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P31513

- FMO3_HUMAN

UniProt

P31513 - FMO3_HUMAN

Protein

Dimethylaniline monooxygenase [N-oxide-forming] 3

Gene

FMO3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 5 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Plays an important role in the metabolism of trimethylamine (TMA), via the production of TMA N-oxide (TMAO). Is also able to perform S-oxidation when acting on sulfide compounds.

    Catalytic activityi

    N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.1 Publication
    N,N,N-trimethylamine + NADPH + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O.1 Publication

    Cofactori

    FAD.

    Kineticsi

    1. KM=21 µM for trimethylamine (at pH 8.5)2 Publications
    2. KM=31 µM for trimethylamine (at pH 7.4 and 37 degrees Celsius)2 Publications
    3. KM=43 µM for benzydamine (at pH 7.4 and 37 degrees Celsius)2 Publications
    4. KM=55.7 µM for ethylenethiourea (at pH 8.5)2 Publications
    5. KM=71.8 µM for methimazole (at pH 8.5)2 Publications
    6. KM=150.1 µM for sulindac (at pH 8.5)2 Publications
    7. KM=248 µM for methyl p-tolyl sulfide (at pH 7.4 and 37 degrees Celsius)2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 146FADSequence Analysis
    Nucleotide bindingi191 – 1966NADPSequence Analysis

    GO - Molecular functioni

    1. amino acid binding Source: Ensembl
    2. flavin adenine dinucleotide binding Source: InterPro
    3. N,N-dimethylaniline monooxygenase activity Source: Reactome
    4. NADP binding Source: Ensembl
    5. trimethylamine monooxygenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. drug metabolic process Source: Ensembl
    2. small molecule metabolic process Source: Reactome
    3. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00223-MONOMER.
    ReactomeiREACT_13653. FMO oxidizes nucleophiles.
    SABIO-RKP31513.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 3 (EC:1.14.13.8)
    Alternative name(s):
    Dimethylaniline oxidase 3
    FMO II
    FMO form 2
    Hepatic flavin-containing monooxygenase 3
    Short name:
    FMO 3
    Trimethylamine monooxygenase (EC:1.14.13.148)
    Gene namesi
    Name:FMO3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3771. FMO3.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. intracellular membrane-bounded organelle Source: ProtInc

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Involvement in diseasei

    Trimethylaminuria (TMAU) [MIM:602079]: Inborn error of metabolism associated with an offensive body odor and caused by deficiency of FMO-mediated N-oxidation of amino-trimethylamine (TMA) derived from foodstuffs. Affected individuals excrete relatively large amounts of TMA in their urine, sweat, and breath, and exhibit a fishy body odor characteristic of the malodorous free amine.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321E → K in TMAU. 1 Publication
    VAR_037306
    Natural varianti52 – 521A → T in TMAU. 1 Publication
    VAR_008146
    Natural varianti61 – 611N → S in TMAU; more than 90% reduction in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide. 1 Publication
    VAR_037307
    Natural varianti66 – 661M → I in TMAU; loss of activity; affects FAD binding. 2 Publications
    VAR_002423
    Natural varianti153 – 1531P → L in TMAU; 90% reduction in catalytic efficiency toward trimethylamine and benzydamine; 34% reduction in catalytic efficiency toward methyl p-tolyl sulfide; nearly no effect on affinity for these substrates. 2 Publications
    VAR_002424
    Natural varianti387 – 3871R → L in TMAU. 1 Publication
    Corresponds to variant rs72549331 [ dbSNP | Ensembl ].
    VAR_008147
    Natural varianti434 – 4341M → I in TMAU; profoundly alters enzyme function. 1 Publication
    VAR_037308
    Natural varianti492 – 4921R → W in TMAU; loss of activity; affects FAD binding. 2 Publications
    VAR_008145

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi602079. phenotype.
    Orphaneti35056. Trimethylaminuria.
    PharmGKBiPA166.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 532531Dimethylaniline monooxygenase [N-oxide-forming] 3PRO_0000147654Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei401 – 4011PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP31513.
    PRIDEiP31513.

    PTM databases

    PhosphoSiteiP31513.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    ArrayExpressiP31513.
    BgeeiP31513.
    CleanExiHS_FMO3.
    GenevestigatoriP31513.

    Organism-specific databases

    HPAiHPA008065.
    HPA013750.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000356729.

    Structurei

    3D structure databases

    ProteinModelPortaliP31513.
    SMRiP31513. Positions 2-231, 300-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FMO family.Curated

    Keywords - Domaini

    Transmembrane

    Phylogenomic databases

    eggNOGiCOG2072.
    HOGENOMiHOG000076537.
    HOVERGENiHBG002037.
    InParanoidiP31513.
    KOiK00485.
    OMAiFMHNSKL.
    OrthoDBiEOG7GXPB6.
    PhylomeDBiP31513.
    TreeFamiTF105285.

