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UniProtKB - Q16853 (AOC3_HUMAN)

Entry version 187 (10 Apr 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Membrane primary amine oxidase

Gene

AOC3

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

Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has semicarbazide-sensitive (SSAO) monoamine oxidase activity. May play a role in adipogenesis.4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.94 mM for 2-phenylethylamine1 Publication
  2. KM=0.67 mM for methylamine1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei386Proton acceptorBy similarity1
    Active sitei471Schiff-base intermediate with substrate; via topaquinoneCombined sources1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi520Copper; via tele nitrogenCombined sources1 Publication1
    Metal bindingi522Copper; via tele nitrogenCombined sources1 Publication1
    Metal bindingi529Calcium 1Combined sources1
    Metal bindingi530Calcium 1; via carbonyl oxygenCombined sources1
    Metal bindingi531Calcium 1Combined sources1
    Metal bindingi572Calcium 2Combined sources1
    Metal bindingi638Calcium 2Combined sources1
    Metal bindingi641Calcium 2Combined sources1
    Metal bindingi663Calcium 2; via carbonyl oxygenCombined sources1
    Metal bindingi665Calcium 2Combined sources1
    Metal bindingi667Calcium 2Combined sources1
    Metal bindingi673Calcium 1Combined sources1
    Metal bindingi674Calcium 1; via carbonyl oxygenCombined sources1
    Metal bindingi684Copper; via pros nitrogenCombined sources1 Publication1

    <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

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the 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 processCell adhesion
    LigandCalcium, Copper, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.4.3.21 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-211945 Phase I - Functionalization of compounds

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		Q16853

    <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_and_taxonomy_section">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:
    Membrane primary amine oxidase (EC:1.4.3.211 Publication)
    Alternative name(s):
    Copper amine oxidase
    HPAO
    Semicarbazide-sensitive amine oxidase
    Short name:
    SSAO
    Vascular adhesion protein 1
    Short name:
    VAP-1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:AOC3
    Synonyms:VAP1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 17

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000131471.6

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:550 AOC3

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		603735 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_Q16853

    <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_location_section">'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 – 5CytoplasmicSequence analysis5
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei6 – 26Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini27 – 763ExtracellularSequence analysisAdd BLAST737

    Keywords - Cellular componenti

    Cell membrane, 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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi211M → V: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with N-394 and G-469. 1 Publication1
    Mutagenesisi394Y → N: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and G-469. 1 Publication1
    Mutagenesisi469L → G: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and N-394. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		8639

    Open Targets

    More...    OpenTargetsi    		ENSG00000131471

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA24840

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL3437

    Drug and drug target database

    More...    DrugBanki    		DB04334 6-hydroxydopa quinone
    DB01275 Hydralazine
    DB00780 Phenelzine

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...    GuidetoPHARMACOLOGYi    		2767

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		AOC3

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		2501336

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000641021 – 763Membrane primary amine oxidaseAdd BLAST763

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi137N-linked (GlcNAc...) asparagineCombined sources2 Publications1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi198 ↔ 1991 Publication
    Glycosylationi212O-linked (GalNAc...) threonine1 Publication1
    Glycosylationi232N-linked (GlcNAc...) asparagineCombined sources1 Publication1
    Glycosylationi294N-linked (GlcNAc...) asparagineCombined sources2 Publications1
    Disulfide bondi404 ↔ 430By similarity
    <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 residuei4712',4',5'-topaquinoneCombined sources1
    Glycosylationi592N-linked (GlcNAc...) (complex) asparagineCombined sources4 Publications1
    Glycosylationi618N-linked (GlcNAc...) asparagineCombined sources3 Publications1
    Glycosylationi666N-linked (GlcNAc...) asparagineCombined sources3 Publications1
    Disulfide bondi734 ↔ 7411 Publication
    Disulfide bondi748Interchain1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.1 Publication
    N- and O-glycosylated.4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, TPQ

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		Q16853

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

    More...    PaxDbi    		Q16853

    PeptideAtlas

    More...    PeptideAtlasi    		Q16853

    PRoteomics IDEntifications database

    More...    PRIDEi    		Q16853

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		61105

    PTM databases

    GlyConnect protein glycosylation platform

    More...    GlyConnecti    		1502

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		Q16853

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

    More...    PhosphoSitePlusi    		Q16853

    <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

    Strongly expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. Also highly expressed in appendix, lung and small intestine. Expressed also in adipose tissue, in bone marrow, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, spleen and testis. Isoform 2 seems to be the predominant transcript in fetal kidneys, fetal cartilage and fetal tonsils. The highest relative expression of isoform 2 occurs in skeletal muscle, heart, pancreas, kidney, and lung.3 Publications

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Up-regulated during in vitro adipocyte differentiation.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000131471 Expressed in 206 organ(s), highest expression level in adipose tissue

