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UniProtKB/Swiss-Prot entry P49326


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FMO5_HUMAN
Primary accession number P49326
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 75)
Name and origin of the protein
Protein name Dimethylaniline monooxygenase [N-oxide-forming] 5
Synonyms EC 1.14.13.8
Hepatic flavin-containing monooxygenase 5
FMO 5
Dimethylaniline oxidase 5
Gene name
Name: FMO5
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1006/abbi.1995.1163; PubMed=7872795 [NCBI, ExPASy, EBI, Israel, Japan]
Overby L.H., Buckpitt A.R., Lawton M.P., Atta-Asafo-Adjei E., Schulze J., Philpot R.M.;
"Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog.";
Arch. Biochem. Biophys. 317:275-284(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver, and Placenta;
Dolphin C.T., Povey S., Shephard E.A., Smith R.L., Phillips I.R.;
"Cloning, primary sequence and chromosomal localisation of human flavin-containing monooxygenase 5 (FMO5).";
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-400 AND SER-506.
Livingston R.J., Rieder M.J., Rajkumar N., Downing T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
VARIANT LEU-457.
DOI=10.1124/dmd.31.2.187; PubMed=12527699 [NCBI, ExPASy, EBI, Israel, Japan]
Furnes B., Feng J., Sommer S.S., Schlenk D.;
"Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans.";
Drug Metab. Dispos. 31:187-193(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L37080; AAA67849.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z47553; CAA87633.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY902236; AAW69390.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356378; CAH72648.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S51131; S51131.
S71618; S71618.
RefSeq NP_001452.1; -.
UniGene Hs.642706
3D structure databases
ModBase P49326.
PTM databases
PhosphoSite P49326; -.
Polymorphism databases
NIEHS-SNPs FMO5.
Organism-specific databases
HGNC HGNC:3773; FMO5.
GenAtlas FMO5.
HPA HPA012373; -.
MIM 603957; gene. [NCBI / EBI]
PharmGKB PA28189; -.
GeneCards P49326.
Gene expression databases
ArrayExpress P49326; -.
CleanEx HS_FMO5; -.
GermOnline ENSG00000131781; Homo sapiens.
Ontologies
GO
GO:0005792; Cellular component: microsome (non-traceable author statement from UniProtKB).
GO:0004499; Molecular function: flavin-containing monooxygenase activity (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR012143; dManiline_mOase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000960; Flavin_mOase.
IPR002257; Flavin_mOase_5.
Graphical view of domain structure.
Pfam PF00743; FMO-like; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000332; FMO; 1.
PRINTS PR00368; FADPNR.
PR00370; FMOXYGENASE.
PR01125; FMOXYGENASE5.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS P49326.
Genome annotation databases
Ensembl ENSG00000131781; Homo sapiens. [Contig view]
GeneID 2330; -.
KEGG hsa:2330; -.
Phylogenomic databases
HOGENOM P49326; -.
HOVERGEN P49326; -.
Other
SOURCE FMO5; Homo sapiens.
ProtoNet P49326.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Methylation; Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Transmembrane.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   533  532     Dimethylaniline monooxygenase [N-oxide-forming] 5. PRO_0000147665
NP_BIND   10    15  6     FAD (Potential). 
NP_BIND   192   197  6     NADP (By similarity). 
MOD_RES   2     2        N-acetylthreonine (By similarity). 
MOD_RES   5     5        Omega-N-methylated arginine (By similarity). 
VARIANT   400   400  1     P -> A. VAR_022308 
VARIANT   457   457  1     P -> L. VAR_015370 
VARIANT   506   506  1     R -> S. VAR_022309 
CONFLICT   351   351        S -> P (in Ref. 2; CAA87633). 
Sequence information
Length: 533 AA [This is the length of the unprocessed precursor] Molecular weight: 60221 Da [This is the MW of the unprocessed precursor] CRC64: F9D9F092F1DD71DA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTKKRIAVIG GGVSGLSSIK CCVEEGLEPV CFERTDDIGG LWRFQENPEE GRASIYKSVI 

        70         80         90        100        110        120 
INTSKEMMCF SDYPIPDHYP NFMHNAQVLE YFRMYAKEFD LLKYIRFKTT VCSVKKQPDF 

       130        140        150        160        170        180 
ATSGQWEVVT ESEGKKEMNV FDGVMVCTGH HTNAHLPLES FPGIEKFKGQ YFHSRDYKNP 

       190        200        210        220        230        240 
EGFTGKRVII IGIGNSGGDL AVEISQTAKQ VFLSTRRGAW ILNRVGDYGY PADVLFSSRL 

       250        260        270        280        290        300 
THFIWKICGQ SLANKYLEKK INQRFDHEMF GLKPKHRALS QHPTLNDDLP NRIISGLVKV 

       310        320        330        340        350        360 
KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYSFDFPFLE DSVKVVKNKI SLYKKVFPPN 

       370        380        390        400        410        420 
LERPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKTLP SQSEMMAEIS KAQEEIDKRY 

       430        440        450        460        470        480 
VESQRHTIQG DYIDTMEELA DLVGVRPNLL SLAFTDPKLA LHLLLGPCTP IHYRVQGPGK 

       490        500        510        520        530 
WDGARKAILT TDDRIRKPLM TRVVERSSSM TSTMTIGKFM LALAFFAIII AYF 

P49326 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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