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P21397

- AOFA_HUMAN

UniProt

P21397 - AOFA_HUMAN

Protein

Amine oxidase [flavin-containing] A

Gene

MAOA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      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. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.

    Catalytic activityi

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

    Cofactori

    FAD.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei335 – 3351Important for substrate specificityBy similarity
    Sitei374 – 3741Important for catalytic activity

    GO - Molecular functioni

    1. primary amine oxidase activity Source: Reactome

    GO - Biological processi

    1. cellular biogenic amine metabolic process Source: ProtInc
    2. dopamine catabolic process Source: Ensembl
    3. neurotransmitter biosynthetic process Source: Reactome
    4. neurotransmitter catabolic process Source: UniProtKB-KW
    5. neurotransmitter secretion Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. synaptic transmission Source: Reactome
    8. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Catecholamine metabolism, Neurotransmitter degradation

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01798-MONOMER.
    BRENDAi1.4.3.4. 2681.
    ReactomeiREACT_15418. Norepinephrine Neurotransmitter Release Cycle.
    REACT_15511. Enzymatic degradation of Dopamine by monoamine oxidase.
    REACT_15532. Metabolism of serotonin.
    REACT_15548. Enzymatic degradation of dopamine by COMT.
    REACT_416. Monoamines are oxidized to aldehydes by MAOA and MAOB, producing NH3 and H2O2.
    SABIO-RKP21397.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amine oxidase [flavin-containing] A (EC:1.4.3.4)
    Alternative name(s):
    Monoamine oxidase type A
    Short name:
    MAO-A
    Gene namesi
    Name:MAOA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:6833. MAOA.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial outer membrane Source: Reactome
    3. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Involvement in diseasei

    Brunner syndrome (BRUNS) [MIM:300615]: A form of X-linked non-dysmorphic mild mental retardation. Male patients are affected by borderline mental retardation and exhibit abnormal behavior, including disturbed regulation of impulsive aggression. Obligate female carriers have normal intelligence and behavior.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi165 – 1651C → S: No loss of activity. 1 Publication
    Mutagenesisi266 – 2661C → S: No loss of activity. 1 Publication
    Mutagenesisi306 – 3061C → S: No loss of activity. 1 Publication
    Mutagenesisi321 – 3211C → S: No loss of activity. 1 Publication
    Mutagenesisi323 – 3231C → S: No loss of activity. 1 Publication
    Mutagenesisi374 – 3741C → S: Complete loss of activity. 1 Publication
    Mutagenesisi398 – 3981C → S: No loss of activity. 1 Publication
    Mutagenesisi406 – 4061C → S: Complete loss of activity. 1 Publication

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi300615. phenotype.
    309850. gene+phenotype.
    Orphaneti3057. Monoamine oxidase A deficiency.
    PharmGKBiPA236.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 527527Amine oxidase [flavin-containing] APRO_0000099850Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei406 – 4061S-8alpha-FAD cysteine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP21397.
    PaxDbiP21397.
    PeptideAtlasiP21397.
    PRIDEiP21397.

    PTM databases

    PhosphoSiteiP21397.

    Expressioni

    Tissue specificityi

    Heart, liver, duodenum, blood vessels and kidney.

    Gene expression databases

    ArrayExpressiP21397.
    BgeeiP21397.
    CleanExiHS_MAOA.
    GenevestigatoriP21397.

    Organism-specific databases

    HPAiCAB009437.

    Interactioni

    Subunit structurei

    Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer.2 Publications

    Protein-protein interaction databases

    BioGridi110301. 2 interactions.
    IntActiP21397. 2 interactions.
    MINTiMINT-4054607.
    STRINGi9606.ENSP00000340684.