    Family and domain databases

    InterProiIPR012143. DiMe-aniline_mOase.
    IPR000960. Flavin_mOase.
    IPR020946. Flavin_mOase-like.
    IPR002255. Flavin_mOase_3.
    [Graphical view]
    PfamiPF00743. FMO-like. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000332. FMO. 1 hit.
    PRINTSiPR00370. FMOXYGENASE.
    PR01123. FMOXYGENASE3.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P31513-1 [UniParc]FASTAAdd to Basket

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    MGKKVAIIGA GVSGLASIRS CLEEGLEPTC FEKSNDIGGL WKFSDHAEEG    50
    RASIYKSVFS NSSKEMMCFP DFPFPDDFPN FMHNSKIQEY IIAFAKEKNL 100
    LKYIQFKTFV SSVNKHPDFA TTGQWDVTTE RDGKKESAVF DAVMVCSGHH 150
    VYPNLPKESF PGLNHFKGKC FHSRDYKEPG VFNGKRVLVV GLGNSGCDIA 200
    TELSRTAEQV MISSRSGSWV MSRVWDNGYP WDMLLVTRFG TFLKNNLPTA 250
    ISDWLYVKQM NARFKHENYG LMPLNGVLRK EPVFNDELPA SILCGIVSVK 300
    PNVKEFTETS AIFEDGTIFE GIDCVIFATG YSFAYPFLDE SIIKSRNNEI 350
    ILFKGVFPPL LEKSTIAVIG FVQSLGAAIP TVDLQSRWAA QVIKGTCTLP 400
    SMEDMMNDIN EKMEKKRKWF GKSETIQTDY IVYMDELSSF IGAKPNIPWL 450
    FLTDPKLAME VYFGPCSPYQ FRLVGPGQWP GARNAILTQW DRSLKPMQTR 500
    VVGRLQKPCF FFHWLKLFAI PILLIAVFLV LT 532
    Length:532
    Mass (Da):60,033
    Last modified:January 23, 2007 - v5
    Checksum:i729E41D53EFC4110
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti298 – 2981S → T in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti369 – 3691I → L in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti400 – 4056PSMEDM → GPFYGKTL in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti410 – 4101N → I in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti418 – 4192KW → ANG in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti444 – 4452KP → T in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti449 – 4491W → M in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti454 – 4541D → G in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti461 – 4622VY → L in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti478 – 4781Q → S in AAA86284. (PubMed:1542660)Curated
    Sequence conflicti486 – 4861I → M in CAA87632. (PubMed:8654418)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241E → D Modest increase in catalytic efficiency toward trimethylamine, methimazole, ethylenethiourea and sulindac. 1 Publication
    VAR_042705
    Natural varianti32 – 321E → K in TMAU. 1 Publication
    VAR_037306
    Natural varianti52 – 521A → T in TMAU. 1 Publication
    VAR_008146
    Natural varianti61 – 611N → K Loss of activity. 1 Publication
    VAR_042706
    Natural varianti61 – 611N → S in TMAU; more than 90% reduction in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide. 1 Publication
    VAR_037307
    Natural varianti66 – 661M → I in TMAU; loss of activity; affects FAD binding. 2 Publications
    VAR_002423
    Natural varianti132 – 1321D → H.2 Publications
    Corresponds to variant rs12072582 [ dbSNP | Ensembl ].
    VAR_015364
    Natural varianti153 – 1531P → L in TMAU; 90% reduction in catalytic efficiency toward trimethylamine and benzydamine; 34% reduction in catalytic efficiency toward methyl p-tolyl sulfide; nearly no effect on affinity for these substrates. 2 Publications
    VAR_002424
    Natural varianti158 – 1581E → K 35%, 45% and 71% increase in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide, respectively. 5 Publications
    Corresponds to variant rs2266782 [ dbSNP | Ensembl ].
    VAR_002425
    Natural varianti198 – 1981D → E.1 Publication
    VAR_018345
    Natural varianti205 – 2051R → C.2 Publications
    Corresponds to variant rs28363549 [ dbSNP | Ensembl ].
    VAR_018346
    Natural varianti257 – 2571V → M 65% increase in catalytic efficiency toward trimethylamine and 60% reduction toward benzydamine and methyl p-tolyl sulfide. 5 Publications
    Corresponds to variant rs1736557 [ dbSNP | Ensembl ].
    VAR_002426
    Natural varianti277 – 2771V → A.1 Publication
    Corresponds to variant rs2066530 [ dbSNP | Ensembl ].
    VAR_014845
    Natural varianti308 – 3081E → G 16% reduction in catalytic efficiency toward trimethylamine and 40% increase toward benzydamine and methyl p-tolyl sulfide. 4 Publications
    Corresponds to variant rs2266780 [ dbSNP | Ensembl ].
    VAR_002427
    Natural varianti360 – 3601L → P.2 Publications
    Corresponds to variant rs28363581 [ dbSNP | Ensembl ].
    VAR_015365
    Natural varianti362 – 3621E → Q.2 Publications
    Corresponds to variant rs2066532 [ dbSNP | Ensembl ].
    VAR_014846
    Natural varianti387 – 3871R → L in TMAU. 1 Publication
    Corresponds to variant rs72549331 [ dbSNP | Ensembl ].
    VAR_008147
    Natural varianti416 – 4161K → N 2-fold decrease in affinity for trimethylamine; 3-fold decrease in catalytic efficiency toward methimazole; 3-fold increase in catalytic efficiency toward sulindac; 30% increase in catalytic efficiency toward ethylenethiourea. 1 Publication
    VAR_042707
    Natural varianti434 – 4341M → I in TMAU; profoundly alters enzyme function. 1 Publication
    VAR_037308
    Natural varianti492 – 4921R → W in TMAU; loss of activity; affects FAD binding. 2 Publications
    VAR_008145
    Natural varianti503 – 5031G → R.1 Publication
    VAR_015366

