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Q99518

- FMO2_HUMAN

UniProt

Q99518 - FMO2_HUMAN

Protein

Dimethylaniline monooxygenase [N-oxide-forming] 2

Gene

FMO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (05 Apr 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the N-oxidation of certain primary alkylamines to their oximes via an N-hydroxylamine intermediate. Inactive toward certain tertiary amines, such as imipramine or chloropromazine. Can catalyze the S-oxidation of methimazole. The truncated form is catalytically inactive.1 Publication

    Catalytic activityi

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

    Cofactori

    FAD.
    Magnesium.

    Regions

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

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. monooxygenase activity Source: Reactome
    3. N,N-dimethylaniline monooxygenase activity Source: BHF-UCL
    4. NADP binding Source: InterPro

    GO - Biological processi

    1. drug metabolic process Source: BHF-UCL
    2. NADPH oxidation Source: UniProtKB
    3. NADP metabolic process Source: BHF-UCL
    4. organic acid metabolic process Source: BHF-UCL
    5. oxygen metabolic process Source: Ensembl
    6. small molecule metabolic process Source: Reactome
    7. toxin metabolic process Source: BHF-UCL
    8. xenobiotic metabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, Magnesium, NADP

    Enzyme and pathway databases

    ReactomeiREACT_13653. FMO oxidizes nucleophiles.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dimethylaniline monooxygenase [N-oxide-forming] 2 (EC:1.14.13.8)
    Alternative name(s):
    Dimethylaniline oxidase 2
    FMO 1B1
    Pulmonary flavin-containing monooxygenase 2
    Short name:
    FMO 2
    Gene namesi
    Name:FMO2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3770. FMO2.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164741534.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 471470Dimethylaniline monooxygenase [N-oxide-forming] 2PRO_0000147646Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Post-translational modificationi

    The truncated form is probably unable to fold correctly and is rapidly degraded.
    FMO2*1 is sumoylated at 'Lys-492'.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    PaxDbiQ99518.
    PRIDEiQ99518.

    PTM databases

    PhosphoSiteiQ99518.

    Expressioni

    Tissue specificityi

    Expressed in lung (at protein level). Expressed predominantly in lung, and at a much lesser extent in kidney. Also expressed in fetal lung, but not in liver, kidney and brain.2 Publications

    Gene expression databases

    ArrayExpressiQ99518.
    BgeeiQ99518.
    CleanExiHS_FMO2.
    GenevestigatoriQ99518.

    Organism-specific databases

    HPAiHPA028261.

    Interactioni

    Protein-protein interaction databases

    IntActiQ99518. 2 interactions.
    STRINGi9606.ENSP00000209929.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99518.
    SMRiQ99518. Positions 3-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FMO family.Curated

    Keywords - Domaini

    Transmembrane

    Phylogenomic databases

    eggNOGiCOG2072.
    HOGENOMiHOG000076537.
    HOVERGENiHBG002037.
    InParanoidiQ99518.
    KOiK00485.
    OMAiHPDGFEG.
    OrthoDBiEOG7GXPB6.
    PhylomeDBiQ99518.
    TreeFamiTF105285.

    Family and domain databases

    InterProiIPR000960. Flavin_mOase.
    IPR020946. Flavin_mOase-like.
    IPR002254. Flavin_mOase_2.
    [Graphical view]
    PfamiPF00743. FMO-like. 1 hit.
    [Graphical view]
    PRINTSiPR00370. FMOXYGENASE.
    PR01122. FMOXYGENASE2.

    Sequencei

    Sequence statusi: Complete.

