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P27338

- AOFB_HUMAN

UniProt

P27338 - AOFB_HUMAN

Protein

Amine oxidase [flavin-containing] B

Gene

MAOB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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.

    Catalytic activityi

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

    Cofactori

    FAD.

    Sites

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

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: Ensembl
    3. primary amine oxidase activity Source: Reactome

    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
    10. small molecule metabolic process Source: Reactome
    11. substantia nigra development Source: UniProt
    12. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00966-MONOMER.
    BRENDAi1.4.3.4. 2681.
    ReactomeiREACT_416. Monoamines are oxidized to aldehydes by MAOA and MAOB, producing NH3 and H2O2.
    SABIO-RKP27338.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:6834. MAOB.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of membrane Source: UniProtKB-KW
    3. mitochondrial envelope Source: ProtInc
    4. mitochondrial inner membrane Source: Ensembl
    5. mitochondrial outer membrane Source: Reactome
    6. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 51C → S: No loss of activity. 1 Publication
    Mutagenesisi156 – 1561C → S: Complete loss of activity. 1 Publication
    Mutagenesisi158 – 1581T → A: Dramatic loss of activity. 1 Publication
    Mutagenesisi172 – 1721C → S: No loss of activity. 1 Publication
    Mutagenesisi192 – 1921C → S: No loss of activity. 1 Publication
    Mutagenesisi199 – 1991I → F: Alters specificity towards synthetic inhibitors.
    Mutagenesisi297 – 2971C → S: No loss of activity. 1 Publication
    Mutagenesisi312 – 3121C → S: No loss of activity. 1 Publication
    Mutagenesisi365 – 3651C → S: Complete loss of activity. 1 Publication
    Mutagenesisi382 – 3821H → R: Significant loss of activity. 1 Publication
    Mutagenesisi386 – 3861K → M: No loss of activity. 1 Publication
    Mutagenesisi389 – 3891C → A: Complete loss of activity. 2 Publications
    Mutagenesisi389 – 3891C → S: No loss of activity. 2 Publications
    Mutagenesisi394 – 3941S → A: No loss of activity. 1 Publication
    Mutagenesisi397 – 3971C → S: Complete loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA237.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 520519Amine oxidase [flavin-containing] BPRO_0000099859Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei52 – 521N6-acetyllysineBy similarity
    Modified residuei397 – 3971S-8alpha-FAD cysteine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP27338.
    PaxDbiP27338.
    PRIDEiP27338.

    PTM databases

    PhosphoSiteiP27338.

    Expressioni

    Gene expression databases

    ArrayExpressiP27338.
    BgeeiP27338.
    CleanExiHS_MAOB.
    GenevestigatoriP27338.

    Organism-specific databases

    HPAiCAB037200.
    HPA002328.

    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

    BioGridi110302. 4 interactions.
    IntActiP27338. 3 interactions.
    MINTiMINT-3010688.
    STRINGi9606.ENSP00000367309.