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83772 mRNA. Translation: AAA86284.1.
    Z47552 mRNA. Translation: CAA87632.1.
    U39967
    , U39961, U39962, U39963, U39964, U39965, U39966 Genomic DNA. Translation: AAC51932.1.
    AY895830 Genomic DNA. Translation: AAW65372.1.
    AK313197 mRNA. Translation: BAG36013.1.
    AL021026 Genomic DNA. Translation: CAA15908.1.
    CH471067 Genomic DNA. Translation: EAW90887.1.
    BC032016 mRNA. Translation: AAH32016.1.
    CCDSiCCDS1292.1.
    PIRiA38228.
    S62367. S51130.
    RefSeqiNP_001002294.1. NM_001002294.2.
    NP_008825.4. NM_006894.5.
    UniGeneiHs.445350.

    Genome annotation databases

    EnsembliENST00000367755; ENSP00000356729; ENSG00000007933.
    GeneIDi2328.
    KEGGihsa:2328.
    UCSCiuc001ghh.3. human.

    Polymorphism databases

    DMDMi6166183.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Protein Spotlight

    A case for discomfort - Issue 149 of June 2013

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83772 mRNA. Translation: AAA86284.1 .
    Z47552 mRNA. Translation: CAA87632.1 .
    U39967
    , U39961 , U39962 , U39963 , U39964 , U39965 , U39966 Genomic DNA. Translation: AAC51932.1 .
    AY895830 Genomic DNA. Translation: AAW65372.1 .
    AK313197 mRNA. Translation: BAG36013.1 .
    AL021026 Genomic DNA. Translation: CAA15908.1 .
    CH471067 Genomic DNA. Translation: EAW90887.1 .
    BC032016 mRNA. Translation: AAH32016.1 .
    CCDSi CCDS1292.1.
    PIRi A38228.
    S62367. S51130.
    RefSeqi NP_001002294.1. NM_001002294.2.
    NP_008825.4. NM_006894.5.
    UniGenei Hs.445350.

    3D structure databases

    ProteinModelPortali P31513.
    SMRi P31513. Positions 2-231, 300-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000356729.

    PTM databases

    PhosphoSitei P31513.

    Polymorphism databases

    DMDMi 6166183.

    Proteomic databases

    PaxDbi P31513.
    PRIDEi P31513.

    Protocols and materials databases

    DNASUi 2328.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367755 ; ENSP00000356729 ; ENSG00000007933 .
    GeneIDi 2328.
    KEGGi hsa:2328.
    UCSCi uc001ghh.3. human.

    Organism-specific databases

    CTDi 2328.
    GeneCardsi GC01P171060.
    GeneReviewsi FMO3.
    HGNCi HGNC:3771. FMO3.
    HPAi HPA008065.
    HPA013750.
    MIMi 136132. gene.
    602079. phenotype.
    neXtProti NX_P31513.
    Orphaneti 35056. Trimethylaminuria.
    PharmGKBi PA166.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2072.
    HOGENOMi HOG000076537.
    HOVERGENi HBG002037.
    InParanoidi P31513.
    KOi K00485.
    OMAi FMHNSKL.
    OrthoDBi EOG7GXPB6.
    PhylomeDBi P31513.
    TreeFami TF105285.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00223-MONOMER.
    Reactomei REACT_13653. FMO oxidizes nucleophiles.
    SABIO-RK P31513.

    Miscellaneous databases

    GeneWikii Flavin_containing_monooxygenase_3.
    GenomeRNAii 2328.
    NextBioi 9447.
    PROi P31513.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31513.
    Bgeei P31513.
    CleanExi HS_FMO3.
    Genevestigatori P31513.

