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Protein

Putative dimethylaniline monooxygenase [N-oxide-forming] 6

Gene

FMO6P

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein uncertaini

Functioni

It is probable that this protein is only produced in very small quantity or not at all as the gene coding for it seems to be unable to produce full length transcripts.

Catalytic activityi

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

Cofactori

FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146FADSequence analysis
Nucleotide bindingi191 – 1966NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Putative dimethylaniline monooxygenase [N-oxide-forming] 6 (EC:1.14.13.8)
Alternative name(s):
Dimethylaniline oxidase 6
Flavin-containing monooxygenase 6
Short name:
FMO 6
Gene namesi
Name:FMO6P
Synonyms:FMO6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:24024. FMO6P.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei518 – 53821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671753.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539Putative dimethylaniline monooxygenase [N-oxide-forming] 6PRO_0000147669Add
BLAST

Proteomic databases

EPDiO60774.
PaxDbiO60774.
PeptideAtlasiO60774.
PRIDEiO60774.

PTM databases

iPTMnetiO60774.
PhosphoSiteiO60774.

Expressioni

Gene expression databases

BgeeiO60774.

Structurei

3D structure databases

ProteinModelPortaliO60774.
SMRiO60774. Positions 3-214, 310-336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FMO family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiO60774.
PhylomeDBiO60774.
TreeFamiTF105285.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 2 hits.
InterProiIPR012143. DiMe-aniline_mOase.
IPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01123. FMOXYGENASE3.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

O60774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRVGIIGA GVSGLAAIWC CLEEGLEPTC FERSDDVGGL WKFSDHTEEG
60 70 80 90 100
RASIYQSVFT NSSKEMMCFP DFPYPDDYPN YIHHSKLQEY IKTYAQKKDL
110 120 130 140 150
LRYIQFETLV SGIKKCPSFL VTGQWVVVTE KDGKQESTIF DAVMICSGHH
160 170 180 190 200
VYPNLPTDSF PGLDQFRGNY LHSRDYKNPE AFKGKRVLVI GLGNSGSDIA
210 220 230 240 250
VELSRLATQV IISTRSASWV MSRVWDDGYP WDMMYVTRFA SFLRNVLPSF
260 270 280 290 300
ISDWLYVQKM NTWFKHENYG LMPLNGSLRK EPVFNDELPS RILCGTLSIK
310 320 330 340 350
PSVKEFTETS AVFEDGTMFE AIDSVIFATG YDYSYPFLDE TIMKSRNNEV
360 370 380 390 400
TLFKGIFPPL MEKPTLAVIG LVQSLGAAIP TADLQAWWAA KVFANSCTLP
410 420 430 440 450
TTNEMMDDTD EKMGKKLKCM FSSFFMFGQS QTLQTDYITY VDELGSFIGA
460 470 480 490 500
KPNIPWLFLT DPRLALEVYF GPCSPYQFRL MGPGKWDGAR NAILTQWNRT
510 520 530
VKPTRTRVVS EVQRPHPFYN LLKMLSFPLL LLAVTLTFY
Length:539
Mass (Da):61,291
Last modified:August 1, 1998 - v1
Checksum:i8E0D15CA4F79FF0C
GO

Polymorphismi

There are two alleles; one major, FMO6X105 (truncated form) and one minor, FMO6Q105, (shown here) (full-length form similar to the protein found in other mammals) (PubMed:12527699). A nonsense mutation transforms the Gln-105 into a premature stop codon (PubMed:12527699). The truncated protein is catalytically inactive (PubMed:12527699).1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti127 – 1271V → I.1 Publication
Corresponds to variant rs61731844 [ dbSNP | Ensembl ].
VAR_015371
Natural varianti257 – 2571V → I.1 Publication
Corresponds to variant rs2272797 [ dbSNP | Ensembl ].
VAR_015372

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021026 Genomic DNA. No translation available.

Genome annotation databases

UCSCiuc057ngh.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021026 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliO60774.
SMRiO60774. Positions 3-214, 310-336.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiO60774.
PhosphoSiteiO60774.

Proteomic databases

EPDiO60774.
PaxDbiO60774.
PeptideAtlasiO60774.
PRIDEiO60774.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc057ngh.1. human.

Organism-specific databases

GeneCardsiFMO6P.
HGNCiHGNC:24024. FMO6P.
neXtProtiNX_O60774.
PharmGKBiPA142671753.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1399. Eukaryota.
COG2072. LUCA.
HOGENOMiHOG000076537.
HOVERGENiHBG002037.
InParanoidiO60774.
PhylomeDBiO60774.
TreeFamiTF105285.

Gene expression databases

BgeeiO60774.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 2 hits.
InterProiIPR012143. DiMe-aniline_mOase.
IPR023753. FAD/NAD-binding_dom.
IPR000960. Flavin_mOase.
IPR020946. Flavin_mOase-like.
IPR002255. Flavin_mOase_3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
PIRSFiPIRSF000332. FMO. 1 hit.
PRINTSiPR00370. FMOXYGENASE.
PR01123. FMOXYGENASE3.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase."
    Hines R.N., Hopp K.A., Franco J., Saeian K., Begun F.P.
    Mol. Pharmacol. 62:320-325(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANALYSIS OF SPLICE VARIANTS.
  3. "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 ILE-127 AND ILE-257, POLYMORPHISM IN POSITION 105.

Entry informationi

Entry nameiFMO6_HUMAN
AccessioniPrimary (citable) accession number: O60774
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 123 of the entry and version 1 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

Could be the product of a pseudogene.Curated

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. SIMILARITY comments
    Index of protein domains and families

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 one 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.