    Structurei

    Secondary structure

    1
    520
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105
    Helixi14 – 2512
    Beta strandi30 – 334
    Beta strandi35 – 406
    Beta strandi45 – 484
    Turni49 – 513
    Beta strandi54 – 574
    Helixi66 – 749
    Beta strandi79 – 813
    Beta strandi85 – 928
    Beta strandi95 – 995
    Beta strandi101 – 1033
    Helixi109 – 12618
    Helixi134 – 1363
    Helixi140 – 1445
    Beta strandi145 – 1473
    Helixi148 – 1558
    Helixi159 – 17315
    Turni177 – 1793
    Helixi182 – 1909
    Turni191 – 1933
    Helixi195 – 1995
    Beta strandi207 – 2104
    Helixi215 – 22511
    Helixi226 – 2283
    Beta strandi229 – 2324
    Beta strandi235 – 2395
    Beta strandi241 – 2499
    Beta strandi254 – 2629
    Helixi266 – 2716
    Beta strandi272 – 2765
    Helixi280 – 2856
    Beta strandi294 – 3007
    Helixi305 – 3095
    Beta strandi311 – 3177
    Beta strandi319 – 3213
    Beta strandi325 – 3295
    Beta strandi339 – 3457
    Helixi347 – 3526
    Helixi357 – 37216
    Helixi375 – 3784
    Beta strandi381 – 3877
    Helixi388 – 3903
    Turni392 – 3943
    Beta strandi396 – 3983
    Helixi406 – 4105
    Helixi411 – 4133
    Beta strandi421 – 4233
    Helixi426 – 4283
    Beta strandi430 – 4323
    Helixi436 – 45318
    Helixi459 – 4613
    Beta strandi470 – 4723
    Helixi481 – 4855
    Helixi489 – 50012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GOSX-ray3.00A/B2-520[»]
    1H8Rmodel-A5-459[»]
    1OJ9X-ray2.30A/B2-520[»]
    1OJAX-ray1.70A/B2-520[»]
    1OJCX-ray2.40A/B2-520[»]
    1OJDX-ray3.10A/B/C/D/E/F/G/H/I/L2-520[»]
    1S2QX-ray2.07A/B1-520[»]
    1S2YX-ray2.12A/B1-520[»]
    1S3BX-ray1.65A/B1-520[»]
    1S3EX-ray1.60A/B1-520[»]
    2BK3X-ray1.80A/B2-520[»]
    2BK4X-ray1.90A/B2-520[»]
    2BK5X-ray1.83A/B1-520[»]
    2BYBX-ray2.20A/B2-520[»]
    2C64X-ray2.20A/B2-520[»]
    2C65X-ray1.70A/B2-520[»]
    2C66X-ray2.50A/B2-520[»]
    2C67X-ray1.70A/B2-520[»]
    2C70X-ray2.06A/B2-520[»]
    2C72X-ray2.00A/B2-520[»]
    2C73X-ray2.20A/B2-520[»]
    2C75X-ray1.70A/B2-520[»]
    2C76X-ray1.70A/B2-520[»]
    2V5ZX-ray1.60A/B2-520[»]
    2V60X-ray2.00A/B2-520[»]
    2V61X-ray1.70A/B2-520[»]
    2VRLX-ray2.40A/B1-520[»]
    2VRMX-ray2.30A/B1-520[»]
    2VZ2X-ray2.30A/B1-520[»]
    2XCGX-ray1.90A/B1-520[»]
    2XFNX-ray1.60A/B1-520[»]
    2XFOX-ray2.10A/B1-520[»]
    2XFPX-ray1.66A/B1-520[»]
    2XFQX-ray2.20A/B1-520[»]
    2XFUX-ray2.20A/B2-520[»]
    3PO7X-ray1.80A/B1-520[»]
    3ZYXX-ray2.20A/B2-520[»]
    4A79X-ray1.89A/B1-520[»]
    4A7AX-ray1.70A/B1-520[»]
    4CRTX-ray1.80A/B1-520[»]
    ProteinModelPortaliP27338.
    SMRiP27338. Positions 3-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27338.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 489488CytoplasmicAdd
    BLAST
    Topological domaini517 – 5204Mitochondrial intermembrane

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei490 – 51627Helical; Anchor for type IV membrane proteinAdd
    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.
    HOGENOMiHOG000221615.
    HOVERGENiHBG004255.
    InParanoidiP27338.
    KOiK00274.
    OMAiWDKMSMQ.
    OrthoDBiEOG7K6PTP.
    PhylomeDBiP27338.
    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.

    P27338-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNKCDVVVV GGGISGMAAA KLLHDSGLNV VVLEARDRVG GRTYTLRNQK    50
    VKYVDLGGSY VGPTQNRILR LAKELGLETY KVNEVERLIH HVKGKSYPFR 100
    GPFPPVWNPI TYLDHNNFWR TMDDMGREIP SDAPWKAPLA EEWDNMTMKE 150
    LLDKLCWTES AKQLATLFVN LCVTAETHEV SALWFLWYVK QCGGTTRIIS 200
    TTNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIYIDQ TRENVLVETL 250
    NHEMYEAKYV ISAIPPTLGM KIHFNPPLPM MRNQMITRVP LGSVIKCIVY 300
    YKEPFWRKKD YCGTMIIDGE EAPVAYTLDD TKPEGNYAAI MGFILAHKAR 350
    KLARLTKEER LKKLCELYAK VLGSLEALEP VHYEEKNWCE EQYSGGCYTT 400
    YFPPGILTQY GRVLRQPVDR IYFAGTETAT HWSGYMEGAV EAGERAAREI 450
    LHAMGKIPED EIWQSEPESV DVPAQPITTT FLERHLPSVP GLLRLIGLTT 500
    IFSATALGFL AHKRGLLVRV 520
    Length:520
    Mass (Da):58,763
    Last modified:January 23, 2007 - v3
    Checksum:i358D1025F5BCA604
    GO

    Mass spectrometryi

    Molecular mass is 59474±14.0 Da from positions 2 - 520. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S62734 mRNA. Translation: AAB27229.1.
    M69135 Genomic DNA. Translation: AAA59551.1.
    AK312679 mRNA. Translation: BAG35560.1.
    M69177 mRNA. Translation: AAA59550.1.
    M89637 Genomic DNA. Translation: AAB46386.1.
    AL008709 Genomic DNA. No translation available.
    AL020990 Genomic DNA. No translation available.
    Z95125 Genomic DNA. No translation available.
    CH471141 Genomic DNA. Translation: EAW59378.1.
    CH471141 Genomic DNA. Translation: EAW59380.1.
    CCDSiCCDS14261.1.
    PIRiJH0817.
    RefSeqiNP_000889.3. NM_000898.4.
    UniGeneiHs.654473.