    Structurei

    Secondary structure

    1
    527
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 195
    Helixi23 – 3412
    Beta strandi39 – 424
    Beta strandi44 – 496
    Beta strandi54 – 574
    Turni58 – 603
    Beta strandi61 – 666
    Helixi75 – 839
    Beta strandi88 – 903
    Beta strandi94 – 1018
    Beta strandi104 – 1085
    Beta strandi110 – 1123
    Helixi118 – 13619
    Helixi143 – 1453
    Helixi149 – 1546
    Helixi157 – 1648
    Helixi168 – 18215
    Turni186 – 1883
    Helixi191 – 1999
    Turni200 – 2023
    Helixi204 – 2085
    Beta strandi211 – 2133
    Beta strandi216 – 2194
    Helixi224 – 23411
    Helixi235 – 2373
    Beta strandi238 – 2414
    Beta strandi244 – 2485
    Beta strandi250 – 2589
    Beta strandi263 – 2719
    Helixi275 – 2784
    Beta strandi281 – 2855
    Helixi289 – 2957
    Beta strandi303 – 3097
    Helixi314 – 3174
    Beta strandi320 – 3278
    Beta strandi334 – 3385
    Beta strandi348 – 3547
    Helixi355 – 3617
    Helixi366 – 38116
    Helixi385 – 3873
    Beta strandi390 – 3978
    Turni401 – 4033
    Beta strandi405 – 4073
    Helixi415 – 4184
    Helixi420 – 4223
    Beta strandi430 – 4323
    Helixi435 – 4373
    Beta strandi439 – 4413
    Helixi445 – 46218
    Beta strandi464 – 4663
    Helixi469 – 4713
    Beta strandi479 – 4813
    Helixi490 – 4945
    Helixi498 – 52023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H8Qmodel-A14-468[»]
    2BXRX-ray3.00A/B1-527[»]
    2BXSX-ray3.15A/B1-527[»]
    2Z5XX-ray2.20A12-524[»]
    2Z5YX-ray2.17A12-524[»]
    ProteinModelPortaliP21397.
    SMRiP21397. Positions 12-524.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21397.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 497497Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini519 – 5279Mitochondrial intermembrane1 Publication

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei498 – 51821Helical; Anchor for type IV membrane proteinAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni520 – 5223Interaction with membrane phospholipid headgroupsCurated

    Sequence similaritiesi

    Belongs to the flavin monoamine oxidase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1231.
    HOGENOMiHOG000221615.
    HOVERGENiHBG004255.
    InParanoidiP21397.
    KOiK00274.
    OMAiMEITHTF.
    OrthoDBiEOG7K6PTP.
    PhylomeDBiP21397.
    TreeFamiTF313314.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P21397-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MENQEKASIA GHMFDVVVIG GGISGLSAAK LLTEYGVSVL VLEARDRVGG    50
    RTYTIRNEHV DYVDVGGAYV GPTQNRILRL SKELGIETYK VNVSERLVQY 100
    VKGKTYPFRG AFPPVWNPIA YLDYNNLWRT IDNMGKEIPT DAPWEAQHAD 150
    KWDKMTMKEL IDKICWTKTA RRFAYLFVNI NVTSEPHEVS ALWFLWYVKQ 200
    CGGTTRIFSV TNGGQERKFV GGSGQVSERI MDLLGDQVKL NHPVTHVDQS 250
    SDNIIIETLN HEHYECKYVI NAIPPTLTAK IHFRPELPAE RNQLIQRLPM 300
    GAVIKCMMYY KEAFWKKKDY CGCMIIEDED APISITLDDT KPDGSLPAIM 350
    GFILARKADR LAKLHKEIRK KKICELYAKV LGSQEALHPV HYEEKNWCEE 400
    QYSGGCYTAY FPPGIMTQYG RVIRQPVGRI FFAGTETATK WSGYMEGAVE 450
    AGERAAREVL NGLGKVTEKD IWVQEPESKD VPAVEITHTF WERNLPSVSG 500
    LLKIIGFSTS VTALGFVLYK YKLLPRS 527
    Length:527
    Mass (Da):59,682
    Last modified:May 1, 1991 - v1
    Checksum:i4270E346928AE832
    GO
    Isoform 2 (identifier: P21397-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.