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		Q16853 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		Q16853 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		CAB025797
    HPA000980

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer; disulfide-linked. Can heterodimerize with isoform 2 leading to reduced surface expression. Forms a heterodimer with AOC2.3 Publications

    GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		114192, 11 interactors

    Protein interaction database and analysis system

    More...    IntActi    		Q16853, 10 interactors

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000312326

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		Q16853

    <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

    1763
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    1PU4X-ray3.20A/B1-763[»]
    1US1X-ray2.90A/B1-763[»]
    2C10X-ray2.50A/B/C/D29-763[»]
    2C11X-ray2.90A/B/C/D29-763[»]
    2Y73X-ray2.60A/B1-763[»]
    2Y74X-ray2.95A/B1-763[»]
    3ALAX-ray2.90A/B/C/D/E/F/G33-763[»]
    4BTWX-ray2.80A/B27-763[»]
    4BTXX-ray2.78A/B27-763[»]
    4BTYX-ray3.10A/B27-763[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		Q16853

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

    More...    SMRi    		Q16853

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		Q16853

    <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>Regioni384 – 394Substrate bindingCombined sourcesAdd BLAST11
    Regioni468 – 473Substrate bindingBy similarity6

    <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 copper/topaquinone oxidase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG1186 Eukaryota
    COG3733 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00950000183207

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000233919

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG004164

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		Q16853

    KEGG Orthology (KO)

    More...    KOi    		K00276

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		ISWGRYQ

    Database of Orthologous Groups

    More...    OrthoDBi    		1320015at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		Q16853

    TreeFam database of animal gene trees

    More...    TreeFami    		TF314750

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		2.70.98.20, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR000269 Cu_amine_oxidase
    IPR015798 Cu_amine_oxidase_C
    IPR036460 Cu_amine_oxidase_C_sf
    IPR016182 Cu_amine_oxidase_N-reg
    IPR015800 Cu_amine_oxidase_N2
    IPR015802 Cu_amine_oxidase_N3

    The PANTHER Classification System

    More...    PANTHERi    		PTHR10638 PTHR10638, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01179 Cu_amine_oxid, 1 hit
    PF02727 Cu_amine_oxidN2, 1 hit
    PF02728 Cu_amine_oxidN3, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00766 CUDAOXIDASE

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF49998 SSF49998, 1 hit
    SSF54416 SSF54416, 2 hits

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS01164 COPPER_AMINE_OXID_1, 1 hit
    PS01165 COPPER_AMINE_OXID_2, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 3 <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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q16853-1) [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
    MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSVSPSAQP 
            60         70         80         90        100
    WTHPGQSQLF ADLSREELTA VMRFLTQRLG PGLVDAAQAR PSDNCVFSVE 
           110        120        130        140        150
    LQLPPKAAAL AHLDRGSPPP AREALAIVFF GRQPQPNVSE LVVGPLPHPS 
           160        170        180        190        200
    YMRDVTVERH GGPLPYHRRP VLFQEYLDID QMIFNRELPQ ASGLLHHCCF 
           210        220        230        240        250
    YKHRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL HHVGLELLVN 
           260        270        280        290        300
    HKALDPARWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW 
           310        320        330        340        350
    SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF 
           360        370        380        390        400
    DVRFQGERLV YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYTTPLTR 
           410        420        430        440        450
    GVDCPYLATY VDWHFLLESQ APKTIRDAFC VFEQNQGLPL RRHHSDLYSH 
           460        470        480        490        500
    YFGGLAETVL VVRSMSTLLN YDYVWDTVFH PSGAIEIRFY ATGYISSAFL 
           510        520        530        540        550
    FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DVAGLENWVW AEDMVFVPMA 
           560        570        580        590        600
    VPWSPEHQLQ RLQVTRKLLE MEEQAAFLVG SATPRYLYLA SNHSNKWGHP 
           610        620        630        640        650
    RGYRIQMLSF AGEPLPQNSS MARGFSWERY QLAVTQRKEE EPSSSSVFNQ 
           660        670        680        690        700
    NDPWAPTVDF SDFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG 
           710        720        730        740        750
    VGFFLRPYNF FDEDPSFYSA DSIYFRGDQD AGACEVNPLA CLPQAAACAP 
           760 
    DLPAFSHGGF SHN
    Length:763
    Mass (Da):84,622
    Last modified:January 23, 2007 - v3
    <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:i58AD55605EC9D228
    GO
    Isoform 2 (identifier: Q16853-2) [UniParc]FASTAAdd to basket
    Also known as: VAP-1Delta3

    The sequence of this isoform differs from the canonical sequence as follows:
         630-634: YQLAV → IWWPG
         635-763: Missing.

