Skip Header

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

Membrane primary amine oxidase

Gene

AOC3

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

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

Catalytic activityi

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.1 Publication

Cofactori

Protein has several cofactor binding sites:

Kineticsi

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei386Proton acceptorBy similarity1
    Active sitei471Schiff-base intermediate with substrate; via topaquinoneCombined sources1
    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

    GO - Molecular functioni

    • aliphatic-amine oxidase activity Source: UniProtKB-EC
    • aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
    • calcium ion binding Source: UniProtKB
    • copper ion binding Source: UniProtKB
    • phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
    • primary amine oxidase activity Source: UniProtKB
    • protein heterodimerization activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • quinone binding Source: UniProtKB
    • tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC

    GO - Biological processi

    • amine metabolic process Source: UniProtKB
    • cell adhesion Source: UniProtKB
    • inflammatory response Source: UniProtKB
    • response to antibiotic Source: UniProtKB
    • xenobiotic metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Copper, Metal-binding

    Enzyme and pathway databases

    BioCyciZFISH:HS05534-MONOMER.
    BRENDAi1.4.3.21. 2681.
    ReactomeiR-HSA-211945. Phase 1 - Functionalization of compounds.
    SABIO-RKQ16853.

    Names & Taxonomyi

    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
    Gene namesi
    Name:AOC3
    Synonyms:VAP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:550. AOC3.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini2 – 5CytoplasmicSequence analysis4
    Transmembranei6 – 26Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini27 – 763ExtracellularSequence analysisAdd BLAST737

    GO - Cellular componenti

    • cell surface Source: UniProtKB
    • cytoplasm Source: UniProtKB
    • early endosome Source: CACAO
    • endoplasmic reticulum Source: CACAO
    • Golgi apparatus Source: CACAO
    • integral component of membrane Source: UniProtKB
    • microvillus Source: UniProtKB
    • plasma membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    DisGeNETi8639.
    OpenTargetsiENSG00000131471.
    PharmGKBiPA24840.

    Chemistry databases

    ChEMBLiCHEMBL3437.
    DrugBankiDB01275. Hydralazine.
    DB00780. Phenelzine.
    GuidetoPHARMACOLOGYi2767.

    Polymorphism and mutation databases

    DMDMi2501336.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedBy similarity
    ChainiPRO_00000641022 – 763Membrane primary amine oxidaseAdd BLAST762

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi137N-linked (GlcNAc...)Combined sources2 Publications1
    Disulfide bondi198 ↔ 1991 Publication
    Glycosylationi212O-linked (GalNAc...)1 Publication1
    Glycosylationi232N-linked (GlcNAc...)Combined sources1 Publication1
    Glycosylationi294N-linked (GlcNAc...)Combined sources2 Publications1
    Disulfide bondi404 ↔ 430By similarity
    Modified residuei4712',4',5'-topaquinoneCombined sources1
    Glycosylationi592N-linked (GlcNAc...) (complex)Combined sources4 Publications1
    Glycosylationi618N-linked (GlcNAc...)Combined sources3 Publications1
    Glycosylationi666N-linked (GlcNAc...)Combined sources3 Publications1
    Disulfide bondi734 ↔ 7411 Publication
    Disulfide bondi748Interchain1 Publication

    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

    PaxDbiQ16853.
    PeptideAtlasiQ16853.
    PRIDEiQ16853.

    PTM databases

    iPTMnetiQ16853.
    PhosphoSitePlusiQ16853.

    Expressioni

    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

    Inductioni

    Up-regulated during in vitro adipocyte differentiation.1 Publication

    Gene expression databases

    BgeeiENSG00000131471.
    CleanExiHS_AOC3.
    ExpressionAtlasiQ16853. baseline and differential.
    GenevisibleiQ16853. HS.

    Organism-specific databases

    HPAiCAB025797.
    HPA000980.

    Interactioni

    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

    • protein heterodimerization activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi114192. 8 interactors.
    IntActiQ16853. 4 interactors.
    STRINGi9606.ENSP00000312326.

    Chemistry databases

    BindingDBiQ16853.

