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Q01740 (FMO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 1

EC=1.14.13.8
Alternative name(s):
Dimethylaniline oxidase 1
Fetal hepatic flavin-containing monooxygenase 1
Short name=FMO 1
Gene names
Name:FMO1
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 transcript level

General annotation (Comments)

Function

This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines.

Catalytic activity

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

Cofactor

FAD.

Subcellular location

Microsome membrane. Endoplasmic reticulum membrane.

Tissue specificity

Expressed mainly in fetal liver, adult kidney and, to a lesser extent, the intestine.

Sequence similarities

Belongs to the FMO family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNADPH oxidation

Inferred from direct assay PubMed 15144220. Source: BHF-UCL

organic acid metabolic process

Inferred from direct assay PubMed 15144220. Source: BHF-UCL

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to osmotic stress

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

toxin metabolic process

Inferred from direct assay PubMed 15144220. Source: BHF-UCL

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionN,N-dimethylaniline monooxygenase activity

Inferred from direct assay PubMed 15144220. Source: BHF-UCL

NADP binding

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

monooxygenase activity

Inferred from direct assay PubMed 19262426. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01740-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q01740-2)

The sequence of this isoform differs from the canonical sequence as follows:
     45-107: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 532531Dimethylaniline monooxygenase [N-oxide-forming] 1
PRO_0000147639

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Alternative sequence45 – 10763Missing in isoform 2.
VSP_054543
Natural variant971H → Q. Ref.7
Corresponds to variant rs56841822 [ dbSNP | Ensembl ].
VAR_015358
Natural variant2231R → Q. Ref.2
Corresponds to variant rs16864310 [ dbSNP | Ensembl ].
VAR_022204
Natural variant2271S → T. Ref.2
VAR_022205
Natural variant3031I → T. Ref.7
Corresponds to variant rs28360418 [ dbSNP | Ensembl ].
VAR_015359
Natural variant3031I → V. Ref.2 Ref.7
Corresponds to variant rs16864314 [ dbSNP | Ensembl ].
VAR_015360
Natural variant3221I → V. Ref.2
Corresponds to variant rs28360419 [ dbSNP | Ensembl ].
VAR_022206
Natural variant3271F → L. Ref.2
Corresponds to variant rs28360420 [ dbSNP | Ensembl ].
VAR_022207
Natural variant3731K → R. Ref.2
Corresponds to variant rs28360421 [ dbSNP | Ensembl ].
VAR_022208
Natural variant4741R → H. Ref.2
Corresponds to variant rs28360433 [ dbSNP | Ensembl ].
VAR_022209

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 627B855F38C2EB6D

FASTA53260,311
        10         20         30         40         50         60 
MAKRVAIVGA GVSGLASIKC CLEEGLEPTC FERSDDLGGL WRFTEHVEEG RASLYKSVVS 

        70         80         90        100        110        120 
NSCKEMSCYS DFPFPEDYPN YVPNSQFLEY LKMYANHFDL LKHIQFKTKV CSVTKCSDSA 

       130        140        150        160        170        180 
VSGQWEVVTM HEEKQESAIF DAVMVCTGFL TNPYLPLDSF PGINAFKGQY FHSRQYKHPD 

       190        200        210        220        230        240 
IFKDKRVLVI GMGNSGTDIA VEASHLAEKV FLSTTGGGWV ISRIFDSGYP WDMVFMTRFQ 

       250        260        270        280        290        300 
NMLRNSLPTP IVTWLMERKI NNWLNHANYG LIPEDRTQLK EFVLNDELPG RIITGKVFIR 

       310        320        330        340        350        360 
PSIKEVKENS VIFNNTSKEE PIDIIVFATG YTFAFPFLDE SVVKVEDGQA SLYKYIFPAH 

       370        380        390        400        410        420 
LQKPTLAIIG LIKPLGSMIP TGETQARWAV RVLKGVNKLP PPSVMIEEIN ARKENKPSWF 

       430        440        450        460        470        480 
GLCYCKALQS DYITYIDELL TYINAKPNLF SMLLTDPHLA LTVFFGPCSP YQFRLTGPGK 

       490        500        510        520        530 
WEGARNAIMT QWDRTFKVIK ARVVQESPSP FESFLKVFSF LALLVAIFLI FL 

« Hide

Isoform 2 [UniParc].

