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HUMAN:FMO3

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) FMO3
Protein Name(s) Dimethylaniline monooxygenase [N-oxide-forming] 3

Dimethylaniline oxidase 3 FMO II FMO form 2 Hepatic flavin-containing monooxygenase 3 FMO 3 Trimethylamine monooxygenase

External Links
UniProt P31513
EMBL M83772
Z47552
U39967
U39961
U39962
U39963
U39964
U39965
U39966
AY895830
AK313197
AL021026
CH471067
BC032016
CCDS CCDS1292.1
PIR A38228
S62367
RefSeq NP_001002294.1
NP_008825.4
UniGene Hs.445350
ProteinModelPortal P31513
SMR P31513
STRING 9606.ENSP00000356729
DrugBank DB00918
DB00501
DB00363
DB00250
DB01254
DB00334
DB00675
DB05294
DB00582
PhosphoSite P31513
DMDM 6166183
PaxDb P31513
PRIDE P31513
DNASU 2328
Ensembl ENST00000367755
GeneID 2328
KEGG hsa:2328
UCSC uc001ghh.3
CTD 2328
GeneCards GC01P171060
GeneReviews FMO3
HGNC HGNC:3771
HPA HPA008065
HPA013750
MIM 136132
602079
neXtProt NX_P31513
Orphanet 35056
PharmGKB PA166
eggNOG COG2072
GeneTree ENSGT00760000119232
HOGENOM HOG000076537
HOVERGEN HBG002037
InParanoid P31513
KO K00485
OMA FMHNSKL
OrthoDB EOG7GXPB6
PhylomeDB P31513
TreeFam TF105285
BioCyc MetaCyc:HS00223-MONOMER
Reactome REACT_13653
SABIO-RK P31513
GeneWiki Flavin_containing_monooxygenase_3
GenomeRNAi 2328
NextBio 9447
PRO PR:P31513
Proteomes UP000005640
Bgee P31513
CleanEx HS_FMO3
ExpressionAtlas P31513
Genevestigator P31513
GO GO:0005789
GO:0016021
GO:0043231
GO:0016597
GO:0050660
GO:0004499
GO:0050661
GO:0034899
GO:0017144
GO:0044281
GO:0006805
InterPro IPR012143
IPR000960
IPR020946
IPR002255
Pfam PF00743
PIRSF PIRSF000332
PRINTS PR00370
PR01123

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0004497

monooxygenase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1310002
MGI:MGI:1916776
PANTHER:PTN000545571
RGD:2622
UniProtKB:Q01740

F

Seeded From UniProt

complete

enables

GO:0004499

N,N-dimethylaniline monooxygenase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000960
InterPro:IPR002255
InterPro:IPR020946

F

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000960
InterPro:IPR020946

F

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000960
InterPro:IPR020946

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000960
InterPro:IPR002255
InterPro:IPR020946

P

Seeded From UniProt

complete

enables

GO:0004499

N,N-dimethylaniline monooxygenase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.14.13.8

F

Seeded From UniProt

complete

enables

GO:0034899

trimethylamine monooxygenase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.14.13.148

F

Seeded From UniProt

complete

part_of

GO:0043231

intracellular membrane-bounded organelle

PMID:9207220[2]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

GO:0055114

oxidation-reduction process

PMID:20454663[3]

ECO:0000314

P

Figure 2. Alignment of the amino acid sequences of FMOs of various acrtiid species

complete
CACAO 10773

involved_in

GO:0006805

xenobiotic metabolic process

Reactome:R-HSA-211945

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

Reactome:R-HSA-139970

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0043231

intracellular membrane-bounded organelle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0492

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0004497

monooxygenase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0503

F

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0256

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0031090

organelle membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0165

C

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0097

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. Chung, WG & Cha, YN (1997) Oxidation of caffeine to theobromine and theophylline is catalyzed primarily by flavin-containing monooxygenase in liver microsomes. Biochem. Biophys. Res. Commun. 235 685-8 PubMed GONUTS page
  3. Sehlmeyer, S et al. (2010) Flavin-dependent monooxygenases as a detoxification mechanism in insects: new insights from the arctiids (lepidoptera). PLoS ONE 5 e10435 PubMed GONUTS page