    Genome annotation databases

    EnsembliENST00000378069; ENSP00000367309; ENSG00000069535.
    GeneIDi4129.
    KEGGihsa:4129.
    UCSCiuc004dfz.4. human.

    Polymorphism databases

    DMDMi113980.

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Wikipedia

    Monoamine oxidase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S62734 mRNA. Translation: AAB27229.1 .
    M69135 Genomic DNA. Translation: AAA59551.1 .
    AK312679 mRNA. Translation: BAG35560.1 .
    M69177 mRNA. Translation: AAA59550.1 .
    M89637 Genomic DNA. Translation: AAB46386.1 .
    AL008709 Genomic DNA. No translation available.
    AL020990 Genomic DNA. No translation available.
    Z95125 Genomic DNA. No translation available.
    CH471141 Genomic DNA. Translation: EAW59378.1 .
    CH471141 Genomic DNA. Translation: EAW59380.1 .
    CCDSi CCDS14261.1.
    PIRi JH0817.
    RefSeqi NP_000889.3. NM_000898.4.
    UniGenei Hs.654473.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GOS X-ray 3.00 A/B 2-520 [» ]
    1H8R model - A 5-459 [» ]
    1OJ9 X-ray 2.30 A/B 2-520 [» ]
    1OJA X-ray 1.70 A/B 2-520 [» ]
    1OJC X-ray 2.40 A/B 2-520 [» ]
    1OJD X-ray 3.10 A/B/C/D/E/F/G/H/I/L 2-520 [» ]
    1S2Q X-ray 2.07 A/B 1-520 [» ]
    1S2Y X-ray 2.12 A/B 1-520 [» ]
    1S3B X-ray 1.65 A/B 1-520 [» ]
    1S3E X-ray 1.60 A/B 1-520 [» ]
    2BK3 X-ray 1.80 A/B 2-520 [» ]
    2BK4 X-ray 1.90 A/B 2-520 [» ]
    2BK5 X-ray 1.83 A/B 1-520 [» ]
    2BYB X-ray 2.20 A/B 2-520 [» ]
    2C64 X-ray 2.20 A/B 2-520 [» ]
    2C65 X-ray 1.70 A/B 2-520 [» ]
    2C66 X-ray 2.50 A/B 2-520 [» ]
    2C67 X-ray 1.70 A/B 2-520 [» ]
    2C70 X-ray 2.06 A/B 2-520 [» ]
    2C72 X-ray 2.00 A/B 2-520 [» ]
    2C73 X-ray 2.20 A/B 2-520 [» ]
    2C75 X-ray 1.70 A/B 2-520 [» ]
    2C76 X-ray 1.70 A/B 2-520 [» ]
    2V5Z X-ray 1.60 A/B 2-520 [» ]
    2V60 X-ray 2.00 A/B 2-520 [» ]
    2V61 X-ray 1.70 A/B 2-520 [» ]
    2VRL X-ray 2.40 A/B 1-520 [» ]
    2VRM X-ray 2.30 A/B 1-520 [» ]
    2VZ2 X-ray 2.30 A/B 1-520 [» ]
    2XCG X-ray 1.90 A/B 1-520 [» ]
    2XFN X-ray 1.60 A/B 1-520 [» ]
    2XFO X-ray 2.10 A/B 1-520 [» ]
    2XFP X-ray 1.66 A/B 1-520 [» ]
    2XFQ X-ray 2.20 A/B 1-520 [» ]
    2XFU X-ray 2.20 A/B 2-520 [» ]
    3PO7 X-ray 1.80 A/B 1-520 [» ]
    3ZYX X-ray 2.20 A/B 2-520 [» ]
    4A79 X-ray 1.89 A/B 1-520 [» ]
    4A7A X-ray 1.70 A/B 1-520 [» ]
    4CRT X-ray 1.80 A/B 1-520 [» ]
    ProteinModelPortali P27338.
    SMRi P27338. Positions 3-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110302. 4 interactions.
    IntActi P27338. 3 interactions.
    MINTi MINT-3010688.
    STRINGi 9606.ENSP00000367309.

    Chemistry

    BindingDBi P27338.
    ChEMBLi CHEMBL2039.
    DrugBanki DB00915. Amantadine.
    DB00182. Amphetamine.
    DB00988. Dopamine.
    DB01363. Ephedra.
    DB03147. Flavin adenine dinucleotide.
    DB00614. Furazolidone.
    DB01247. Isocarboxazid.
    DB00601. Linezolid.
    DB01577. Methamphetamine.
    DB01171. Moclobemide.
    DB08804. Nandrolone decanoate.
    DB00184. Nicotine.
    DB01626. Pargyline.
    DB00780. Phenelzine.
    DB00191. Phentermine.
    DB00721. Procaine.
    DB01367. Rasagiline.
    DB01037. Selegiline.
    DB01104. Sertraline.
    DB00752. Tranylcypromine.
    DB00909. Zonisamide.
    GuidetoPHARMACOLOGYi 2490.

