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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 3

Gene

FMO3

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

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 (PubMed:9224773).By similarity1 Publication

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

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00223-MONOMER.
    BRENDAi1.14.13.148. 2681.
    1.14.13.8. 2681.
    ReactomeiREACT_13653. FMO oxidises nucleophiles.
    REACT_268486. Defective FMO3 causes Trimethylaminuria (TMAU).
    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 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3771. FMO3.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Involvement in diseasei

    Trimethylaminuria (TMAU)5 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionInborn 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.

    See also OMIM:602079
    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. 2 Publications
    VAR_037307
    Natural varianti66 – 661M → I in TMAU; loss of activity; affects FAD binding. 3 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. 3 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. 3 Publications
    VAR_008145

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi602079. phenotype.
    Orphaneti35056. Trimethylaminuria.
    PharmGKBiPA166.

    Chemistry

    DrugBankiDB00918. Almotriptan.
    DB00501. Cimetidine.
    DB00363. Clozapine.
    DB00250. Dapsone.
    DB01254. Dasatinib.
    DB00334. Olanzapine.
    DB00675. Tamoxifen.
    DB05294. Vandetanib.
    DB00582. Voriconazole.

    Polymorphism and mutation databases

    BioMutaiFMO3.
    DMDMi6166183.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    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

    BgeeiP31513.
    CleanExiHS_FMO3.
    ExpressionAtlasiP31513. baseline and differential.
    GenevisibleiP31513. HS.

    Organism-specific databases

    HPAiHPA008065.
    HPA013750.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000356729.

    Structurei

    3D structure databases

    ProteinModelPortaliP31513.
    SMRiP31513. Positions 4-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FMO family.Curated

    Keywords - Domaini

    Transmembrane

    Phylogenomic databases

    eggNOGiCOG2072.
    GeneTreeiENSGT00760000119232.
    HOGENOMiHOG000076537.
    HOVERGENiHBG002037.
    InParanoidiP31513.
    KOiK00485.
    OMAiAQVIKGT.
    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

    « Hide

            10         20         30         40         50
    MGKKVAIIGA GVSGLASIRS CLEEGLEPTC FEKSNDIGGL WKFSDHAEEG
    60 70 80 90 100
    RASIYKSVFS NSSKEMMCFP DFPFPDDFPN FMHNSKIQEY IIAFAKEKNL
    110 120 130 140 150
    LKYIQFKTFV SSVNKHPDFA TTGQWDVTTE RDGKKESAVF DAVMVCSGHH
    160 170 180 190 200
    VYPNLPKESF PGLNHFKGKC FHSRDYKEPG VFNGKRVLVV GLGNSGCDIA
    210 220 230 240 250
    TELSRTAEQV MISSRSGSWV MSRVWDNGYP WDMLLVTRFG TFLKNNLPTA
    260 270 280 290 300
    ISDWLYVKQM NARFKHENYG LMPLNGVLRK EPVFNDELPA SILCGIVSVK
    310 320 330 340 350
    PNVKEFTETS AIFEDGTIFE GIDCVIFATG YSFAYPFLDE SIIKSRNNEI
    360 370 380 390 400
    ILFKGVFPPL LEKSTIAVIG FVQSLGAAIP TVDLQSRWAA QVIKGTCTLP
    410 420 430 440 450
    SMEDMMNDIN EKMEKKRKWF GKSETIQTDY IVYMDELSSF IGAKPNIPWL
    460 470 480 490 500
    FLTDPKLAME VYFGPCSPYQ FRLVGPGQWP GARNAILTQW DRSLKPMQTR
    510 520 530
    VVGRLQKPCF FFHWLKLFAI PILLIAVFLV LT
    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. 2 Publications
    VAR_037307
    Natural varianti66 – 661M → I in TMAU; loss of activity; affects FAD binding. 3 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. 3 Publications
    VAR_002424
    Natural varianti158 – 1581E → K 35%, 45% and 71% increase in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide, respectively. 6 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. 6 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. 5 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. 3 Publications
    VAR_008145
    Natural varianti503 – 5031G → R.1 Publication
    VAR_015366

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    ProteinModelPortaliP31513.
    SMRiP31513. Positions 4-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9606.ENSP00000356729.

    Chemistry

    DrugBankiDB00918. Almotriptan.
    DB00501. Cimetidine.
    DB00363. Clozapine.
    DB00250. Dapsone.
    DB01254. Dasatinib.
    DB00334. Olanzapine.
    DB00675. Tamoxifen.
    DB05294. Vandetanib.
    DB00582. Voriconazole.

    PTM databases

    PhosphoSiteiP31513.

    Polymorphism and mutation databases

    BioMutaiFMO3.
    DMDMi6166183.

    Proteomic databases

    PaxDbiP31513.
    PRIDEiP31513.

    Protocols and materials databases

    DNASUi2328.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi2328.
    GeneCardsiGC01P171060.
    GeneReviewsiFMO3.
    HGNCiHGNC:3771. FMO3.
    HPAiHPA008065.
    HPA013750.
    MIMi136132. gene.
    602079. phenotype.
    neXtProtiNX_P31513.
    Orphaneti35056. Trimethylaminuria.
    PharmGKBiPA166.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG2072.
    GeneTreeiENSGT00760000119232.
    HOGENOMiHOG000076537.
    HOVERGENiHBG002037.
    InParanoidiP31513.
    KOiK00485.
    OMAiAQVIKGT.
    OrthoDBiEOG7GXPB6.
    PhylomeDBiP31513.
    TreeFamiTF105285.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00223-MONOMER.
    BRENDAi1.14.13.148. 2681.
    1.14.13.8. 2681.
    ReactomeiREACT_13653. FMO oxidises nucleophiles.
    REACT_268486. Defective FMO3 causes Trimethylaminuria (TMAU).
    SABIO-RKP31513.

    Miscellaneous databases

    GeneWikiiFlavin_containing_monooxygenase_3.
    GenomeRNAii2328.
    NextBioi9447.
    PROiP31513.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP31513.
    CleanExiHS_FMO3.
    ExpressionAtlasiP31513. baseline and differential.
    GenevisibleiP31513. HS.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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. "Baculovirus-mediated expression and purification of human FMO3: catalytic, immunochemical, and structural characterization."
      Haining R.L., Hunter A.P., Sadeque A.J., Philpot R.M., Rettie A.E.
      Drug Metab. Dispos. 25:790-797(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "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.
    11. "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.
    12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "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.
    14. "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.
    15. "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.
    16. "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.
    17. "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.
    18. "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.
    19. "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: July 22, 2015
    This is version 159 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, Direct protein sequencing, 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

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.