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P31513 (FMO3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FMO3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O. Ref.9

N,N,N-trimethylamine + NADPH + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O. Ref.9

Cofactor

FAD.

Subcellular location

Microsome membrane. Endoplasmic reticulum membrane.

Tissue specificity

Liver.

Involvement in disease

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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16

Sequence similarities

Belongs to the FMO family.

Biophysicochemical properties

Kinetic parameters:

KM=21 µM for trimethylamine (at pH 8.5) Ref.16 Ref.17

KM=31 µM for trimethylamine (at pH 7.4 and 37 degrees Celsius)

KM=43 µM for benzydamine (at pH 7.4 and 37 degrees Celsius)

KM=55.7 µM for ethylenethiourea (at pH 8.5)

KM=71.8 µM for methimazole (at pH 8.5)

KM=150.1 µM for sulindac (at pH 8.5)

KM=248 µM for methyl p-tolyl sulfide (at pH 7.4 and 37 degrees Celsius)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 532531Dimethylaniline monooxygenase [N-oxide-forming] 3
PRO_0000147654

Regions

Nucleotide binding9 – 146FAD Potential
Nucleotide binding191 – 1966NADP Potential

Amino acid modifications

Modified residue4011Phosphoserine By similarity

Natural variations

Natural variant241E → D Modest increase in catalytic efficiency toward trimethylamine, methimazole, ethylenethiourea and sulindac. Ref.17
VAR_042705
Natural variant321E → K in TMAU. Ref.15
VAR_037306
Natural variant521A → T in TMAU. Ref.11
VAR_008146
Natural variant611N → K Loss of activity. Ref.17
VAR_042706
Natural variant611N → S in TMAU; more than 90% reduction in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide. Ref.12 Ref.16
VAR_037307
Natural variant661M → I in TMAU; loss of activity; affects FAD binding. Ref.9 Ref.10 Ref.16
VAR_002423
Natural variant1321D → H. Ref.4 Ref.13
Corresponds to variant rs12072582 [ dbSNP | Ensembl ].
VAR_015364
Natural variant1531P → 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. Ref.9 Ref.12 Ref.16
VAR_002424
Natural variant1581E → K 35%, 45% and 71% increase in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide, respectively. Ref.4 Ref.9 Ref.11 Ref.13 Ref.16 Ref.17
Corresponds to variant rs2266782 [ dbSNP | Ensembl ].
VAR_002425
Natural variant1981D → E. Ref.14
VAR_018345
Natural variant2051R → C. Ref.4 Ref.14
Corresponds to variant rs28363549 [ dbSNP | Ensembl ].
VAR_018346
Natural variant2571V → M 65% increase in catalytic efficiency toward trimethylamine and 60% reduction toward benzydamine and methyl p-tolyl sulfide. Ref.4 Ref.8 Ref.9 Ref.13 Ref.16 Ref.17
Corresponds to variant rs1736557 [ dbSNP | Ensembl ].
VAR_002426
Natural variant2771V → A. Ref.4
Corresponds to variant rs2066530 [ dbSNP | Ensembl ].
VAR_014845
Natural variant3081E → G 16% reduction in catalytic efficiency toward trimethylamine and 40% increase toward benzydamine and methyl p-tolyl sulfide. Ref.4 Ref.9 Ref.11 Ref.16 Ref.17
Corresponds to variant rs2266780 [ dbSNP | Ensembl ].
VAR_002427
Natural variant3601L → P. Ref.4 Ref.13
Corresponds to variant rs28363581 [ dbSNP | Ensembl ].
VAR_015365
Natural variant3621E → Q. Ref.4 Ref.13
Corresponds to variant rs2066532 [ dbSNP | Ensembl ].
VAR_014846
Natural variant3871R → L in TMAU. Ref.11
Corresponds to variant rs72549331 [ dbSNP | Ensembl ].
VAR_008147
Natural variant4161K → 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. Ref.17
VAR_042707
Natural variant4341M → I in TMAU; profoundly alters enzyme function. Ref.12
VAR_037308
Natural variant4921R → W in TMAU; loss of activity; affects FAD binding. Ref.10 Ref.12 Ref.16
VAR_008145
Natural variant5031G → R. Ref.13
VAR_015366

