Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P21397 (AOFA_HUMAN)

Entry version 221 (02 Dec 2020)
Sequence version 1 (01 May 1991)
Previous versions | rss
Add a publicationFeedback
Protein

Amine oxidase [flavin-containing] A

Gene

MAOA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei335Important for substrate specificityBy similarity1
Sitei374Important for catalytic activity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processCatecholamine metabolism, Neurotransmitter degradation
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS01798-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.4.3.4, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P21397

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-141333, Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB
R-HSA-181430, Norepinephrine Neurotransmitter Release Cycle
R-HSA-379397, Enzymatic degradation of dopamine by COMT
R-HSA-379398, Enzymatic degradation of Dopamine by monoamine oxidase
R-HSA-380612, Metabolism of serotonin
R-HSA-5579012, Defective MAOA causes Brunner syndrome (BRUNS)
R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P21397

SIGNOR Signaling Network Open Resource

More...SIGNORi		P21397

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MAOA
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000189221.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:6833, MAOA

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		309850, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P21397

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 497Cytoplasmic1 PublicationAdd BLAST497
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei498 – 518Helical; Anchor for type IV membrane proteinAdd BLAST21
Topological domaini519 – 527Mitochondrial intermembrane1 Publication9

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Brunner syndrome (BRNRS)1 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.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi165C → S: No loss of activity. 1 Publication1
Mutagenesisi266C → S: No loss of activity. 1 Publication1
Mutagenesisi306C → S: No loss of activity. 1 Publication1
Mutagenesisi321C → S: No loss of activity. 1 Publication1
Mutagenesisi323C → S: No loss of activity. 1 Publication1
Mutagenesisi374C → S: Complete loss of activity. 1 Publication1
Mutagenesisi398C → S: No loss of activity. 1 Publication1
Mutagenesisi406C → S: Complete loss of activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

More...DisGeNETi		4128

MalaCards human disease database

More...MalaCardsi		MAOA
MIMi300615, phenotype

Open Targets

More...OpenTargetsi		ENSG00000189221

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		3057, Monoamine oxidase A deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA236

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P21397, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1951

Drug and drug target database

More...DrugBanki		DB01472, 4-Methoxyamphetamine
DB00918, Almotriptan
DB00182, Amphetamine
DB04889, Bicifadine
DB13876, Brofaromine
DB01445, Bufotenine
DB06774, Capsaicin
DB04017, Clorgiline
DB09130, Copper
DB05205, CX157
DB07641, Decyl(dimethyl)phosphine oxide
DB00988, Dopamine
DB01363, Ephedra sinica root
DB00668, Epinephrine
DB12329, Eravacycline
DB01175, Escitalopram
DB03147, Flavin adenine dinucleotide
DB14914, Flortaucipir F-18
DB00614, Furazolidone
DB07919, Harmine
DB04818, Iproniazid
DB01247, Isocarboxazid
DB00601, Linezolid
DB01577, Metamfetamine
DB00805, Minaprine
DB01442, MMDA
DB01171, Moclobemide
DB08804, Nandrolone decanoate
DB00952, Naratriptan
DB04820, Nialamide
DB00184, Nicotine
DB04821, Nomifensine
DB06412, Oxymetholone
DB01626, Pargyline
DB00780, Phenelzine
DB00191, Phentermine
DB00388, Phenylephrine
DB00397, Phenylpropanolamine
DB09244, Pirlindole
DB04850, Posizolid
DB00721, Procaine
DB01168, Procarbazine
DB00571, Propranolol
DB00852, Pseudoephedrine
DB09363, Rauwolfia serpentina root
DB00140, Riboflavin
DB00953, Rizatriptan
DB06654, Safinamide
DB01037, Selegiline
DB01104, Sertraline
DB00669, Sumatriptan
DB14569, Tedizolid
DB09042, Tedizolid phosphate
DB00624, Testosterone
DB13943, Testosterone cypionate
DB13944, Testosterone enanthate
DB13946, Testosterone undecanoate
DB09245, Toloxatone
DB00752, Tranylcypromine
DB15328, Ubrogepant
DB04832, Zimelidine
DB00315, Zolmitriptan
DB00909, Zonisamide

DrugCentral

More...DrugCentrali		P21397

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2489

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MAOA

Domain mapping of disease mutations (DMDM)

