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Q8BW75

- AOFB_MOUSE

UniProt

Q8BW75 - AOFB_MOUSE

Protein

Amine oxidase [flavin-containing] B

Gene

Maob

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine By similarity.By similarity

    Catalytic activityi

    RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.

    Cofactori

    FAD.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei156 – 1561Important for catalytic activityBy similarity
    Sitei365 – 3651Important for catalytic activityBy similarity
    Sitei382 – 3821Important for catalytic activityBy similarity

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: Ensembl
    2. oxidoreductase activity Source: UniProtKB-KW

    GO - Biological processi

    1. negative regulation of serotonin secretion Source: Ensembl
    2. positive regulation of dopamine metabolic process Source: Ensembl
    3. response to aluminum ion Source: Ensembl
    4. response to corticosterone Source: Ensembl
    5. response to drug Source: Ensembl
    6. response to ethanol Source: Ensembl
    7. response to lipopolysaccharide Source: Ensembl
    8. response to selenium ion Source: Ensembl
    9. response to toxic substance Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BRENDAi1.4.3.4. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amine oxidase [flavin-containing] B (EC:1.4.3.4)
    Alternative name(s):
    Monoamine oxidase type B
    Short name:
    MAO-B
    Gene namesi
    Name:Maob
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:96916. Maob.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: MGI
    3. mitochondrial outer membrane Source: UniProtKB-SubCell
    4. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 520519Amine oxidase [flavin-containing] BPRO_0000099860Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei52 – 521N6-acetyllysine1 Publication
    Modified residuei248 – 2481N6-acetyllysine1 Publication
    Modified residuei397 – 3971S-8alpha-FAD cysteineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8BW75.
    PaxDbiQ8BW75.
    PRIDEiQ8BW75.

    PTM databases

    PhosphoSiteiQ8BW75.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BW75.
    BgeeiQ8BW75.
    CleanExiMM_MAOB.
    GenevestigatoriQ8BW75.

    Interactioni

    Subunit structurei

    Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8BW75. 2 interactions.
    MINTiMINT-1861050.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BW75.
    SMRiQ8BW75. Positions 3-495.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 489488CytoplasmicBy similarityAdd
    BLAST
    Topological domaini517 – 5204Mitochondrial intermembraneBy similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei490 – 51627Helical; Anchor for type IV membrane proteinBy similarityAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi36 – 5217Arg/Lys-rich (basic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the flavin monoamine oxidase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1231.
    GeneTreeiENSGT00730000110903.
    HOGENOMiHOG000221615.
    HOVERGENiHBG004255.
    InParanoidiQ14CG9.
    KOiK00274.
    OMAiIPPILGM.
    OrthoDBiEOG7K6PTP.
    TreeFamiTF313314.

    Family and domain databases

    InterProiIPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8BW75-1 [UniParc]FASTAAdd to Basket

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    MSNKSDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN    50
    VKYVDLGGSY VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR 100
    GPFPPVWNPI TYLDNNNLWR TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE 150
    LLDKICWTKS TKQIATLFVN LCVTAETHEV SALWFLWYVK QCGGTTRIIS 200
    TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ TGENVIVKTL 250
    NHEIYEAKYV ISAIPPALGM KIHYSPPLPM LRNQLISRVP LGSVIKCMVY 300
    YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGTYAAI MGFILAHKAR 350
    KLVRLTKEER LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTT 400
    YFPPGILTQY GRVLRQPVGK IFFAGTETAS HWSGYMEGAV EAGERAAREI 450
    LHAIGKIPED EIWQPEPESL DVPARPITST FLERHLPSVP GLLKLFGLTT 500
    ILSATALGFL AHKRGLFVHF 520
    Length:520
    Mass (Da):58,558
    Last modified:July 27, 2011 - v4
    Checksum:iA5982EBBF5C4BD62
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti408 – 4081T → S in BAC35634. (PubMed:16141072)Curated
    Sequence conflicti482 – 4821L → M in BAC27571. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK031833 mRNA. Translation: BAC27571.1.
    AK054050 mRNA. Translation: BAC35634.1.
    AL732321, AL831729 Genomic DNA. Translation: CAM16088.1.
    AL831729, AL732321 Genomic DNA. Translation: CAM26633.1.
    CH466584 Genomic DNA. Translation: EDL35718.1.
    BC113182 mRNA. Translation: AAI13183.1.
    BC113788 mRNA. Translation: AAI13789.1.
    CCDSiCCDS40882.1.
    RefSeqiNP_766366.2. NM_172778.2.
    UniGeneiMm.241656.

    Genome annotation databases

    EnsembliENSMUST00000040820; ENSMUSP00000040550; ENSMUSG00000040147.
    GeneIDi109731.
    KEGGimmu:109731.
    UCSCiuc009ssb.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK031833 mRNA. Translation: BAC27571.1 .
    AK054050 mRNA. Translation: BAC35634.1 .
    AL732321 , AL831729 Genomic DNA. Translation: CAM16088.1 .
    AL831729 , AL732321 Genomic DNA. Translation: CAM26633.1 .
    CH466584 Genomic DNA. Translation: EDL35718.1 .
    BC113182 mRNA. Translation: AAI13183.1 .
    BC113788 mRNA. Translation: AAI13789.1 .
    CCDSi CCDS40882.1.
    RefSeqi NP_766366.2. NM_172778.2.
    UniGenei Mm.241656.

    3D structure databases

    ProteinModelPortali Q8BW75.
    SMRi Q8BW75. Positions 3-495.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BW75. 2 interactions.
    MINTi MINT-1861050.

    Chemistry

    BindingDBi Q8BW75.
    ChEMBLi CHEMBL2111442.

    PTM databases

    PhosphoSitei Q8BW75.

    Proteomic databases

    MaxQBi Q8BW75.
    PaxDbi Q8BW75.
    PRIDEi Q8BW75.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040820 ; ENSMUSP00000040550 ; ENSMUSG00000040147 .
    GeneIDi 109731.
    KEGGi mmu:109731.
    UCSCi uc009ssb.2. mouse.

    Organism-specific databases

    CTDi 4129.
    MGIi MGI:96916. Maob.

    Phylogenomic databases

    eggNOGi COG1231.
    GeneTreei ENSGT00730000110903.
    HOGENOMi HOG000221615.
    HOVERGENi HBG004255.
    InParanoidi Q14CG9.
    KOi K00274.
    OMAi IPPILGM.
    OrthoDBi EOG7K6PTP.
    TreeFami TF313314.

    Enzyme and pathway databases

    BRENDAi 1.4.3.4. 3474.

    Miscellaneous databases

    NextBioi 362651.
    PROi Q8BW75.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BW75.
    Bgeei Q8BW75.
    CleanExi MM_MAOB.
    Genevestigatori Q8BW75.

    Family and domain databases

    InterProi IPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00757. AMINEOXDASEF.
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Medulla oblongata and Oviduct.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiAOFB_MOUSE
    AccessioniPrimary (citable) accession number: Q8BW75
    Secondary accession number(s): Q14CG9, Q8C0B2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 93 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3