    Family and domain databases

    InterProi IPR012143. DiMe-aniline_mOase.
    IPR000960. Flavin_mOase.
    IPR020946. Flavin_mOase-like.
    IPR002255. Flavin_mOase_3.
    [Graphical view ]
    Pfami PF00743. FMO-like. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000332. FMO. 1 hit.
    PRINTSi PR00370. FMOXYGENASE.
    PR01123. FMOXYGENASE3.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver."
      Lomri N., Gu Q., Cashman J.R.
      Proc. Natl. Acad. Sci. U.S.A. 89:1685-1689(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Differential developmental and tissue-specific regulation of expression of the genes encoding three members of the flavin-containing monooxygenase family of man, FMO1, FMO3 and FM04."
      Dolphin C.T., Cullingford T.E., Shephard E.A., Smith R.L., Phillips I.R.
      Eur. J. Biochem. 235:683-689(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA."
      Dolphin C.T., Riley J.H., Smith R.L., Shephard E.A., Phillips I.R.
      Genomics 46:260-267(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. NIEHS SNPs program
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-132; LYS-158; CYS-205; MET-257; ALA-277; GLY-308; PRO-360 AND GLN-362.
    5. "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].
      Tissue: Liver.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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], VARIANT MET-257.
      Tissue: Brain and Lung.
    9. "Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication."
      Treacy E.P., Akerman B.R., Chow L.M.L., Youil R., Bibeau C., Lin J., Bruce A.G., Knight M., Danks D.M., Cashman J.R., Forrest S.M.
      Hum. Mol. Genet. 7:839-845(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, VARIANTS TMAU ILE-66 AND LEU-153, VARIANTS LYS-158; MET-257 AND GLY-308.
    10. "Two novel mutations of the FMO3 gene in a proband with trimethylaminuria."
      Akerman B.R., Forrest S.M., Chow L.M.L., Youil R., Knight M., Treacy E.P.
      Hum. Mutat. 13:376-379(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TMAU ILE-66 AND TRP-492.
    11. "Trimethylaminuria is caused by mutations of the FMO3 gene in a North American cohort."
      Akerman B.R., Lemass H., Chow L.M.L., Lambert D.M., Greenberg C., Bibeau C., Mamer O.A., Treacy E.P.
      Mol. Genet. Metab. 68:24-31(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TMAU THR-52 AND LEU-387, VARIANTS LYS-158 AND GLY-308.
    12. "Compound heterozygosity for missense mutations in the flavin-containing monooxygenase 3 (FM03) gene in patients with fish-odour syndrome."
      Dolphin C.T., Janmohamed A., Smith R.L., Shephard E.A., Phillips I.R.
      Pharmacogenetics 10:799-807(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TMAU SER-61; LEU-153; ILE-434 AND TRP-492, CHARACTERIZATION OF VARIANTS TMAU SER-61; LEU-153; ILE-434 AND TRP-492.
    13. "Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans."
      Furnes B., Feng J., Sommer S.S., Schlenk D.
      Drug Metab. Dispos. 31:187-193(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIS-132; LYS-158; MET-257; PRO-360; GLN-362 AND ARG-503.
    14. "Two novel single nucleotide polymorphisms (SNPs) of the FMO3 gene in Japanese."
      Fujieda M., Yamazaki H., Togashi M., Saito T., Kamataki T.
      Drug Metab. Pharmacokinet. 18:333-335(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLU-198 AND CYS-205.
    15. "Deleterious mutations in the flavin-containing monooxygenase 3 (FMO3) gene causing trimethylaminuria."
      Zhang J., Tran Q., Lattard V., Cashman J.R.
      Pharmacogenetics 13:495-500(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TMAU LYS-32.
    16. "Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria."
      Yeung C.K., Adman E.T., Rettie A.E.
      Arch. Biochem. Biophys. 464:251-259(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS TMAU SER-61; ILE-66; LEU-153 AND TRP-492, CHARACTERIZATION OF VARIANTS LYS-158; MET-257 AND GLY-308.
    17. "Identification and functional analysis of common human flavin-containing monooxygenase 3 genetic variants."
      Koukouritaki S.B., Poch M.T., Henderson M.C., Siddens L.K., Krueger S.K., VanDyke J.E., Williams D.E., Pajewski N.M., Wang T., Hines R.N.
      J. Pharmacol. Exp. Ther. 320:266-273(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ASP-24; LYS-61; LYS-158; MET-257; GLY-308 AND ASN-416, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ASP-24; LYS-61 AND ASN-416.

    Entry informationi

    Entry nameiFMO3_HUMAN
    AccessioniPrimary (citable) accession number: P31513
    Secondary accession number(s): B2R816, Q14854, Q8N5N5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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