More...DMDMi		113978

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000998501 – 527Amine oxidase [flavin-containing] AAdd BLAST527

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionine1 Publication1
Modified residuei383PhosphoserineBy similarity1
Modified residuei406S-8alpha-FAD cysteineCombined sources1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P21397

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P21397

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P21397

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P21397

PeptideAtlas

More...PeptideAtlasi		P21397

PRoteomics IDEntifications database

More...PRIDEi		P21397

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		4005
53866 [P21397-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P21397

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P21397

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P21397

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Heart, liver, duodenum, blood vessels and kidney.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000189221, Expressed in small intestine and 238 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P21397, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P21397, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000189221, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		110301, 7 interactors

Protein interaction database and analysis system

More...IntActi		P21397, 6 interactors

Molecular INTeraction database

More...MINTi		P21397

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000340684

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P21397

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P21397, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1527
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P21397

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P21397

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni520 – 522Interaction with membrane phospholipid headgroupsCurated3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0029, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160514

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_004498_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P21397

Identification of Orthologs from Complete Genome Data

More...OMAi		EWTRGAY

Database for complete collections of gene phylogenies

More...PhylomeDBi		P21397

TreeFam database of animal gene trees

More...TreeFami		TF313314

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.50.50.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002937, Amino_oxidase
IPR036188, FAD/NAD-bd_sf
IPR001613, Flavin_amine_oxidase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01593, Amino_oxidase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00757, AMINEOXDASEF

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51905, SSF51905, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P21397-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti397W → M AA sequence (PubMed:3178846).Curated1

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 60512±6 Da. Determined by ESI. 1 Publication

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03654515D → E in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_064573188E → K1 PublicationCorresponds to variant dbSNP:rs77698881Ensembl.1
Natural variantiVAR_071963266C → F Probable disease-associated variant found in a family with Brunner syndrome-like behavioral disturbances; reduced activity. 1 PublicationCorresponds to variant dbSNP:rs587777457EnsemblClinVar.1
Natural variantiVAR_014795314F → V. Corresponds to variant dbSNP:rs1799835Ensembl.1
Natural variantiVAR_014796520K → R. Corresponds to variant dbSNP:rs1800466EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0451731 – 133Missing in isoform 2. 1 PublicationAdd BLAST133

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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 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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS14260.1 [P21397-1]
CCDS59163.1 [P21397-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A36175

NCBI Reference Sequences

More...RefSeqi		NP_000231.1, NM_000240.3 [P21397-1]
NP_001257387.1, NM_001270458.1 [P21397-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000338702; ENSP00000340684; ENSG00000189221 [P21397-1]
ENST00000542639; ENSP00000440846; ENSG00000189221 [P21397-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4128

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4128

UCSC genome browser

More...UCSCi		uc011mkw.3, human [P21397-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Monoamine oxidase entry

Protein Spotlight

Approaching happiness - Issue 172 of August 2015

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 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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H8Qmodel-A14-468[»]
2BXRX-ray3.00A/B1-527[»]
2BXSX-ray3.15A/B1-527[»]
2Z5XX-ray2.20A12-524[»]
2Z5YX-ray2.17A12-524[»]
SMRiP21397
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi110301, 7 interactors
IntActiP21397, 6 interactors
MINTiP21397
STRINGi9606.ENSP00000340684