    PTM databases

    PhosphoSitei P27338.

    Polymorphism databases

    DMDMi 113980.

    Proteomic databases

    MaxQBi P27338.
    PaxDbi P27338.
    PRIDEi P27338.

    Protocols and materials databases

    DNASUi 4129.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378069 ; ENSP00000367309 ; ENSG00000069535 .
    GeneIDi 4129.
    KEGGi hsa:4129.
    UCSCi uc004dfz.4. human.

    Organism-specific databases

    CTDi 4129.
    GeneCardsi GC0XM043625.
    HGNCi HGNC:6834. MAOB.
    HPAi CAB037200.
    HPA002328.
    MIMi 309860. gene.
    neXtProti NX_P27338.
    PharmGKBi PA237.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1231.
    HOGENOMi HOG000221615.
    HOVERGENi HBG004255.
    InParanoidi P27338.
    KOi K00274.
    OMAi WDKMSMQ.
    OrthoDBi EOG7K6PTP.
    PhylomeDBi P27338.
    TreeFami TF313314.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00966-MONOMER.
    BRENDAi 1.4.3.4. 2681.
    Reactomei REACT_416. Monoamines are oxidized to aldehydes by MAOA and MAOB, producing NH3 and H2O2.
    SABIO-RK P27338.

    Miscellaneous databases

    ChiTaRSi MAOB. human.
    EvolutionaryTracei P27338.
    GeneWikii Monoamine_oxidase_B.
    GenomeRNAii 4129.
    NextBioi 16210.
    PROi P27338.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27338.
    Bgeei P27338.
    CleanExi HS_MAOB.
    Genevestigatori P27338.

    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. "Human monoamine oxidase A and B genes exhibit identical exon-intron organization."
      Grimsby J., Chen K., Wang L.J., Lan N.C., Shih J.C.
      Proc. Natl. Acad. Sci. U.S.A. 88:3637-3641(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties."
      Bach A.W.J., Lan N.C., Johnson D.L., Abell C.W., Bembenek M.E., Kwan S.W., Seeburg P.H., Shih J.C.
      Proc. Natl. Acad. Sci. U.S.A. 85:4934-4938(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical."
      Chen K., Wu H.F., Shih J.C.
      J. Neurochem. 61:187-190(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Promoter organization and activity of human monoamine oxidase (MAO) A and B genes."
      Zhu Q.S., Grimsby J.S., Chen K., Shih J.C.
      J. Neurosci. 12:4437-4446(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
    8. "High-level expression of human liver monoamine oxidase B in Pichia pastoris."
      Newton-Vinson P., Hubalek F., Edmondson D.E.
      Protein Expr. Purif. 20:334-345(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, MASS SPECTROMETRY.
    9. "Investigation on the structure of the active site of monoamine oxidase-B by affinity labeling with the selective inhibitor lazabemide and by site-directed mutagenesis."
      Cesura A.M., Gottowik J., Lahm H.-W., Lang G., Imhof R., Malherbe P., Roethlisberger U., Da Prada M.
      Eur. J. Biochem. 236:996-1002(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 371-391, MUTAGENESIS OF THR-158; HIS-382; LYS-386; CYS-389 AND SER-394.
    10. "Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines."
      Wu H.F., Chen K., Shih J.C.
      Mol. Pharmacol. 43:888-893(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-5; CYS-156; CYS-172; CYS-192; CYS-297; CYS-312; CYS-365; CYS-389 AND CYS-397.
    11. "Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders."
      Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., Mattevi A.
      Nat. Struct. Biol. 9:22-26(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    12. "Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures."
      Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., Mattevi A.
      Proc. Natl. Acad. Sci. U.S.A. 100:9750-9755(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
    13. "Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class."
      Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E., Mattevi A.
      J. Med. Chem. 47:1767-1774(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
    14. "Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors."
      Hubalek F., Binda C., Khalil A., Li M., Mattevi A., Castagnoli N., Edmondson D.E.
      J. Biol. Chem. 280:15761-15766(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT PHE-199 IN COMPLEXES WITH INHIBITORS.
    15. "Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis."
      Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E., Mattevi A.
      J. Med. Chem. 48:8148-8154(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.

    Entry informationi

    Entry nameiAOFB_HUMAN
    AccessioniPrimary (citable) accession number: P27338
    Secondary accession number(s): B2R6R3, D3DWC3, Q7Z6S2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 158 of the entry and version 3 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3