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P31513

- FMO3_HUMAN

UniProt

P31513 - FMO3_HUMAN

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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

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146FAD Reviewed prediction
Nucleotide bindingi191 – 1966NADP Reviewed prediction

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.6 Publications
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.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei401 – 4011Phosphoserine By 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.

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.

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

« Hide

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti298 – 2981S → T in AAA86284. 1 Publication
Sequence conflicti369 – 3691I → L in AAA86284. 1 Publication
Sequence conflicti400 – 4056PSMEDM → GPFYGKTL in AAA86284. 1 Publication
Sequence conflicti410 – 4101N → I in AAA86284. 1 Publication
Sequence conflicti418 – 4192KW → ANG in AAA86284. 1 Publication
Sequence conflicti444 – 4452KP → T in AAA86284. 1 Publication
Sequence conflicti449 – 4491W → M in AAA86284. 1 Publication
Sequence conflicti454 – 4541D → G in AAA86284. 1 Publication
Sequence conflicti461 – 4622VY → L in AAA86284. 1 Publication
Sequence conflicti478 – 4781Q → S in AAA86284. 1 Publication
Sequence conflicti486 – 4861I → M in CAA87632. 1 Publication

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.
ENST00000392085; ENSP00000375935; 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 .
ENST00000392085 ; ENSP00000375935 ; 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

« 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. "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: September 3, 2014
This is version 148 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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