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Protein

Amine oxidase [flavin-containing] A

Gene

MAOA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

FAD2 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: ParkinsonsUK-UCL
  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
Complete GO annotation...

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. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 497497Cytoplasmic1 PublicationAdd
BLAST
Transmembranei498 – 51821Helical; Anchor for type IV membrane proteinAdd
BLAST
Topological domaini519 – 5279Mitochondrial intermembrane1 Publication

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial outer membrane Source: ParkinsonsUK-UCL
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Brunner syndrome1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:300615

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

Disease mutation, 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

BgeeiP21397.
CleanExiHS_MAOA.
ExpressionAtlasiP21397. baseline and differential.
GenevestigatoriP21397.

Organism-specific databases

HPAiCAB009437.
HPA054807.
HPA059299.

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00730000110903.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP21397.
KOiK00274.
OMAiDAPWEAP.
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. AlignAdd to basket

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

        10         20         30         40         50
MENQEKASIA GHMFDVVVIG GGISGLSAAK LLTEYGVSVL VLEARDRVGG
60 70 80 90 100
RTYTIRNEHV DYVDVGGAYV GPTQNRILRL SKELGIETYK VNVSERLVQY
110 120 130 140 150
VKGKTYPFRG AFPPVWNPIA YLDYNNLWRT IDNMGKEIPT DAPWEAQHAD
160 170 180 190 200
KWDKMTMKEL IDKICWTKTA RRFAYLFVNI NVTSEPHEVS ALWFLWYVKQ
210 220 230 240 250
CGGTTRIFSV TNGGQERKFV GGSGQVSERI MDLLGDQVKL NHPVTHVDQS
260 270 280 290 300
SDNIIIETLN HEHYECKYVI NAIPPTLTAK IHFRPELPAE RNQLIQRLPM
310 320 330 340 350
GAVIKCMMYY KEAFWKKKDY CGCMIIEDED APISITLDDT KPDGSLPAIM
360 370 380 390 400
GFILARKADR LAKLHKEIRK KKICELYAKV LGSQEALHPV HYEEKNWCEE
410 420 430 440 450
QYSGGCYTAY FPPGIMTQYG RVIRQPVGRI FFAGTETATK WSGYMEGAVE
460 470 480 490 500
AGERAAREVL NGLGKVTEKD IWVQEPESKD VPAVEITHTF WERNLPSVSG
510 520
LLKIIGFSTS VTALGFVLYK YKLLPRS
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 varianti266 – 2661C → F Probable disease-associated mutation found in a family with Brunner syndrome-like behavioral disturbances; reduced activity. 1 Publication
VAR_071963
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

BindingDBiP21397.
ChEMBLiCHEMBL1951.
DrugBankiDB00918. 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.
GuidetoPHARMACOLOGYi2489.

PTM databases

PhosphoSiteiP21397.

Polymorphism databases

DMDMi113978.

Proteomic databases

MaxQBiP21397.
PaxDbiP21397.
PeptideAtlasiP21397.
PRIDEiP21397.

Protocols and materials databases

DNASUi4128.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4128.
GeneCardsiGC0XP043515.
HGNCiHGNC:6833. MAOA.
HPAiCAB009437.
HPA054807.
HPA059299.
MIMi300615. phenotype.
309850. gene+phenotype.
neXtProtiNX_P21397.
Orphaneti3057. Monoamine oxidase A deficiency.
PharmGKBiPA236.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1231.
GeneTreeiENSGT00730000110903.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP21397.
KOiK00274.
OMAiDAPWEAP.
OrthoDBiEOG7K6PTP.
PhylomeDBiP21397.
TreeFamiTF313314.

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. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
SABIO-RKP21397.

Miscellaneous databases

ChiTaRSiMAOA. human.
EvolutionaryTraceiP21397.
GeneWikiiMonoamine_oxidase_A.
GenomeRNAii4128.
NextBioi16206.
PROiP21397.
SOURCEiSearch...

Gene expression databases

BgeeiP21397.
CleanExiHS_MAOA.
ExpressionAtlasiP21397. baseline and differential.
GenevestigatoriP21397.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "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.
  19. "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.
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-15.
  21. Cited for: VARIANT LYS-188.
  22. "20 ans apres: a second mutation in MAOA identified by targeted high-throughput sequencing in a family with altered behavior and cognition."
    Piton A., Poquet H., Redin C., Masurel A., Lauer J., Muller J., Thevenon J., Herenger Y., Chancenotte S., Bonnet M., Pinoit J.M., Huet F., Thauvin-Robinet C., Jaeger A.S., Le Gras S., Jost B., Gerard B., Peoc'h K.
    , Launay J.M., Faivre L., Mandel J.L.
    Eur. J. Hum. Genet. 22:776-783(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PHE-266, CHARACTERIZATION OF VARIANT PHE-266.

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: March 4, 2015
This is version 174 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.