P31513 (FMO3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

FMO3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	532 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Such 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)

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transmembrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	drug metabolic process Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	N,N-dimethylaniline monooxygenase activity Traceable author statement. Source: Reactome NADP binding Inferred from electronic annotation. Source: Compara amino acid binding Inferred from electronic annotation. Source: Compara flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro trimethylamine monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 532	531	Dimethylaniline monooxygenase [N-oxide-forming] 3		PRO_0000147654
Regions
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP Potential
Amino acid modifications
	Modified residue	401	1	Phosphoserine By similarity
Natural variations
	Natural variant	24	1	E → D Modest increase in catalytic efficiency toward trimethylamine, methimazole, ethylenethiourea and sulindac. Ref.17		VAR_042705
	Natural variant	32	1	E → K in TMAU. Ref.15		VAR_037306
	Natural variant	52	1	A → T in TMAU. Ref.11		VAR_008146
	Natural variant	61	1	N → K Loss of activity. Ref.17		VAR_042706
	Natural variant	61	1	N → 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 variant	66	1	M → I in TMAU; loss of activity; affects FAD binding. Ref.9 Ref.10 Ref.16		VAR_002423
	Natural variant	132	1	D → H. Ref.4 Ref.13 Corresponds to variant rs12072582 [ dbSNP | Ensembl ].		VAR_015364
	Natural variant	153	1	P → 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 variant	158	1	E → 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 variant	198	1	D → E. Ref.14		VAR_018345
	Natural variant	205	1	R → C. Ref.4 Ref.14 Corresponds to variant rs28363549 [ dbSNP | Ensembl ].		VAR_018346
	Natural variant	257	1	V → 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 variant	277	1	V → A. Ref.4 Corresponds to variant rs2066530 [ dbSNP | Ensembl ].		VAR_014845
	Natural variant	308	1	E → 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 variant	360	1	L → P. Ref.4 Ref.13 Corresponds to variant rs28363581 [ dbSNP | Ensembl ].		VAR_015365
	Natural variant	362	1	E → Q. Ref.4 Ref.13 Corresponds to variant rs2066532 [ dbSNP | Ensembl ].		VAR_014846
	Natural variant	387	1	R → L in TMAU. Ref.11		VAR_008147
	Natural variant	416	1	K → 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 variant	434	1	M → I in TMAU; profoundly alters enzyme function. Ref.12		VAR_037308
	Natural variant	492	1	R → W in TMAU; loss of activity; affects FAD binding. Ref.10 Ref.12 Ref.16		VAR_008145
	Natural variant	503	1	G → R. Ref.13		VAR_015366
Experimental info
	Sequence conflict	298	1	S → T in AAA86284. Ref.1
	Sequence conflict	369	1	I → L in AAA86284. Ref.1
	Sequence conflict	400 – 405	6	PSMEDM → GPFYGKTL in AAA86284. Ref.1
	Sequence conflict	410	1	N → I in AAA86284. Ref.1
	Sequence conflict	418 – 419	2	KW → ANG in AAA86284. Ref.1
	Sequence conflict	444 – 445	2	KP → T in AAA86284. Ref.1
	Sequence conflict	449	1	W → M in AAA86284. Ref.1
	Sequence conflict	454	1	D → G in AAA86284. Ref.1
	Sequence conflict	461 – 462	2	VY → L in AAA86284. Ref.1
	Sequence conflict	478	1	Q → S in AAA86284. Ref.1
	Sequence conflict	486	1	I → M in CAA87632. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P31513 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 729E41D53EFC4110	FASTA	532	60,033
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00329033.
PIR	A38228. S51130. S62367.
RefSeq	NP_001002294.1. NM_001002294.2. NP_008825.4. NM_006894.5.
UniGene	Hs.445350.
3D structure databases
ProteinModelPortal	P31513.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000356729.
PTM databases
PhosphoSite	P31513.
Polymorphism databases
DMDM	6166183.
Proteomic databases
PaxDb	P31513.
PRIDE	P31513.
Protocols and materials databases
DNASU	2328.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367755; ENSP00000356729; ENSG00000007933. ENST00000392085; ENSP00000375935; ENSG00000007933.
GeneID	2328.
KEGG	hsa:2328.
UCSC	uc001ghh.3. human.
Organism-specific databases
CTD	2328.
GeneCards	GC01P171060.
HGNC	HGNC:3771. FMO3.
HPA	HPA008065. HPA013750.
MIM	136132. gene. 602079. phenotype.
neXtProt	NX_P31513.
Orphanet	35056. Trimethylaminuria.
PharmGKB	PA166.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2072.
HOGENOM	HOG000076537.
HOVERGEN	HBG002037.
InParanoid	P31513.
KO	K00485.
OMA	LTQWDRS.
OrthoDB	EOG4HQDJ5.
PhylomeDB	P31513.
Enzyme and pathway databases
BioCyc	MetaCyc:HS00223-MONOMER.
Reactome	REACT_111217. Metabolism.
SABIO-RK	P31513.
Gene expression databases
ArrayExpress	P31513.
Bgee	P31513.
CleanEx	HS_FMO3.
Genevestigator	P31513.
GermOnline	ENSG00000007933. Homo sapiens.
Family and domain databases
InterPro	IPR012143. DiMe-aniline_mOase. IPR000960. Flavin_mOase. IPR020946. Flavin_mOase-like. IPR002255. Flavin_mOase_3. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01123. FMOXYGENASE3.
ProtoNet	Search...
Other
GenomeRNAi	2328.
NextBio	9447.
SOURCE	Search...

Entry information

Entry name

FMO3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 136 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.