanExi HS_AADAC.
ExpressionAtlasi P22760. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 136 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