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Protein

Dimethylaniline monooxygenase [N-oxide-forming] 4

Gene

FMO4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides.

Catalytic activityi

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

Cofactori

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146FADSequence Analysis
Nucleotide bindingi191 – 1966NADPSequence Analysis

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. N,N-dimethylaniline monooxygenase activity Source: UniProtKB
  3. NADP binding Source: InterPro

GO - Biological processi

  1. drug catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 4 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 4
Hepatic flavin-containing monooxygenase 4
Short name:
FMO 4
Gene namesi
Name:FMO4
Synonyms:FMO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3772. FMO4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei517 – 53115HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28188.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Dimethylaniline monooxygenase [N-oxide-forming] 4PRO_0000147660Add
BLAST

Proteomic databases

PaxDbiP31512.
PRIDEiP31512.

PTM databases

PhosphoSiteiP31512.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiP31512.
CleanExiHS_FMO2.
HS_FMO4.
GenevestigatoriP31512.

Organism-specific databases

HPAiHPA049100.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000356723.

Structurei

3D structure databases

ProteinModelPortaliP31512.
SMRiP31512. Positions 2-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2072.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP31512.
KOiK00485.
OMAiCKIPPSQ.
OrthoDBiEOG7GXPB6.
PhylomeDBiP31512.
TreeFamiTF105285.

Family and domain databases

InterProiIPR012143. DiMe-aniline_mOase.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002256. Flavin_mOase_4.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01124. FMOXYGENASE4.

Sequencei

Sequence statusi: Complete.

P31512-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKVAVIGA GVSGLSSIKC CVDEDLEPTC FERSDDIGGL WKFTESSKDG
60 70 80 90 100
MTRVYKSLVT NVCKEMSCYS DFPFHEDYPN FMNHEKFWDY LQEFAEHFDL
110 120 130 140 150
LKYIQFKTTV CSITKRPDFS ETGQWDVVTE TEGKQNRAVF DAVMVCTGHF
160 170 180 190 200
LNPHLPLEAF PGIHKFKGQI LHSQEYKIPE GFQGKRVLVI GLGNTGGDIA
210 220 230 240 250
VELSRTAAQV LLSTRTGTWV LGRSSDWGYP YNMMVTRRCC SFIAQVLPSR
260 270 280 290 300
FLNWIQERKL NKRFNHEDYG LSITKGKKAK FIVNDELPNC ILCGAITMKT
310 320 330 340 350
SVIEFTETSA VFEDGTVEEN IDVVIFTTGY TFSFPFFEEP LKSLCTKKIF
360 370 380 390 400
LYKQVFPLNL ERATLAIIGL IGLKGSILSG TELQARWVTR VFKGLCKIPP
410 420 430 440 450
SQKLMMEATE KEQLIKRGVF KDTSKDKFDY IAYMDDIAAC IGTKPSIPLL
460 470 480 490 500
FLKDPRLAWE VFFGPCTPYQ YRLMGPGKWD GARNAILTQW DRTLKPLKTR
510 520 530 540 550
IVPDSSKPAS MSHYLKAWGA PVLLASLLLI CKSSLFLKLV RDKLQDRMSP

YLVSLWRG
Length:558
Mass (Da):63,343
Last modified:January 23, 2007 - v3
Checksum:i6981AE9180C07802
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371I → T.1 Publication
VAR_015367
Natural varianti308 – 3081T → S.
Corresponds to variant rs3737925 [ dbSNP | Ensembl ].
VAR_049090
Natural varianti323 – 3231V → A.2 Publications
Corresponds to variant rs1042767 [ dbSNP | Ensembl ].
VAR_015368
Natural varianti339 – 3391E → Q.1 Publication
Corresponds to variant rs61342270 [ dbSNP | Ensembl ].
VAR_015369
Natural varianti372 – 3721G → S.1 Publication
Corresponds to variant rs45599742 [ dbSNP | Ensembl ].
VAR_022305
Natural varianti536 – 5361F → L.1 Publication
Corresponds to variant rs45487792 [ dbSNP | Ensembl ].
VAR_022306
Natural varianti544 – 5441L → R.1 Publication
VAR_022307

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11737 mRNA. Translation: CAA77797.1.
AY882422 Genomic DNA. Translation: AAW56938.1.
BT007444 mRNA. Translation: AAP36112.1.
AL031274 Genomic DNA. Translation: CAB42008.1.
CH471067 Genomic DNA. Translation: EAW90896.1.
BC002780 mRNA. Translation: AAH02780.1.
CCDSiCCDS1295.1.
PIRiS29125.
RefSeqiNP_002013.1. NM_002022.1.
UniGeneiHs.386502.

Genome annotation databases

EnsembliENST00000367749; ENSP00000356723; ENSG00000076258.
GeneIDi2329.
KEGGihsa:2329.
UCSCiuc001gho.3. human.

Polymorphism databases

DMDMi399506.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11737 mRNA. Translation: CAA77797.1.
AY882422 Genomic DNA. Translation: AAW56938.1.
BT007444 mRNA. Translation: AAP36112.1.
AL031274 Genomic DNA. Translation: CAB42008.1.
CH471067 Genomic DNA. Translation: EAW90896.1.
BC002780 mRNA. Translation: AAH02780.1.
CCDSiCCDS1295.1.
PIRiS29125.
RefSeqiNP_002013.1. NM_002022.1.
UniGeneiHs.386502.

3D structure databases

ProteinModelPortaliP31512.
SMRiP31512. Positions 2-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000356723.

PTM databases

PhosphoSiteiP31512.

Polymorphism databases

DMDMi399506.

Proteomic databases

PaxDbiP31512.
PRIDEiP31512.

Protocols and materials databases

DNASUi2329.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367749; ENSP00000356723; ENSG00000076258.
GeneIDi2329.
KEGGihsa:2329.
UCSCiuc001gho.3. human.

Organism-specific databases

CTDi2329.
GeneCardsiGC01P171283.
HGNCiHGNC:3772. FMO4.
HPAiHPA049100.
MIMi136131. gene.
neXtProtiNX_P31512.
PharmGKBiPA28188.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2072.
GeneTreeiENSGT00760000119232.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiP31512.
KOiK00485.
OMAiCKIPPSQ.
OrthoDBiEOG7GXPB6.
PhylomeDBiP31512.
TreeFamiTF105285.

Miscellaneous databases

ChiTaRSiFMO4. human.
GeneWikiiFMO4.
GenomeRNAii2329.
NextBioi9453.
PROiP31512.
SOURCEiSearch...

Gene expression databases

BgeeiP31512.
CleanExiHS_FMO2.
HS_FMO4.
GenevestigatoriP31512.

Family and domain databases

InterProiIPR012143. DiMe-aniline_mOase.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002256. Flavin_mOase_4.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01124. FMOXYGENASE4.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family."
    Dolphin C.T., Shephard E.A., Povey S., Smith R.L., Phillips I.R.
    Biochem. J. 287:261-267(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. NIEHS SNPs program
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-323; SER-372; LEU-536 AND ARG-544.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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.
    , 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. 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].
    Tissue: Skin.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "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 THR-37; ALA-323 AND GLN-339.

Entry informationi

Entry nameiFMO4_HUMAN
AccessioniPrimary (citable) accession number: P31512
Secondary accession number(s): Q53XR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 139 of the entry and version 3 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

Caution

Was originally termed FMO2.1 Publication

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.