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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei32FADBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi9 – 13FADBy similarity5
    Nucleotide bindingi40 – 41FADBy similarity2
    Nucleotide bindingi60 – 61NADPBy similarity2
    Nucleotide bindingi61 – 62FADBy similarity2
    Nucleotide bindingi195 – 198NADPBy similarity4

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionMonooxygenase, Oxidoreductase
    LigandFAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS00223-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.14.13.148 2681
    1.14.13.8 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-217271 FMO oxidises nucleophiles
    R-HSA-5579019 Defective FMO3 causes Trimethylaminuria (TMAU)

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P31513

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:FMO3
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000007933.12

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:3771 FMO3

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    136132 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P31513

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei510 – 530HelicalSequence analysisAdd BLAST21

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Trimethylaminuria (TMAU)6 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)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03730632E → K in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549320EnsemblClinVar.1
    Natural variantiVAR_00814652A → T in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549321EnsemblClinVar.1
    Natural variantiVAR_03730761N → S in TMAU; more than 90% reduction in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide. 2 PublicationsCorresponds to variant dbSNP:rs72549322EnsemblClinVar.1
    Natural variantiVAR_00242366M → I in TMAU; loss of activity; affects FAD binding. 3 PublicationsCorresponds to variant dbSNP:rs72549323EnsemblClinVar.1
    Natural variantiVAR_002424153P → 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 PublicationsCorresponds to variant dbSNP:rs72549326EnsemblClinVar.1
    Natural variantiVAR_008147387R → L in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549331EnsemblClinVar.1
    Natural variantiVAR_037308434M → I in TMAU; profoundly alters enzyme function. 1 PublicationCorresponds to variant dbSNP:rs72549332EnsemblClinVar.1
    Natural variantiVAR_008145492R → W in TMAU; loss of activity; affects FAD binding. 3 PublicationsCorresponds to variant dbSNP:rs72549334EnsemblClinVar.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    2328

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    FMO3

    MalaCards human disease database

    More...
    MalaCardsi
    FMO3
    MIMi602079 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000007933

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    35056 NON RARE IN EUROPE: Trimethylaminuria
    468726 Severe primary trimethylaminuria

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA166

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3430864

    Drug and drug target database

    More...
    DrugBanki
    DB00918 Almotriptan
    DB00501 Cimetidine
    DB00363 Clozapine
    DB00250 Dapsone
    DB01254 Dasatinib
    DB00334 Olanzapine
    DB00675 Tamoxifen
    DB05294 Vandetanib
    DB00582 Voriconazole

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    FMO3

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    6166183

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001476542 – 532Dimethylaniline monooxygenase [N-oxide-forming] 3Add BLAST531

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei401PhosphoserineBy similarity1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P31513

    PeptideAtlas

    More...
    PeptideAtlasi
    P31513

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P31513

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    54793

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P31513

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P31513

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Liver.

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000007933 Expressed in 124 organ(s), highest expression level in liver

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_FMO3

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P31513 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P31513 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA013750

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    CREB3O43889-23EBI-12361463,EBI-625022

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    108615, 1 interactor

    Protein interaction database and analysis system

    More...
    IntActi
    P31513, 4 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000356729

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P31513

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P31513

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the FMO family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1399 Eukaryota
    COG2072 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000161339

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000076537

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG002037

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P31513

    KEGG Orthology (KO)

    More...
    KOi
    K00485

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NARFKHE

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0465

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P31513

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105285

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.50.50.60, 4 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036188 FAD/NAD-bd_sf
    IPR000960 Flavin_mOase
    IPR020946 Flavin_mOase-like
    IPR002255 Flavin_mOase_3

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00743 FMO-like, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000332 FMO, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00370 FMOXYGENASE
    PR01123 FMOXYGENASE3

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51905 SSF51905, 2 hits

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i729E41D53EFC4110
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    V9GYP3V9GYP3_HUMAN
    Flavin-containing monooxygenase
    FMO3
    48Annotation score:

    Annotation score:2 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    V9GZ60V9GZ60_HUMAN
    Dimethylaniline monooxygenase [N-ox...
    FMO3
    218Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti298S → T in AAA86284 (PubMed:1542660).Curated1
    Sequence conflicti369I → L in AAA86284 (PubMed:1542660).Curated1
    Sequence conflicti400 – 405PSMEDM → GPFYGKTL in AAA86284 (PubMed:1542660).Curated6
    Sequence conflicti410N → I in AAA86284 (PubMed:1542660).Curated1
    Sequence conflicti418 – 419KW → ANG in AAA86284 (PubMed:1542660).Curated2
    Sequence conflicti444 – 445KP → T in AAA86284 (PubMed:1542660).Curated2
    Sequence conflicti449W → M in AAA86284 (PubMed:1542660).Curated1
    Sequence conflicti454D → G in AAA86284 (PubMed:1542660).Curated1
    Sequence conflicti461 – 462VY → L in AAA86284 (PubMed:1542660).Curated2
    Sequence conflicti478Q → S in AAA86284 (PubMed:1542660).Curated1
    Sequence conflicti486I → M in CAA87632 (PubMed:8654418).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_04270524E → D Modest increase in catalytic efficiency toward trimethylamine, methimazole, ethylenethiourea and sulindac. 1 Publication1
    Natural variantiVAR_03730632E → K in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549320EnsemblClinVar.1
    Natural variantiVAR_00814652A → T in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549321EnsemblClinVar.1
    Natural variantiVAR_04270661N → K Loss of activity. 1 Publication1
    Natural variantiVAR_03730761N → S in TMAU; more than 90% reduction in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide. 2 PublicationsCorresponds to variant dbSNP:rs72549322EnsemblClinVar.1
    Natural variantiVAR_00242366M → I in TMAU; loss of activity; affects FAD binding. 3 PublicationsCorresponds to variant dbSNP:rs72549323EnsemblClinVar.1
    Natural variantiVAR_015364132D → H2 PublicationsCorresponds to variant dbSNP:rs12072582EnsemblClinVar.1
    Natural variantiVAR_002424153P → 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 PublicationsCorresponds to variant dbSNP:rs72549326EnsemblClinVar.1
    Natural variantiVAR_002425158E → K 35%, 45% and 71% increase in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide, respectively. 6 PublicationsCorresponds to variant dbSNP:rs2266782EnsemblClinVar.1
    Natural variantiVAR_018345198D → E1 PublicationCorresponds to variant dbSNP:rs529940450Ensembl.1
    Natural variantiVAR_018346205R → C2 PublicationsCorresponds to variant dbSNP:rs28363549Ensembl.1
    Natural variantiVAR_002426257V → M 65% increase in catalytic efficiency toward trimethylamine and 60% reduction toward benzydamine and methyl p-tolyl sulfide. 6 PublicationsCorresponds to variant dbSNP:rs1736557EnsemblClinVar.1
    Natural variantiVAR_014845277V → A1 PublicationCorresponds to variant dbSNP:rs2066530EnsemblClinVar.1
    Natural variantiVAR_002427308E → G 16% reduction in catalytic efficiency toward trimethylamine and 40% increase toward benzydamine and methyl p-tolyl sulfide. 5 PublicationsCorresponds to variant dbSNP:rs2266780EnsemblClinVar.1
    Natural variantiVAR_015365360L → P2 PublicationsCorresponds to variant dbSNP:rs28363581EnsemblClinVar.1
    Natural variantiVAR_014846362E → Q2 PublicationsCorresponds to variant dbSNP:rs2066532Ensembl.1
    Natural variantiVAR_008147387R → L in TMAU. 1 PublicationCorresponds to variant dbSNP:rs72549331EnsemblClinVar.1
    Natural variantiVAR_042707416K → 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 PublicationCorresponds to variant dbSNP:rs774785217Ensembl.1
    Natural variantiVAR_037308434M → I in TMAU; profoundly alters enzyme function. 1 PublicationCorresponds to variant dbSNP:rs72549332EnsemblClinVar.1
    Natural variantiVAR_008145492R → W in TMAU; loss of activity; affects FAD binding. 3 PublicationsCorresponds to variant dbSNP:rs72549334EnsemblClinVar.1
    Natural variantiVAR_015366503G → R1 PublicationCorresponds to variant dbSNP:rs72549335Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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 No translation available.
    CH471067 Genomic DNA Translation: EAW90887.1
    BC032016 mRNA Translation: AAH32016.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS1292.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A38228
    S62367 S51130

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001002294.1, NM_001002294.2
    NP_001306102.1, NM_001319173.1
    NP_001306103.1, NM_001319174.1
    NP_008825.4, NM_006894.5

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.445350

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000367755; ENSP00000356729; ENSG00000007933

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    2328

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:2328

    UCSC genome browser

    More...
    UCSCi
    uc001ghi.3 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 No translation available.
    CH471067 Genomic DNA Translation: EAW90887.1
    BC032016 mRNA Translation: AAH32016.1
    CCDSiCCDS1292.1
    PIRiA38228
    S62367 S51130
    RefSeqiNP_001002294.1, NM_001002294.2
    NP_001306102.1, NM_001319173.1
    NP_001306103.1, NM_001319174.1
    NP_008825.4, NM_006894.5
    UniGeneiHs.445350

    3D structure databases

    ProteinModelPortaliP31513
    SMRiP31513
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108615, 1 interactor
    IntActiP31513, 4 interactors
    STRINGi9606.ENSP00000356729

    Chemistry databases

    ChEMBLiCHEMBL3430864
    DrugBankiDB00918 Almotriptan
    DB00501 Cimetidine
    DB00363 Clozapine
    DB00250 Dapsone
    DB01254 Dasatinib
    DB00334 Olanzapine
    DB00675 Tamoxifen
    DB05294 Vandetanib
    DB00582 Voriconazole

    PTM databases

    iPTMnetiP31513
    PhosphoSitePlusiP31513

    Polymorphism and mutation databases

    BioMutaiFMO3
    DMDMi6166183

    Proteomic databases

    PaxDbiP31513
    PeptideAtlasiP31513
    PRIDEiP31513
    ProteomicsDBi54793

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    2328
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000367755; ENSP00000356729; ENSG00000007933
    GeneIDi2328
    KEGGihsa:2328
    UCSCiuc001ghi.3 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    2328
    DisGeNETi2328
    EuPathDBiHostDB:ENSG00000007933.12

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    FMO3
    GeneReviewsiFMO3
    HGNCiHGNC:3771 FMO3
    HPAiHPA013750
    MalaCardsiFMO3
    MIMi136132 gene
    602079 phenotype
    neXtProtiNX_P31513
    OpenTargetsiENSG00000007933
    Orphaneti35056 NON RARE IN EUROPE: Trimethylaminuria
    468726 Severe primary trimethylaminuria
    PharmGKBiPA166

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1399 Eukaryota
    COG2072 LUCA
    GeneTreeiENSGT00940000161339
    HOGENOMiHOG000076537
    HOVERGENiHBG002037
    InParanoidiP31513
    KOiK00485
    OMAiNARFKHE
    OrthoDBiEOG091G0465
    PhylomeDBiP31513
    TreeFamiTF105285

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00223-MONOMER
    BRENDAi1.14.13.148 2681
    1.14.13.8 2681
    ReactomeiR-HSA-217271 FMO oxidises nucleophiles
    R-HSA-5579019 Defective FMO3 causes Trimethylaminuria (TMAU)
    SABIO-RKiP31513

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    FMO3 human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    Flavin_containing_monooxygenase_3

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    2328

    Protein Ontology

    More...
    PROi
    PR:P31513

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000007933 Expressed in 124 organ(s), highest expression level in liver
    CleanExiHS_FMO3
    ExpressionAtlasiP31513 baseline and differential
    GenevisibleiP31513 HS

    Family and domain databases

    Gene3Di3.50.50.60, 4 hits
    InterProiView protein in InterPro
    IPR036188 FAD/NAD-bd_sf
    IPR000960 Flavin_mOase
    IPR020946 Flavin_mOase-like
    IPR002255 Flavin_mOase_3
    PfamiView protein in Pfam
    PF00743 FMO-like, 1 hit
    PIRSFiPIRSF000332 FMO, 1 hit
    PRINTSiPR00370 FMOXYGENASE
    PR01123 FMOXYGENASE3
    SUPFAMiSSF51905 SSF51905, 2 hits

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFMO3_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P31513
    Secondary accession number(s): B2R816, Q14854, Q8N5N5
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 188 of the entry and version 5 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. SIMILARITY comments
      Index of protein domains and families
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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