    Show »
    Length:394
    Mass (Da):44,848
    Checksum:iCA2429F72CD7F231
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti397 – 3971W → M AA sequence (PubMed:3178846)Curated

    Mass spectrometryi

    Molecular mass is 60512±6 Da from positions 1 - 527. Determined by ESI. 1 Publication

    Polymorphismi

    A polymorphism 1.2 kb upstream of the MAOA coding sequences consists of a 30-bp repeated sequence present in 3, 3.5, 4, or 5 copies. The polymorphism affect transcriptional activity of the MAOA gene promoter. Alleles with 3.5 or 4 copies of the repeat sequence are transcribed 2 to 10 times more efficiently than those with 3 or 5 copies of the repeat.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151D → E in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036545
    Natural varianti188 – 1881E → K.1 Publication
    Corresponds to variant rs77698881 [ dbSNP | Ensembl ].
    VAR_064573
    Natural varianti314 – 3141F → V.
    Corresponds to variant rs1799835 [ dbSNP | Ensembl ].
    VAR_014795
    Natural varianti520 – 5201K → R.
    Corresponds to variant rs1800466 [ dbSNP | Ensembl ].
    VAR_014796

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 133133Missing in isoform 2. 1 PublicationVSP_045173Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69226 mRNA. Translation: AAA59549.1.
    M68840 mRNA. Translation: AAA59548.1.
    X60806 Genomic DNA. No translation available.
    X60807 Genomic DNA. No translation available.
    X60808 Genomic DNA. No translation available.
    X60809 Genomic DNA. No translation available.
    X60810 Genomic DNA. No translation available.
    X60811 Genomic DNA. No translation available.
    X60812 Genomic DNA. No translation available.
    X60813 Genomic DNA. No translation available.
    X60814 Genomic DNA. No translation available.
    X60815 Genomic DNA. No translation available.
    X60816 Genomic DNA. No translation available.
    X60817 Genomic DNA. No translation available.
    X60818 Genomic DNA. No translation available.
    X60819 Genomic DNA. No translation available.
    M68857
    , M68843, M68844, M68845, M68846, M68847, M68848, M68849, M68850, M68851, M68852, M68853, M68854, M68855, M68856 Genomic DNA. Translation: AAA59547.1.
    AK293926 mRNA. Translation: BAG57307.1.
    AL109855 Genomic DNA. No translation available.
    BX530072 Genomic DNA. No translation available.
    BX537147 Genomic DNA. No translation available.
    BX537148 Genomic DNA. No translation available.
    BC008064 mRNA. Translation: AAH08064.1.
    M89636 Genomic DNA. Translation: AAB46385.1.
    S81371 Genomic DNA. Translation: AAD14361.1.
    S72704 Genomic DNA. Translation: AAD14113.1.
    CCDSiCCDS14260.1. [P21397-1]
    CCDS59163.1. [P21397-2]
    PIRiA36175.
    RefSeqiNP_000231.1. NM_000240.3. [P21397-1]
    NP_001257387.1. NM_001270458.1. [P21397-2]
    UniGeneiHs.183109.

    Genome annotation databases

    EnsembliENST00000338702; ENSP00000340684; ENSG00000189221. [P21397-1]
    ENST00000542639; ENSP00000440846; ENSG00000189221. [P21397-2]
    GeneIDi4128.
    KEGGihsa:4128.
    UCSCiuc004dfy.4. human. [P21397-1]

    Polymorphism databases

    DMDMi113978.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Monoamine oxidase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69226 mRNA. Translation: AAA59549.1 .
    M68840 mRNA. Translation: AAA59548.1 .
    X60806 Genomic DNA. No translation available.
    X60807 Genomic DNA. No translation available.
    X60808 Genomic DNA. No translation available.
    X60809 Genomic DNA. No translation available.
    X60810 Genomic DNA. No translation available.
    X60811 Genomic DNA. No translation available.
    X60812 Genomic DNA. No translation available.
    X60813 Genomic DNA. No translation available.
    X60814 Genomic DNA. No translation available.
    X60815 Genomic DNA. No translation available.
    X60816 Genomic DNA. No translation available.
    X60817 Genomic DNA. No translation available.
    X60818 Genomic DNA. No translation available.
    X60819 Genomic DNA. No translation available.
    M68857
    , M68843 , M68844 , M68845 , M68846 , M68847 , M68848 , M68849 , M68850 , M68851 , M68852 , M68853 , M68854 , M68855 , M68856 Genomic DNA. Translation: AAA59547.1 .
    AK293926 mRNA. Translation: BAG57307.1 .
    AL109855 Genomic DNA. No translation available.
    BX530072 Genomic DNA. No translation available.
    BX537147 Genomic DNA. No translation available.
    BX537148 Genomic DNA. No translation available.
    BC008064 mRNA. Translation: AAH08064.1 .
    M89636 Genomic DNA. Translation: AAB46385.1 .
    S81371 Genomic DNA. Translation: AAD14361.1 .
    S72704 Genomic DNA. Translation: AAD14113.1 .
    CCDSi CCDS14260.1. [P21397-1 ]
    CCDS59163.1. [P21397-2 ]
    PIRi A36175.
    RefSeqi NP_000231.1. NM_000240.3. [P21397-1 ]
    NP_001257387.1. NM_001270458.1. [P21397-2 ]
    UniGenei Hs.183109.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H8Q model - A 14-468 [» ]
    2BXR X-ray 3.00 A/B 1-527 [» ]
    2BXS X-ray 3.15 A/B 1-527 [» ]
    2Z5X X-ray 2.20 A 12-524 [» ]
    2Z5Y X-ray 2.17 A 12-524 [» ]
    ProteinModelPortali P21397.
    SMRi P21397. Positions 12-524.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110301. 2 interactions.
    IntActi P21397. 2 interactions.
    MINTi MINT-4054607.
    STRINGi 9606.ENSP00000340684.

    Chemistry

    BindingDBi P21397.
    ChEMBLi CHEMBL1951.
    DrugBanki DB00918. Almotriptan.
    DB00988. Dopamine.
    DB01363. Ephedra.
    DB03147. Flavin adenine dinucleotide.
    DB00614. Furazolidone.
    DB01247. Isocarboxazid.
    DB00601. Linezolid.
    DB01577. Methamphetamine.
    DB00805. Minaprine.
    DB01171. Moclobemide.
    DB08804. Nandrolone decanoate.
    DB00952. Naratriptan.
    DB00184. Nicotine.
    DB01626. Pargyline.
    DB00780. Phenelzine.
    DB00191. Phentermine.
    DB00388. Phenylephrine.
    DB00397. Phenylpropanolamine.
    DB00721. Procaine.
    DB00852. Pseudoephedrine.
    DB00140. Riboflavin.
    DB00953. Rizatriptan.
    DB01037. Selegiline.
    DB01104. Sertraline.
    DB00669. Sumatriptan.
    DB00624. Testosterone.
    DB00752. Tranylcypromine.
    DB00315. Zolmitriptan.
    DB00909. Zonisamide.
    GuidetoPHARMACOLOGYi 2489.

    PTM databases

    PhosphoSitei P21397.

    Polymorphism databases

    DMDMi 113978.

    Proteomic databases

    MaxQBi P21397.
    PaxDbi P21397.
    PeptideAtlasi P21397.
    PRIDEi P21397.

    Protocols and materials databases

    DNASUi 4128.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338702 ; ENSP00000340684 ; ENSG00000189221 . [P21397-1 ]
    ENST00000542639 ; ENSP00000440846 ; ENSG00000189221 . [P21397-2 ]
    GeneIDi 4128.
    KEGGi hsa:4128.
    UCSCi uc004dfy.4. human. [P21397-1 ]