    Note: Devoid of the semicarbazide-sensitive amine oxidase (SSAO) activity.
    Show »
    Length:634
    Mass (Da):70,675
    Checksum:i3275AE7C61775C99
    GO
    Isoform 3 (identifier: Q16853-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-543: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:220
    Mass (Da):24,533
    Checksum:i37CB1D564AC233E2
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    K7EIK5K7EIK5_HUMAN
    Amine oxidase
    AOC3
    		144Annotation score:

    Annotation score:2 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>
    K7EL47K7EL47_HUMAN
    Amine oxidase
    AOC3
    		152Annotation score:

    Annotation score:2 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>
    K7EQZ5K7EQZ5_HUMAN
    Amine oxidase
    AOC3
    		112Annotation score:

    Annotation score:2 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>

    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_0250355T → R1 PublicationCorresponds to variant dbSNP:rs33954211Ensembl.1
    Natural variantiVAR_05260378R → Q. Corresponds to variant dbSNP:rs402680Ensembl.1
    Natural variantiVAR_025027167H → Y1 PublicationCorresponds to variant dbSNP:rs2228470Ensembl.1
    Natural variantiVAR_052604171V → M. Corresponds to variant dbSNP:rs408038Ensembl.1
    Natural variantiVAR_052605203H → R. Corresponds to variant dbSNP:rs630079Ensembl.1
    Natural variantiVAR_012064317Y → H. Corresponds to variant dbSNP:rs438287Ensembl.1
    Natural variantiVAR_024343329R → Q. Corresponds to variant dbSNP:rs2229595Ensembl.1
    Natural variantiVAR_025028371I → T1 PublicationCorresponds to variant dbSNP:rs35097308Ensembl.1
    Natural variantiVAR_025029408A → S1 PublicationCorresponds to variant dbSNP:rs35643019Ensembl.1
    Natural variantiVAR_025030426R → H1 PublicationCorresponds to variant dbSNP:rs33986943Ensembl.1
    Natural variantiVAR_025031441R → W1 PublicationCorresponds to variant dbSNP:rs2229596Ensembl.1
    Natural variantiVAR_025032582A → T1 PublicationCorresponds to variant dbSNP:rs34987927Ensembl.1
    Natural variantiVAR_025033700G → S1 PublicationCorresponds to variant dbSNP:rs477207Ensembl.1
    Natural variantiVAR_025034749A → V1 PublicationCorresponds to variant dbSNP:rs34012919Ensembl.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_0552011 – 543Missing in isoform 3. 1 PublicationAdd BLAST543
    Alternative sequenceiVSP_053751630 – 634YQLAV → IWWPG in isoform 2. 1 Publication5
    Alternative sequenceiVSP_053752635 – 763Missing in isoform 2. 1 PublicationAdd BLAST129

    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
    		U39447 mRNA Translation: AAC50919.1
    AF067406 mRNA Translation: AAC25170.1
    AB050502 Genomic DNA Translation: BAB18866.1
    JX020506 mRNA Translation: AGB67480.1
    AK025727 mRNA No translation available.
    AK315129 mRNA Translation: BAG37582.1
    DQ143944 Genomic DNA Translation: AAZ38716.1
    AC016889 Genomic DNA No translation available.
    BC050549 mRNA Translation: AAH50549.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS11444.1 [Q16853-1]
    CCDS62198.1 [Q16853-3]
    CCDS74071.1 [Q16853-2]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		JC5234

    NCBI Reference Sequences

    More...    RefSeqi    		NP_001264660.1, NM_001277731.1 [Q16853-2]
    NP_001264661.1, NM_001277732.1 [Q16853-3]
    NP_003725.1, NM_003734.3 [Q16853-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Hs.198241

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000308423; ENSP00000312326; ENSG00000131471 [Q16853-1]
    ENST00000591562; ENSP00000468632; ENSG00000131471 [Q16853-3]
    ENST00000613571; ENSP00000484312; ENSG00000131471 [Q16853-2]
    ENST00000617500; ENSP00000477686; ENSG00000131471 [Q16853-3]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		8639

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:8639

    UCSC genome browser

    More...    UCSCi    		uc002ibv.6 human [Q16853-1]

    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_references_section">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

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		U39447 mRNA Translation: AAC50919.1
    AF067406 mRNA Translation: AAC25170.1
    AB050502 Genomic DNA Translation: BAB18866.1
    JX020506 mRNA Translation: AGB67480.1
    AK025727 mRNA No translation available.
    AK315129 mRNA Translation: BAG37582.1
    DQ143944 Genomic DNA Translation: AAZ38716.1
    AC016889 Genomic DNA No translation available.
    BC050549 mRNA Translation: AAH50549.1
    CCDSiCCDS11444.1 [Q16853-1]
    CCDS62198.1 [Q16853-3]
    CCDS74071.1 [Q16853-2]
    PIRiJC5234
    RefSeqiNP_001264660.1, NM_001277731.1 [Q16853-2]
    NP_001264661.1, NM_001277732.1 [Q16853-3]
    NP_003725.1, NM_003734.3 [Q16853-1]
    UniGeneiHs.198241

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1PU4X-ray3.20A/B1-763[»]
    1US1X-ray2.90A/B1-763[»]
    2C10X-ray2.50A/B/C/D29-763[»]
    2C11X-ray2.90A/B/C/D29-763[»]
    2Y73X-ray2.60A/B1-763[»]
    2Y74X-ray2.95A/B1-763[»]
    3ALAX-ray2.90A/B/C/D/E/F/G33-763[»]
    4BTWX-ray2.80A/B27-763[»]
    4BTXX-ray2.78A/B27-763[»]
    4BTYX-ray3.10A/B27-763[»]
    ProteinModelPortaliQ16853
    SMRiQ16853
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114192, 11 interactors
    IntActiQ16853, 10 interactors
    STRINGi9606.ENSP00000312326

    Chemistry databases

    BindingDBiQ16853
    ChEMBLiCHEMBL3437
    DrugBankiDB04334 6-hydroxydopa quinone
    DB01275 Hydralazine
    DB00780 Phenelzine
    GuidetoPHARMACOLOGYi2767

    PTM databases

    GlyConnecti1502
    iPTMnetiQ16853
    PhosphoSitePlusiQ16853

    Polymorphism and mutation databases

    BioMutaiAOC3
    DMDMi2501336

    Proteomic databases

    jPOSTiQ16853
    PaxDbiQ16853
    PeptideAtlasiQ16853
    PRIDEiQ16853
    ProteomicsDBi61105

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000308423; ENSP00000312326; ENSG00000131471 [Q16853-1]
    ENST00000591562; ENSP00000468632; ENSG00000131471 [Q16853-3]
    ENST00000613571; ENSP00000484312; ENSG00000131471 [Q16853-2]
    ENST00000617500; ENSP00000477686; ENSG00000131471 [Q16853-3]
    GeneIDi8639
    KEGGihsa:8639
    UCSCiuc002ibv.6 human [Q16853-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		8639
    DisGeNETi8639
    EuPathDBiHostDB:ENSG00000131471.6

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		AOC3
    HGNCiHGNC:550 AOC3
    HPAiCAB025797
    HPA000980
    MIMi603735 gene
    neXtProtiNX_Q16853
    OpenTargetsiENSG00000131471
    PharmGKBiPA24840

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG1186 Eukaryota
    COG3733 LUCA
    GeneTreeiENSGT00950000183207
    HOGENOMiHOG000233919
    HOVERGENiHBG004164
    InParanoidiQ16853
    KOiK00276
    OMAiISWGRYQ
    OrthoDBi1320015at2759
    PhylomeDBiQ16853
    TreeFamiTF314750

    Enzyme and pathway databases

    BRENDAi1.4.3.21 2681
    ReactomeiR-HSA-211945 Phase I - Functionalization of compounds
    SABIO-RKiQ16853

    Miscellaneous databases

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

    More...    ChiTaRSi    		AOC3 human
    EvolutionaryTraceiQ16853

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		AOC3

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

    More...    GenomeRNAii    		8639

    Protein Ontology

    More...    PROi    		PR:Q16853

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000131471 Expressed in 206 organ(s), highest expression level in adipose tissue
    ExpressionAtlasiQ16853 baseline and differential
    GenevisibleiQ16853 HS

    Family and domain databases

    Gene3Di2.70.98.20, 1 hit
    InterProiView protein in InterPro
    IPR000269 Cu_amine_oxidase
    IPR015798 Cu_amine_oxidase_C
    IPR036460 Cu_amine_oxidase_C_sf
    IPR016182 Cu_amine_oxidase_N-reg
    IPR015800 Cu_amine_oxidase_N2
    IPR015802 Cu_amine_oxidase_N3
    PANTHERiPTHR10638 PTHR10638, 1 hit
    PfamiView protein in Pfam
    PF01179 Cu_amine_oxid, 1 hit
    PF02727 Cu_amine_oxidN2, 1 hit
    PF02728 Cu_amine_oxidN3, 1 hit
    PRINTSiPR00766 CUDAOXIDASE
    SUPFAMiSSF49998 SSF49998, 1 hit
    SSF54416 SSF54416, 2 hits
    PROSITEiView protein in PROSITE
    PS01164 COPPER_AMINE_OXID_1, 1 hit
    PS01165 COPPER_AMINE_OXID_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		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 nameiAOC3_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: Q16853
    Secondary accession number(s): B2RCI5
    , K7ESB3, L0L8N9, Q45F94
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: April 10, 2019
    This is version 187 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    6. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
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