UniProt Accession

 FMO1_MOUSE; P50285 

Genbank Protein ID

 D16215; U87456; BC011229 

Genbank Nucleotide ID

 BAA03745.1; AAB47569.1; AAH11229.1 

Protein Name

 Dimethylaniline monooxygenase [N-oxide-forming] 1 

Protein Synonyms/Alias

 Dimethylaniline oxidase 1; Hepatic flavin-containing monooxygenase 1; FMO 1 

Gene Name

 Fmo1 

Gene Synonyms/Alias

 Fmo-1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
56	EGRASLYKSVVSNSS	ubiquitination	[1]
115	TKVCSITKRPDFAVS	ubiquitination	[1]
208	VEASHLAKKVFLSTT	ubiquitination	[1]
259	VSWLISKKMNSWFNH	ubiquitination	[1]
296	PGRIITGKVFIKPSI	ubiquitination	[1]
300	ITGKVFIKPSIKEVK	acetylation	[2]
300	ITGKVFIKPSIKEVK	ubiquitination	[1]
304	VFIKPSIKEVKENSV	acetylation	[2, 3]
304	VFIKPSIKEVKENSV	ubiquitination	[1]
307	KPSIKEVKENSVVFN	ubiquitination	[1]
480	FRLTGPGKWEGARKA	ubiquitination	[1]
486	GKWEGARKAILTQWD	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 

Functional Description

 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. 

Sequence Annotation

 NP_BIND 9 14 FAD (Potential).
 NP_BIND 191 196 NADP (Potential).  

Keyword

 Complete proteome; Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Reference proteome; Transmembrane. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 532 AA 

Protein Sequence

Gene Ontology

 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031227; C:intrinsic to endoplasmic reticulum membrane; IEA:InterPro.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:EC.
 GO:0050661; F:NADP binding; IEA:InterPro.
 GO:0070995; P:NADPH oxidation; IEA:Compara.
 GO:0006082; P:organic acid metabolic process; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
 GO:0006970; P:response to osmotic stress; IEA:Compara.
 GO:0009404; P:toxin metabolic process; IEA:Compara. 

Interpro

 IPR012143; DiMe-aniline_mOase.
 IPR000960; Flavin_mOase.
 IPR020946; Flavin_mOase-like.
 IPR002253; Flavin_mOase_1.
 IPR016040; NAD(P)-bd_dom. 

Pfam

 PF00743; FMO-like 

SMART

  

PROSITE

  

PRINTS

 PR00370; FMOXYGENASE.
 PR01121; FMOXYGENASE1.