Chemistry databases

BindingDBiP21397
ChEMBLiCHEMBL1951
DrugBankiDB01472, 4-Methoxyamphetamine
DB00918, Almotriptan
DB00182, Amphetamine
DB04889, Bicifadine
DB13876, Brofaromine
DB01445, Bufotenine
DB06774, Capsaicin
DB04017, Clorgiline
DB09130, Copper
DB05205, CX157
DB07641, Decyl(dimethyl)phosphine oxide
DB00988, Dopamine
DB01363, Ephedra sinica root
DB00668, Epinephrine
DB12329, Eravacycline
DB01175, Escitalopram
DB03147, Flavin adenine dinucleotide
DB14914, Flortaucipir F-18
DB00614, Furazolidone
DB07919, Harmine
DB04818, Iproniazid
DB01247, Isocarboxazid
DB00601, Linezolid
DB01577, Metamfetamine
DB00805, Minaprine
DB01442, MMDA
DB01171, Moclobemide
DB08804, Nandrolone decanoate
DB00952, Naratriptan
DB04820, Nialamide
DB00184, Nicotine
DB04821, Nomifensine
DB06412, Oxymetholone
DB01626, Pargyline
DB00780, Phenelzine
DB00191, Phentermine
DB00388, Phenylephrine
DB00397, Phenylpropanolamine
DB09244, Pirlindole
DB04850, Posizolid
DB00721, Procaine
DB01168, Procarbazine
DB00571, Propranolol
DB00852, Pseudoephedrine
DB09363, Rauwolfia serpentina root
DB00140, Riboflavin
DB00953, Rizatriptan
DB06654, Safinamide
DB01037, Selegiline
DB01104, Sertraline
DB00669, Sumatriptan
DB14569, Tedizolid
DB09042, Tedizolid phosphate
DB00624, Testosterone
DB13943, Testosterone cypionate
DB13944, Testosterone enanthate
DB13946, Testosterone undecanoate
DB09245, Toloxatone
DB00752, Tranylcypromine
DB15328, Ubrogepant
DB04832, Zimelidine
DB00315, Zolmitriptan
DB00909, Zonisamide
DrugCentraliP21397
GuidetoPHARMACOLOGYi2489

PTM databases

iPTMnetiP21397
PhosphoSitePlusiP21397
SwissPalmiP21397

Polymorphism and mutation databases

BioMutaiMAOA
DMDMi113978

Proteomic databases

EPDiP21397
jPOSTiP21397
MassIVEiP21397
PaxDbiP21397
PeptideAtlasiP21397
PRIDEiP21397
ProteomicsDBi4005
53866 [P21397-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		10933, 445 antibodies

The DNASU plasmid repository

More...DNASUi		4128

Genome annotation databases

EnsembliENST00000338702; ENSP00000340684; ENSG00000189221 [P21397-1]
ENST00000542639; ENSP00000440846; ENSG00000189221 [P21397-2]
GeneIDi4128
KEGGihsa:4128
UCSCiuc011mkw.3, human [P21397-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4128
DisGeNETi4128
EuPathDBiHostDB:ENSG00000189221.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		MAOA
HGNCiHGNC:6833, MAOA
HPAiENSG00000189221, Low tissue specificity
MalaCardsiMAOA
MIMi300615, phenotype
309850, gene
neXtProtiNX_P21397
OpenTargetsiENSG00000189221
Orphaneti3057, Monoamine oxidase A deficiency
PharmGKBiPA236

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0029, Eukaryota
GeneTreeiENSGT00940000160514
HOGENOMiCLU_004498_0_1_1
InParanoidiP21397
OMAiEWTRGAY
PhylomeDBiP21397
TreeFamiTF313314

Enzyme and pathway databases

BioCyciMetaCyc:HS01798-MONOMER
BRENDAi1.4.3.4, 2681
PathwayCommonsiP21397
ReactomeiR-HSA-141333, Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB
R-HSA-181430, Norepinephrine Neurotransmitter Release Cycle
R-HSA-379397, Enzymatic degradation of dopamine by COMT
R-HSA-379398, Enzymatic degradation of Dopamine by monoamine oxidase
R-HSA-380612, Metabolism of serotonin
R-HSA-5579012, Defective MAOA causes Brunner syndrome (BRUNS)
R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling
SABIO-RKiP21397
SIGNORiP21397

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		4128, 4 hits in 471 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		MAOA, human
EvolutionaryTraceiP21397

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Monoamine_oxidase_A

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		4128
PharosiP21397, Tclin

Protein Ontology

More...PROi		PR:P21397
RNActiP21397, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000189221, Expressed in small intestine and 238 other tissues
ExpressionAtlasiP21397, baseline and differential
GenevisibleiP21397, HS

Family and domain databases

Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR002937, Amino_oxidase
IPR036188, FAD/NAD-bd_sf
IPR001613, Flavin_amine_oxidase
PfamiView protein in Pfam
PF01593, Amino_oxidase, 1 hit
PRINTSiPR00757, AMINEOXDASEF
SUPFAMiSSF51905, SSF51905, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAOFA_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P21397
Secondary accession number(s): B4DF46, Q16426
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: December 2, 2020
This is version 221 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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
  5. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  6. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again