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

    Q99518-1 [UniParc]FASTAAdd to Basket

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    MAKKVAVIGA GVSGLISLKC CVDEGLEPTC FERTEDIGGV WRFKENVEDG    50
    RASIYQSVVT NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL 100
    LKYIQFQTTV LSVRKCPDFS SSGQWKVVTQ SNGKEQSAVF DAVMVCSGHH 150
    ILPHIPLKSF PGMERFKGQY FHSRQYKHPD GFEGKRILVI GMGNSGSDIA 200
    VELSKNAAQV FISTRHGTWV MSRISEDGYP WDSVFHTRFR SMLRNVLPRT 250
    AVKWMIEQQM NRWFNHENYG LEPQNKYIMK EPVLNDDVPS RLLCGAIKVK 300
    STVKELTETS AIFEDGTVEE NIDVIIFATG YSFSFPFLED SLVKVENNMV 350
    SLYKYIFPAH LDKSTLACIG LIQPLGSIFP TAELQARWVT RVFKGLCSLP 400
    SERTMMMDII KRNEKRIDLF GESQSQTLQT NYVDYLDELA LEIGAKPDFC 450
    SLLFKDPKLA VRLYFGPCNS Y 471
    Length:471
    Mass (Da):53,644
    Last modified:April 5, 2011 - v4
    Checksum:iAF87E304131BA703
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711D → DD in AAW82431. 1 PublicationCurated

    Polymorphismi

    The sequence shown is that of the allele FMO2*2A. There are two alleles; one major, FMO2*2A (truncated form) and one minor, FMO2*1 (full-length form similar to the protein found in other mammals). A nonsense mutation transforms the Gln-472 of FMO2*1 in a premature stop codon. FMO2*2A occurs in essentially 100% of Caucasians and Asians. FMO2*1 is present at a frequency of approximately 4% to 13% in the sample of population of African descent. FMO2*2A is catalytically inactive.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361D → G.2 Publications
    Corresponds to variant rs2020870 [ dbSNP | Ensembl ].
    VAR_014840
    Natural varianti59 – 591V → I.1 Publication
    Corresponds to variant rs55708639 [ dbSNP | Ensembl ].
    VAR_015361
    Natural varianti69 – 691F → Y.1 Publication
    Corresponds to variant rs28745274 [ dbSNP | Ensembl ].
    VAR_022185
    Natural varianti81 – 811F → S.1 Publication
    Corresponds to variant rs2020860 [ dbSNP | Ensembl ].
    VAR_014841
    Natural varianti182 – 1821F → S.2 Publications
    Corresponds to variant rs2307492 [ dbSNP | Ensembl ].
    VAR_014842
    Natural varianti195 – 1951S → L.2 Publications
    Corresponds to variant rs2020862 [ dbSNP | Ensembl ].
    VAR_014843
    Natural varianti238 – 2381R → Q.2 Publications
    Corresponds to variant rs28369895 [ dbSNP | Ensembl ].
    VAR_015362
    Natural varianti314 – 3141E → G.1 Publication
    Corresponds to variant rs2020863 [ dbSNP | Ensembl ].
    VAR_022186
    Natural varianti391 – 3911R → T.2 Publications
    Corresponds to variant rs28369899 [ dbSNP | Ensembl ].
    VAR_015363
    Natural varianti413 – 4131N → K.2 Publications
    Corresponds to variant rs2020865 [ dbSNP | Ensembl ].
    VAR_014844
    Natural varianti471 – 4711Y → YQYRLVGPGQWEGARNAIFT QKQRILKPLKTRALKDSSNF SVSFLLKILGLLAVVVAFFC QLQWS in allele FMO2*1.
    VAR_064887

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09267 mRNA. Translation: CAA70462.1.
    AY916056 Genomic DNA. Translation: AAW82431.1.
    BT006979 mRNA. Translation: AAP35625.1.
    AL021026 Genomic DNA. Translation: CAA15910.1.
    CH471067 Genomic DNA. Translation: EAW90889.1.
    BC005894 mRNA. Translation: AAH05894.1.
    CCDSiCCDS1293.1.
    RefSeqiNP_001451.1. NM_001460.3.
    UniGeneiHs.144912.

    Genome annotation databases

    EnsembliENST00000209929; ENSP00000209929; ENSG00000094963.
    GeneIDi2327.
    KEGGihsa:2327.
    UCSCiuc001ghk.1. human.

    Polymorphism databases

    DMDMi327478599.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09267 mRNA. Translation: CAA70462.1 .
    AY916056 Genomic DNA. Translation: AAW82431.1 .
    BT006979 mRNA. Translation: AAP35625.1 .
    AL021026 Genomic DNA. Translation: CAA15910.1 .
    CH471067 Genomic DNA. Translation: EAW90889.1 .
    BC005894 mRNA. Translation: AAH05894.1 .
    CCDSi CCDS1293.1.
    RefSeqi NP_001451.1. NM_001460.3.
    UniGenei Hs.144912.

    3D structure databases

    ProteinModelPortali Q99518.
    SMRi Q99518. Positions 3-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q99518. 2 interactions.
    STRINGi 9606.ENSP00000209929.

    PTM databases

    PhosphoSitei Q99518.

    Polymorphism databases

    DMDMi 327478599.

    Proteomic databases

    PaxDbi Q99518.
    PRIDEi Q99518.

    Protocols and materials databases

    DNASUi 2327.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000209929 ; ENSP00000209929 ; ENSG00000094963 .
    GeneIDi 2327.
    KEGGi hsa:2327.
    UCSCi uc001ghk.1. human.

    Organism-specific databases

    CTDi 2327.
    GeneCardsi GC01P171154.
    HGNCi HGNC:3770. FMO2.
    HPAi HPA028261.
    MIMi 603955. gene.
    neXtProti NX_Q99518.
    PharmGKBi PA164741534.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2072.
    HOGENOMi HOG000076537.
    HOVERGENi HBG002037.
    InParanoidi Q99518.
    KOi K00485.
    OMAi HPDGFEG.
    OrthoDBi EOG7GXPB6.
    PhylomeDBi Q99518.
    TreeFami TF105285.

    Enzyme and pathway databases

    Reactomei REACT_13653. FMO oxidizes nucleophiles.

    Miscellaneous databases

    GeneWikii FMO2.
    GenomeRNAii 2327.
    NextBioi 9443.
    PROi Q99518.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99518.
    Bgeei Q99518.
    CleanExi HS_FMO2.
    Genevestigatori Q99518.

    Family and domain databases

    InterProi IPR000960. Flavin_mOase.
    IPR020946. Flavin_mOase-like.
    IPR002254. Flavin_mOase_2.
    [Graphical view ]
    Pfami PF00743. FMO-like. 1 hit.
    [Graphical view ]
    PRINTSi PR00370. FMOXYGENASE.
    PR01122. FMOXYGENASE2.
    ProtoNeti Search...

    Publicationsi

    1. "The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein."
      Dolphin C.T., Beckett D.J., Janmohamed A., Cullingford T.E., Smith R.L., Shephard E.A., Phillips I.R.
      J. Biol. Chem. 273:30599-30607(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALLELE FMO2*1 TYR-471 INS.
      Tissue: Lung.
    2. NIEHS SNPs program
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALLELE FMO2*1 TYR-471 INS, VARIANTS GLY-36; TYR-69; SER-81; SER-182; LEU-195; GLN-238; GLY-314; THR-391 AND LYS-413.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], ALLELE FMO2*1 TYR-471 INS.
      Tissue: Skeletal muscle.
    7. "Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African-Americans."
      Whetstine J.R., Yueh M.F., McCarver D.G., Williams D.E., Park C.S., Kang J.H., Cha Y.N., Dolphin C.T., Shephard E.A., Phillips I.R., Hines R.N.
      Toxicol. Appl. Pharmacol. 168:216-224(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALLELE FMO2*1 TYR-471 INS.
    8. "In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
      Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
      J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
      Tissue: Cervix carcinoma.
    9. "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 GLY-36; ILE-59; SER-182; LEU-195; GLN-238; THR-391 AND LYS-413.
    10. "The potentially deleterious functional variant flavin-containing monooxygenase 2*1 is at high frequency throughout sub-Saharan Africa."
      Veeramah K.R., Thomas M.G., Weale M.E., Zeitlyn D., Tarekegn A., Bekele E., Mendell N.R., Shephard E.A., Bradman N., Phillips I.R.
      Pharmacogenet. Genomics 18:877-886(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALLELE FMO2*1 TYR-471 INS.

    Entry informationi

    Entry nameiFMO2_HUMAN
    AccessioniPrimary (citable) accession number: Q99518
    Secondary accession number(s): Q5EBX4, Q86U73, Q9BRX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: April 5, 2011
    Last modified: October 1, 2014
    This is version 142 of the entry and version 4 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3