Checksum: FC2C46683FE78025
Show »

FASTA46952,813

References

« Hide 'large scale' references
[1]"Cloning, primary sequence, and chromosomal mapping of a human flavin-containing monooxygenase (FMO1)."
Dolphin C.T., Shephard E.A., Povey S., Palmer C.N.A., Ziegler D.M., Ayesh R., Smith R.L., Phillips I.R.
J. Biol. Chem. 266:12379-12385(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]NIEHS SNPs program
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-223; THR-227; VAL-303; VAL-322; LEU-327; ARG-373 AND HIS-474.
[3]"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] (ISOFORMS 1 AND 2).
Tissue: Thalamus.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. 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].
[5]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].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon.
[7]"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 GLN-97; THR-303 AND VAL-303.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64082 mRNA. Translation: AAA52457.1.
AY879266 Genomic DNA. Translation: AAW56076.1.
AK290113 mRNA. Translation: BAF82802.1.
AK296198 mRNA. Translation: BAH12280.1.
AL021026 Genomic DNA. No translation available.
AL445673, AL031274 Genomic DNA. Translation: CAI21383.1.
AL031274, AL445673 Genomic DNA. Translation: CAI22846.1.
CH471067 Genomic DNA. Translation: EAW90892.1.
BC047129 mRNA. Translation: AAH47129.1.
CCDSCCDS1294.1.
PIRA40876.
RefSeqNP_001269621.1. NM_001282692.1.
NP_001269622.1. NM_001282693.1. [Q01740-1]
NP_001269623.1. NM_001282694.1. [Q01740-2]
NP_002012.1. NM_002021.2. [Q01740-1]
UniGeneHs.1424.

3D structure databases

ProteinModelPortalQ01740.
SMRQ01740. Positions 1-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000346901.

PTM databases

PhosphoSiteQ01740.

Polymorphism databases

DMDM399505.

Proteomic databases

PaxDbQ01740.
PRIDEQ01740.

Protocols and materials databases

DNASU2326.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354841; ENSP00000346901; ENSG00000010932.
ENST00000367750; ENSP00000356724; ENSG00000010932.
ENST00000402921; ENSP00000385543; ENSG00000010932.
GeneID2326.
KEGGhsa:2326.
UCSCuc001ghl.3. human. [Q01740-1]

Organism-specific databases

CTD2326.
GeneCardsGC01P171217.
H-InvDBHIX0028548.
HGNCHGNC:3769. FMO1.
HPAHPA023680.
MIM136130. gene.
neXtProtNX_Q01740.
PharmGKBPA165.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2072.
HOGENOMHOG000076537.
HOVERGENHBG002037.
InParanoidQ01740.
KOK00485.
OMATRFQNML.
PhylomeDBQ01740.
TreeFamTF105285.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ01740.
BgeeQ01740.
CleanExHS_FMO1.
GenevestigatorQ01740.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR012143. DiMe-aniline_mOase.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002253. Flavin_mOase_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFPIRSF000332. FMO. 1 hit.
PRINTSPR00370. FMOXYGENASE.
PR01121. FMOXYGENASE1.
ProtoNetSearch...

Other

GeneWikiFlavin_containing_monooxygenase_1.
GenomeRNAi2326.
NextBio35479295.
PROQ01740.
SOURCESearch...

Entry information

Entry nameFMO1_HUMAN
AccessionPrimary (citable) accession number: Q01740
Secondary accession number(s): A8K248 expand/collapse secondary AC list , B7Z3P4, Q5QPT2, Q9UJC2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 131 of the entry and version 3 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

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