Experimental info

Sequence conflict2981S → T in AAA86284. Ref.1
Sequence conflict3691I → L in AAA86284. Ref.1
Sequence conflict400 – 4056PSMEDM → GPFYGKTL in AAA86284. Ref.1
Sequence conflict4101N → I in AAA86284. Ref.1
Sequence conflict418 – 4192KW → ANG in AAA86284. Ref.1
Sequence conflict444 – 4452KP → T in AAA86284. Ref.1
Sequence conflict4491W → M in AAA86284. Ref.1
Sequence conflict4541D → G in AAA86284. Ref.1
Sequence conflict461 – 4622VY → L in AAA86284. Ref.1
Sequence conflict4781Q → S in AAA86284. Ref.1
Sequence conflict4861I → M in CAA87632. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P31513 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 729E41D53EFC4110

FASTA53260,033
        10         20         30         40         50         60 
MGKKVAIIGA GVSGLASIRS CLEEGLEPTC FEKSNDIGGL WKFSDHAEEG RASIYKSVFS 

        70         80         90        100        110        120 
NSSKEMMCFP DFPFPDDFPN FMHNSKIQEY IIAFAKEKNL LKYIQFKTFV SSVNKHPDFA 

       130        140        150        160        170        180 
TTGQWDVTTE RDGKKESAVF DAVMVCSGHH VYPNLPKESF PGLNHFKGKC FHSRDYKEPG 

       190        200        210        220        230        240 
VFNGKRVLVV GLGNSGCDIA TELSRTAEQV MISSRSGSWV MSRVWDNGYP WDMLLVTRFG 

       250        260        270        280        290        300 
TFLKNNLPTA ISDWLYVKQM NARFKHENYG LMPLNGVLRK EPVFNDELPA SILCGIVSVK 

       310        320        330        340        350        360 
PNVKEFTETS AIFEDGTIFE GIDCVIFATG YSFAYPFLDE SIIKSRNNEI ILFKGVFPPL 

       370        380        390        400        410        420 
LEKSTIAVIG FVQSLGAAIP TVDLQSRWAA QVIKGTCTLP SMEDMMNDIN EKMEKKRKWF 

       430        440        450        460        470        480 
GKSETIQTDY IVYMDELSSF IGAKPNIPWL FLTDPKLAME VYFGPCSPYQ FRLVGPGQWP 

       490        500        510        520        530 
GARNAILTQW DRSLKPMQTR VVGRLQKPCF FFHWLKLFAI PILLIAVFLV LT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Protein Spotlight

A case for discomfort - Issue 149 of June 2013

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83772 mRNA. Translation: AAA86284.1.
Z47552 mRNA. Translation: CAA87632.1.
U39967 expand/collapse EMBL AC list , 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.
CCDSCCDS1292.1.
PIRA38228.
S51130. S62367.
RefSeqNP_001002294.1. NM_001002294.2.
NP_008825.4. NM_006894.5.
UniGeneHs.445350.

3D structure databases

ProteinModelPortalP31513.
SMRP31513. Positions 2-231, 300-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000356729.

PTM databases

PhosphoSiteP31513.

Polymorphism databases

DMDM6166183.

Proteomic databases

PaxDbP31513.
PRIDEP31513.

Protocols and materials databases

DNASU2328.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367755; ENSP00000356729; ENSG00000007933.
ENST00000392085; ENSP00000375935; ENSG00000007933.
GeneID2328.
KEGGhsa:2328.
UCSCuc001ghh.3. human.

Organism-specific databases

CTD2328.
GeneCardsGC01P171060.
GeneReviewsFMO3.
HGNCHGNC:3771. FMO3.
HPAHPA008065.
HPA013750.
MIM136132. gene.
602079. phenotype.
neXtProtNX_P31513.
Orphanet35056. Trimethylaminuria.
PharmGKBPA166.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2072.
HOGENOMHOG000076537.
HOVERGENHBG002037.
InParanoidP31513.
KOK00485.
OMAFMHNSKL.
OrthoDBEOG7GXPB6.
PhylomeDBP31513.
TreeFamTF105285.

Enzyme and pathway databases

BioCycMetaCyc:HS00223-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP31513.

Gene expression databases

ArrayExpressP31513.
BgeeP31513.
CleanExHS_FMO3.
GenevestigatorP31513.

Family and domain databases

InterProIPR012143. DiMe-aniline_mOase.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
[Graphical view]
PfamPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFPIRSF000332. FMO. 1 hit.
PRINTSPR00370. FMOXYGENASE.
PR01123. FMOXYGENASE3.
ProtoNetSearch...

Other

GeneWikiFlavin_containing_monooxygenase_3.
GenomeRNAi2328.
NextBio9447.
PROP31513.
SOURCESearch...

Entry information

Entry nameFMO3_HUMAN
AccessionPrimary (citable) accession number: P31513
Secondary accession number(s): B2R816, Q14854, Q8N5N5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 147 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM