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P21397 (AOFA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amine oxidase [flavin-containing] A

EC=1.4.3.4
Alternative name(s):
Monoamine oxidase type A
Short name=MAO-A
Gene names
Name:MAOA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

FAD. Ref.17 Ref.18

Subunit structure

Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer. Ref.17

Subcellular location

Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.

Tissue specificity

Heart, liver, duodenum, blood vessels and kidney.

Polymorphism

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.

Involvement in disease

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

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Mass spectrometry

Molecular mass is 60512±6 Da from positions 1 - 527. Determined by ESI. Ref.13

Ontologies

Keywords
   Biological processCatecholamine metabolism
Neurotransmitter degradation
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbehavior

Traceable author statement. Source: ProtInc

cellular biogenic amine metabolic process

Traceable author statement Ref.15. Source: ProtInc

dopamine catabolic process

Inferred from electronic annotation. Source: Ensembl

neurotransmitter biosynthetic process

Traceable author statement. Source: Reactome

neurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

neurotransmitter secretion

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

   Molecular_functionprimary amine oxidase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P21397-1)

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.
Isoform 2 (identifier: P21397-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Amine oxidase [flavin-containing] A
PRO_0000099850

Regions

Topological domain1 – 497497Cytoplasmic Ref.18
Transmembrane498 – 51821Helical; Anchor for type IV membrane protein
Topological domain519 – 5279Mitochondrial intermembrane Ref.18
Region520 – 5223Interaction with membrane phospholipid headgroups Probable

Sites

Site3351Important for substrate specificity By similarity
Site3741Important for catalytic activity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13
Modified residue4061S-8alpha-FAD cysteine

Natural variations

Alternative sequence1 – 133133Missing in isoform 2.
VSP_045173
Natural variant151D → E in a breast cancer sample; somatic mutation. Ref.19
VAR_036545
Natural variant1881E → K. Ref.20
Corresponds to variant rs77698881 [ dbSNP | Ensembl ].
VAR_064573
Natural variant3141F → V.
Corresponds to variant rs1799835 [ dbSNP | Ensembl ].
VAR_014795
Natural variant5201K → R.
Corresponds to variant rs1800466 [ dbSNP | Ensembl ].
VAR_014796

Experimental info

Mutagenesis1651C → S: No loss of activity. Ref.14
Mutagenesis2661C → S: No loss of activity. Ref.14
Mutagenesis3061C → S: No loss of activity. Ref.14
Mutagenesis3211C → S: No loss of activity. Ref.14
Mutagenesis3231C → S: No loss of activity. Ref.14
Mutagenesis3741C → S: Complete loss of activity. Ref.14
Mutagenesis3981C → S: No loss of activity. Ref.14
Mutagenesis4061C → S: Complete loss of activity. Ref.14
Sequence conflict3971W → M AA sequence Ref.11

Secondary structure

....................................................................................................... 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 4270E346928AE832

FASTA52759,682
        10         20         30         40         50         60 
MENQEKASIA GHMFDVVVIG GGISGLSAAK LLTEYGVSVL VLEARDRVGG RTYTIRNEHV 

        70         80         90        100        110        120 
DYVDVGGAYV GPTQNRILRL SKELGIETYK VNVSERLVQY VKGKTYPFRG AFPPVWNPIA 

       130        140        150        160        170        180 
YLDYNNLWRT IDNMGKEIPT DAPWEAQHAD KWDKMTMKEL IDKICWTKTA RRFAYLFVNI 

       190        200        210        220        230        240 
NVTSEPHEVS ALWFLWYVKQ CGGTTRIFSV TNGGQERKFV GGSGQVSERI MDLLGDQVKL 

       250        260        270        280        290        300 
NHPVTHVDQS SDNIIIETLN HEHYECKYVI NAIPPTLTAK IHFRPELPAE RNQLIQRLPM 

       310        320        330        340        350        360 
GAVIKCMMYY KEAFWKKKDY CGCMIIEDED APISITLDDT KPDGSLPAIM GFILARKADR 

       370        380        390        400        410        420 
LAKLHKEIRK KKICELYAKV LGSQEALHPV HYEEKNWCEE QYSGGCYTAY FPPGIMTQYG 

       430        440        450        460        470        480 
RVIRQPVGRI FFAGTETATK WSGYMEGAVE AGERAAREVL NGLGKVTEKD IWVQEPESKD 

       490        500        510        520 
VPAVEITHTF WERNLPSVSG LLKIIGFSTS VTALGFVLYK YKLLPRS 

« Hide

Isoform 2 [UniParc].

Checksum: CA2429F72CD7F231
Show »

FASTA39444,848

References

« Hide 'large scale' references
[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]"Structure of the human gene for monoamine oxidase type A."
Chen Z.-Y., Hotamisligil G.S., Huang J.-K., Wen L., Ezzeddine D., Aydin-Muderrisoglu N., Powell J.F., Huang R.H., Breakefield X.O., Craig I., Hsu Y.-P.P.
Nucleic Acids Res. 19:4537-4541(1991) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-15.
[20]"A population-specific HTR2B stop codon predisposes to severe impulsivity."
Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T., Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L., Virkkunen M., Goldman D.
Nature 468:1061-1066(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-188.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Monoamine oxidase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , 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.
PIRA36175.
RefSeqNP_000231.1. NM_000240.3.
NP_001257387.1. NM_001270458.1.
UniGeneHs.183109.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H8Qmodel-A14-468[»]
2BXRX-ray3.00A/B1-527[»]
2BXSX-ray3.15A/B1-527[»]
2Z5XX-ray2.20A12-524[»]
2Z5YX-ray2.17A12-524[»]
ProteinModelPortalP21397.
SMRP21397. Positions 12-524.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110301. 2 interactions.
IntActP21397. 2 interactions.
MINTMINT-4054607.
STRING9606.ENSP00000340684.

Chemistry

BindingDBP21397.
ChEMBLCHEMBL1951.
DrugBankDB00918. Almotriptan.
DB00190. Carbidopa.
DB01068. Clonazepam.
DB00988. Dopamine.
DB00176. Fluvoxamine.
DB01381. Ginkgo biloba.
DB00458. Imipramine.
DB01247. Isocarboxazid.
DB01235. Levodopa.
DB00601. Linezolid.
DB00186. Lorazepam.
DB01171. Moclobemide.
DB00184. Nicotine.
DB00368. Norepinephrine.
DB00780. Phenelzine.
DB00830. Phenmetrazine.
DB00191. Phentermine.
DB00388. Phenylephrine.
DB00397. Phenylpropanolamine.
DB00852. Pseudoephedrine.
DB01367. Rasagiline.
DB00140. Riboflavin.
DB00953. Rizatriptan.
DB01037. Selegiline.
DB00669. Sumatriptan.
DB00624. Testosterone.
DB00752. Tranylcypromine.
DB00315. Zolmitriptan.
GuidetoPHARMACOLOGY2489.

PTM databases

PhosphoSiteP21397.

Polymorphism databases

DMDM113978.

Proteomic databases

PaxDbP21397.
PeptideAtlasP21397.
PRIDEP21397.

Protocols and materials databases

DNASU4128.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338702; ENSP00000340684; ENSG00000189221. [P21397-1]
ENST00000542639; ENSP00000440846; ENSG00000189221. [P21397-2]
GeneID4128.
KEGGhsa:4128.
UCSCuc004dfy.4. human. [P21397-1]

Organism-specific databases

CTD4128.
GeneCardsGC0XP043515.
HGNCHGNC:6833. MAOA.
HPACAB009437.
MIM300615. phenotype.
309850. gene+phenotype.
neXtProtNX_P21397.
Orphanet3057. Monoamine oxidase A deficiency.
PharmGKBPA236.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1231.
HOGENOMHOG000221615.
HOVERGENHBG004255.
InParanoidP21397.
KOK00274.
OMADAPWEAP.
OrthoDBEOG7K6PTP.
PhylomeDBP21397.
TreeFamTF313314.

Enzyme and pathway databases

BioCycMetaCyc:HS01798-MONOMER.
BRENDA1.4.3.4. 2681.
ReactomeREACT_111217. Metabolism.
REACT_13685. Neuronal System.
SABIO-RKP21397.

Gene expression databases

ArrayExpressP21397.
BgeeP21397.
CleanExHS_MAOA.
GenevestigatorP21397.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Other

EvolutionaryTraceP21397.
GeneWikiMonoamine_oxidase_A.
GenomeRNAi4128.
NextBio16206.
PROP21397.
SOURCESearch...

Entry information

Entry nameAOFA_HUMAN
AccessionPrimary (citable) accession number: P21397
Secondary accession number(s): B4DF46, Q16426
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM