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Protein

Retina-specific copper amine oxidase

Gene

AOC2

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

Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina.2 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=0.056 mM for tryptamine1 Publication
  2. KM=0.077 mM for 2-phenylethylamine1 Publication
  3. KM=0.167 mM for benzylamine1 Publication
  4. KM=0.178 mM for p-tyramine1 Publication
  5. KM=1.7 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 sitei380Proton acceptorBy similarity1
    Active sitei465Schiff-base intermediate with substrate; via topaquinoneBy similarity1
    <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 bindingi516Copper; via tele nitrogenBy similarity1
    Metal bindingi518Copper; via tele nitrogenBy similarity1
    Metal bindingi525Calcium 1By similarity1
    Metal bindingi526Calcium 1; via carbonyl oxygenBy similarity1
    Metal bindingi527Calcium 1By similarity1
    Metal bindingi568Calcium 2By similarity1
    Metal bindingi659Calcium 2; via carbonyl oxygenBy similarity1
    Metal bindingi661Calcium 2By similarity1
    Metal bindingi663Calcium 2By similarity1
    Metal bindingi669Calcium 1By similarity1
    Metal bindingi670Calcium 1; via carbonyl oxygenBy similarity1
    Metal bindingi680Copper; via pros nitrogenBy similarity1

    <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

    GO - Biological processi

    <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
    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
    O75106

    <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:
    Retina-specific copper amine oxidase (EC:1.4.3.21By similarity)
    Short name:
    RAO
    Alternative name(s):
    Amine oxidase [copper-containing]
    Semicarbazide-sensitive amine oxidase
    Short name:
    SSAO
    <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:AOC2
    <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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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:ENSG00000131480.8

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:549 AOC2

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    602268 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_O75106

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, 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

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    314

    Open Targets

    More...
    OpenTargetsi
    ENSG00000131480

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA24839

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4112

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    AOC2

    <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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 32Sequence analysisAdd BLAST32
    <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_000003567133 – 756Retina-specific copper amine oxidaseAdd BLAST724

    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>Glycosylationi133N-linked (GlcNAc...) asparagineBy similarity1
    Glycosylationi198N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi226N-linked (GlcNAc...) asparagineBy similarity1
    <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 bondi398 ↔ 424By 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 residuei4652',4',5'-topaquinoneBy similarity1
    Glycosylationi588N-linked (GlcNAc...) (complex) asparagineBy similarity1
    Glycosylationi662N-linked (GlcNAc...) asparagineBy similarity1
    Disulfide bondi730 ↔ 737By similarity
    Disulfide bondi744InterchainBy similarity

    <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.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, TPQ

    Proteomic databases

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

    More...
    PaxDbi
    O75106

    PeptideAtlas

    More...
    PeptideAtlasi
    O75106

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O75106

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    49761
    49762 [O75106-2]

    PTM databases

    GlyConnect protein glycosylation platform

    More...
    GlyConnecti
    1714

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    O75106

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

    More...
    PhosphoSitePlusi
    O75106

    <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

    Expressed in many tissues with much higher expression in retina. Isoform 1 and isoform 2 are expressed in adipose tissue, whereas isoform 1 only seems to be present in thymus, and isoform 2 only in testis.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
    ENSG00000131480 Expressed in 97 organ(s), highest expression level in blood

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_AOC2

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    O75106 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA057779

    <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 (By similarity). Forms a heterodimer with AOC3, in vitro.By similarity1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    106811, 6 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    O75106, 2 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000253799

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    O75106

    <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

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    O75106

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

    More...
    SMRi
    O75106

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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>Regioni378 – 388Substrate bindingBy similarityAdd BLAST11
    Regioni462 – 467Substrate bindingBy similarity6
    Regioni574 – 581Heparin-bindingBy similarity8

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1186 Eukaryota
    COG3733 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000153738

    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
    O75106

    KEGG Orthology (KO)

    More...
    KOi
    K00276

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NANWARY

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G02WY

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    O75106

    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
    IPR032952 AOC2
    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
    PTHR10638:SF4 PTHR10638:SF4, 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 (2)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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
    Note: Additional isoforms seem to exist.
    Isoform 1 (identifier: O75106-1) [UniParc]FASTAAdd to basket
    Also known as: Long

    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
    MHLKIVLAFL ALSLITIFAL AYVLLTSPGG SSQPPHCPSV SHRAQPWPHP
    60 70 80 90 100
    GQSQLFADLS REELTAVMRF LTQRLGPGLV DAAQAQPSDN CIFSVELQLP
    110 120 130 140 150
    PKAAALAHLD RGSPPPAREA LAIVLFGGQP QPNVSELVVG PLPHPSYMRD
    160 170 180 190 200
    VTVERHGGPL PYHRRPVLRA EFTQMWRHLK EVELPKAPIF LSSTFNYNGS
    210 220 230 240 250
    TLAAVHATPR GLRSGDRATW MALYHNISGV GLFLHPVGLE LLLDHRALDP
    260 270 280 290 300
    AHWTVQQVFY LGHYYADLGQ LEREFKSGRL EVVRVPLPPP NGASSLRSRN
    310 320 330 340 350
    SPGPLPPLQF SPQGSQYSVQ GNLVVSSLWS FTFGHGVFSG LRIFDVRFQG
    360 370 380 390 400
    ERIAYEVSVQ ECVSIYGADS PKTMLTRYLD SSFGLGRNSR GLVRGVDCPY
    410 420 430 440 450
    QATMVDIHIL VGKGAVQLLP GAVCVFEEAQ GLPLRRHHNY LQNHFYGGLA
    460 470 480 490 500
    SSALVVRSVS SVGNYDYIWD FVLYPNGALE GRVHATGYIN TAFLKGGEEG
    510 520 530 540 550
    LLFGNRVGER VLGTVHTHAF HFKLDLDVAG LKNWVVAEDV VFKPVAAPWN
    560 570 580 590 600
    PEHWLQRPQL TRQVLGKEDL TAFSLGSPLP RYLYLASNQT NAWGHQRGYR
    610 620 630 640 650
    IQIHSPLGIH IPLESDMERA LSWGRYQLVV TQRKEEESQS SSIYHQNDIW
    660 670 680 690 700
    TPTVTFADFI NNETLLGEDL VAWVTASFLH IPHAEDIPNT VTLGNRVGFL
    710 720 730 740 750
    LRPYNFFDED PSIFSPGSVY FEKGQDAGLC SINPVACLPD LAACVPDLPP

    FSYHGF
    Length:756
    Mass (Da):83,673
    Last modified:January 24, 2006 - v2
    <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:i10263D8D56D3BD25
    GO
    Isoform 2 (identifier: O75106-2) [UniParc]FASTAAdd to basket
    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         599-625: Missing.

    Show »
    Length:729
    Mass (Da):80,516
    Checksum:i5F28CCC8EE353415
    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 conflicti181E → D (PubMed:9119395).Curated1
    Sequence conflicti181E → D (PubMed:9722954).Curated1
    Sequence conflicti215 – 218GDRA → RERT (PubMed:9119395).Curated4
    Sequence conflicti215 – 218GDRA → RERT (PubMed:9722954).Curated4
    Sequence conflicti221 – 222MA → IG (PubMed:9119395).Curated2
    Sequence conflicti610H → Q (PubMed:9119395).Curated1
    Sequence conflicti610H → Q (PubMed:9722954).Curated1

    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_0250225I → V1 PublicationCorresponds to variant dbSNP:rs34230945Ensembl.1
    Natural variantiVAR_02502322Y → C1 PublicationCorresponds to variant dbSNP:rs34435306Ensembl.1
    Natural variantiVAR_025024141P → L1 PublicationCorresponds to variant dbSNP:rs35833794Ensembl.1
    Natural variantiVAR_025025273R → Q1 PublicationCorresponds to variant dbSNP:rs35508987Ensembl.1
    Natural variantiVAR_025026427E → D1 PublicationCorresponds to variant dbSNP:rs34351794Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006549599 – 625Missing in isoform 2. 1 PublicationAdd BLAST27

    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
    D88213 mRNA Translation: BAA19001.1
    AB012943 Genomic DNA Translation: BAA32590.1
    AB012943 Genomic DNA Translation: BAA32589.1
    AF081363 mRNA Translation: AAD39345.1
    DQ060035 Genomic DNA Translation: AAY43129.1
    AC016889 Genomic DNA No translation available.
    CH471152 Genomic DNA Translation: EAW60895.1
    BC142641 mRNA Translation: AAI42642.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS11443.1 [O75106-1]
    CCDS45690.1 [O75106-2]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001149.2, NM_001158.4 [O75106-2]
    NP_033720.2, NM_009590.3 [O75106-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.143102

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000253799; ENSP00000253799; ENSG00000131480 [O75106-1]
    ENST00000452774; ENSP00000406134; ENSG00000131480 [O75106-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    314

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:314

    UCSC genome browser

    More...
    UCSCi
    uc002ibt.5 human [O75106-1]

    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
    D88213 mRNA Translation: BAA19001.1
    AB012943 Genomic DNA Translation: BAA32590.1
    AB012943 Genomic DNA Translation: BAA32589.1
    AF081363 mRNA Translation: AAD39345.1
    DQ060035 Genomic DNA Translation: AAY43129.1
    AC016889 Genomic DNA No translation available.
    CH471152 Genomic DNA Translation: EAW60895.1
    BC142641 mRNA Translation: AAI42642.1
    CCDSiCCDS11443.1 [O75106-1]
    CCDS45690.1 [O75106-2]
    RefSeqiNP_001149.2, NM_001158.4 [O75106-2]
    NP_033720.2, NM_009590.3 [O75106-1]
    UniGeneiHs.143102

    3D structure databases

    ProteinModelPortaliO75106
    SMRiO75106
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi106811, 6 interactors
    IntActiO75106, 2 interactors
    STRINGi9606.ENSP00000253799

    Chemistry databases

    BindingDBiO75106
    ChEMBLiCHEMBL4112

    PTM databases

    GlyConnecti1714
    iPTMnetiO75106
    PhosphoSitePlusiO75106

    Polymorphism and mutation databases

    BioMutaiAOC2

    Proteomic databases

    PaxDbiO75106
    PeptideAtlasiO75106
    PRIDEiO75106
    ProteomicsDBi49761
    49762 [O75106-2]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000253799; ENSP00000253799; ENSG00000131480 [O75106-1]
    ENST00000452774; ENSP00000406134; ENSG00000131480 [O75106-2]
    GeneIDi314
    KEGGihsa:314
    UCSCiuc002ibt.5 human [O75106-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    314
    DisGeNETi314
    EuPathDBiHostDB:ENSG00000131480.8

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    AOC2
    HGNCiHGNC:549 AOC2
    HPAiHPA057779
    MIMi602268 gene
    neXtProtiNX_O75106
    OpenTargetsiENSG00000131480
    PharmGKBiPA24839

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1186 Eukaryota
    COG3733 LUCA
    GeneTreeiENSGT00940000153738
    HOGENOMiHOG000233919
    HOVERGENiHBG004164
    InParanoidiO75106
    KOiK00276
    OMAiNANWARY
    OrthoDBiEOG091G02WY
    PhylomeDBiO75106
    TreeFamiTF314750

    Enzyme and pathway databases

    BRENDAi1.4.3.21 2681
    ReactomeiR-HSA-211945 Phase I - Functionalization of compounds
    SABIO-RKiO75106

    Miscellaneous databases

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

    More...
    GenomeRNAii
    314

    Protein Ontology

    More...
    PROi
    PR:O75106

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000131480 Expressed in 97 organ(s), highest expression level in blood
    CleanExiHS_AOC2
    GenevisibleiO75106 HS

    Family and domain databases

    Gene3Di2.70.98.20, 1 hit
    InterProiView protein in InterPro
    IPR032952 AOC2
    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
    PTHR10638:SF4 PTHR10638:SF4, 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 nameiAOC2_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: O75106
    Secondary accession number(s): A5PKW2
    , O00120, O75105, Q4TTW5, Q9UNY0
    <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: July 15, 1999
    Last sequence update: January 24, 2006
    Last modified: December 5, 2018
    This is version 159 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    UniProt is an ELIXIR core data resource
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