    Organism-specific databases

    CTDi 4128.
    GeneCardsi GC0XP043515.
    HGNCi HGNC:6833. MAOA.
    HPAi CAB009437.
    MIMi 300615. phenotype.
    309850. gene+phenotype.
    neXtProti NX_P21397.
    Orphaneti 3057. Monoamine oxidase A deficiency.
    PharmGKBi PA236.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1231.
    HOGENOMi HOG000221615.
    HOVERGENi HBG004255.
    InParanoidi P21397.
    KOi K00274.
    OMAi MEITHTF.
    OrthoDBi EOG7K6PTP.
    PhylomeDBi P21397.
    TreeFami TF313314.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01798-MONOMER.
    BRENDAi 1.4.3.4. 2681.
    Reactomei REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
    REACT_15511. Enzymatic degradation of Dopamine by monoamine oxidase.
    REACT_15532. Metabolism of serotonin.
    REACT_15548. Enzymatic degradation of dopamine by COMT.
    REACT_416. Monoamines are oxidized to aldehydes by MAOA and MAOB, producing NH3 and H2O2.
    SABIO-RK P21397.

    Miscellaneous databases

    EvolutionaryTracei P21397.
    GeneWikii Monoamine_oxidase_A.
    GenomeRNAii 4128.
    NextBioi 16206.
    PROi P21397.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21397.
    Bgeei P21397.
    CleanExi HS_MAOA.
    Genevestigatori P21397.

    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. "Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences."
      Hsu Y.-P.P., Weyler W., Chen S., Sims K.B., Rinehart W.B., Utterback M.C., Powell J.F., Breakefield X.O.
      J. Neurochem. 51:1321-1324(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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].
    5. "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] (ISOFORM 2).
      Tissue: Cerebellum.
    6. "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].
    7. "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] (ISOFORM 1).
      Tissue: Ovary.
    8. "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 1-24.
    9. "The promoter of the human monoamine oxidase A gene."
      Denney R.M.
      Prog. Brain Res. 106:57-66(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
    10. "A new look at the promoter of the human monoamine oxidase A gene: mapping transcription initiation sites and capacity to drive luciferase expression."
      Denney R.M., Sharma A., Dave S.K., Waguespack A.
      J. Neurochem. 63:843-856(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
    11. "Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B."
      Chen S.-Y., Weyler W.
      Biochem. Biophys. Res. Commun. 156:445-450(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-45; 62-78; 109-129; 268-288; 298-315; 318-332; 336-352; 372-412; 430-440 AND 458-493.
      Tissue: Placenta.
    12. "Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit."
      Weyler W.
      Biochem. J. 260:725-729(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: DETERMINATION OF PROTEIN-FAD RATIO.
      Tissue: Placenta.
    13. "High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae."
      Li M., Hubalek F., Newton-Vinson P., Edmondson D.E.
      Protein Expr. Purif. 24:152-162(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT MET-1, MASS SPECTROMETRY.
    14. "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-165; CYS-266; CYS-306; CYS-321; CYS-323; CYS-374; CYS-398 AND CYS-406.
    15. "Abnormal behavior associated with a point mutation in the structural gene for monoamine oxidase A."
      Brunner H.G., Nelen M., Breakefield X.O., Ropers H.-H., van Oost B.A.
      Science 262:578-580(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN BRUNNER SYNDROME.
    16. "A functional polymorphism in the monoamine oxidase A gene promoter."
      Sabol S.Z., Hu S., Hamer D.
      Hum. Genet. 103:273-279(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM IN THE PROMOTER REGION.
    17. "Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B."
      De Colibus L., Li M., Binda C., Lustig A., Edmondson D.E., Mattevi A.
      Proc. Natl. Acad. Sci. U.S.A. 102:12684-12689(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), COFACTOR, SUBUNIT.
    18. "Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors."
      Son S.-Y., Ma J., Kondou Y., Yoshimura M., Yamashita E., Tsukihara T.
      Proc. Natl. Acad. Sci. U.S.A. 105:5739-5744(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 12-524 IN COMPLEX WITH FAD AND THE INHIBITOR HARMINE, COFACTOR, TOPOLOGY.
    19. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-15.
    20. Cited for: VARIANT LYS-188.

    Entry informationi

    Entry nameiAOFA_HUMAN
    AccessioniPrimary (citable) accession number: P21397
    Secondary accession number(s): B4DF46, Q16426
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 169 of the entry and version 1 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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3