    Structurei

    Secondary structure

    1763
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi65 – 78Combined sources14
    Beta strandi83 – 85Combined sources3
    Helixi86 – 88Combined sources3
    Beta strandi93 – 102Combined sources10
    Helixi106 – 115Combined sources10
    Beta strandi123 – 130Combined sources8
    Beta strandi132 – 135Combined sources4
    Beta strandi137 – 144Combined sources8
    Beta strandi146 – 148Combined sources3
    Beta strandi151 – 154Combined sources4
    Helixi156 – 160Combined sources5
    Helixi166 – 168Combined sources3
    Helixi173 – 185Combined sources13
    Helixi188 – 191Combined sources4
    Helixi192 – 199Combined sources8
    Turni203 – 206Combined sources4
    Beta strandi208 – 211Combined sources4
    Beta strandi217 – 219Combined sources3
    Beta strandi224 – 231Combined sources8
    Beta strandi234 – 236Combined sources3
    Helixi238 – 240Combined sources3
    Beta strandi242 – 250Combined sources9
    Beta strandi253 – 255Combined sources3
    Helixi256 – 258Combined sources3
    Beta strandi260 – 266Combined sources7
    Beta strandi269 – 272Combined sources4
    Helixi274 – 282Combined sources9
    Turni283 – 285Combined sources3
    Turni298 – 300Combined sources3
    Beta strandi314 – 316Combined sources3
    Beta strandi318 – 320Combined sources3
    Beta strandi322 – 326Combined sources5
    Beta strandi329 – 342Combined sources14
    Turni343 – 345Combined sources3
    Beta strandi346 – 354Combined sources9
    Beta strandi357 – 372Combined sources16
    Helixi377 – 380Combined sources4
    Beta strandi383 – 385Combined sources3
    Helixi386 – 388Combined sources3
    Turni391 – 394Combined sources4
    Turni400 – 402Combined sources3
    Beta strandi408 – 421Combined sources14
    Beta strandi423 – 445Combined sources23
    Beta strandi447 – 449Combined sources3
    Beta strandi451 – 468Combined sources18
    Beta strandi471 – 479Combined sources9
    Turni481 – 483Combined sources3
    Beta strandi485 – 493Combined sources9
    Beta strandi497 – 499Combined sources3
    Beta strandi506 – 512Combined sources7
    Beta strandi515 – 518Combined sources4
    Beta strandi520 – 530Combined sources11
    Beta strandi534 – 551Combined sources18
    Beta strandi554 – 569Combined sources16
    Helixi572 – 575Combined sources4
    Beta strandi577 – 581Combined sources5
    Beta strandi585 – 594Combined sources10
    Beta strandi600 – 608Combined sources9
    Beta strandi617 – 619Combined sources3
    Helixi622 – 629Combined sources8
    Beta strandi630 – 636Combined sources7
    Turni647 – 651Combined sources5
    Beta strandi653 – 655Combined sources3
    Helixi660 – 663Combined sources4
    Beta strandi670 – 684Combined sources15
    Helixi688 – 690Combined sources3
    Beta strandi700 – 713Combined sources14
    Helixi715 – 718Combined sources4
    Beta strandi723 – 729Combined sources7
    Turni734 – 736Combined sources3
    Helixi738 – 741Combined sources4
    Helixi742 – 745Combined sources4

    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...

    Miscellaneous databases

    EvolutionaryTraceiQ16853.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni384 – 394Substrate bindingCombined sourcesAdd BLAST11
    Regioni468 – 473Substrate bindingBy similarity6

    Sequence similaritiesi

    Belongs to the copper/topaquinone oxidase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG1186. Eukaryota.
    COG3733. LUCA.
    GeneTreeiENSGT00510000046461.
    HOGENOMiHOG000233919.
    HOVERGENiHBG004164.
    InParanoidiQ16853.
    KOiK00276.
    OMAiDEGRFNW.
    OrthoDBiEOG091G02WY.
    PhylomeDBiQ16853.
    TreeFamiTF314750.

    Family and domain databases

    Gene3Di2.70.98.20. 1 hit.
    InterProiIPR000269. Cu_amine_oxidase.
    IPR015798. Cu_amine_oxidase_C.
    IPR016182. Cu_amine_oxidase_N-reg.
    IPR015800. Cu_amine_oxidase_N2.
    IPR015802. Cu_amine_oxidase_N3.
    [Graphical view]
    PANTHERiPTHR10638. PTHR10638. 1 hit.
    PfamiPF01179. Cu_amine_oxid. 1 hit.
    PF02727. Cu_amine_oxidN2. 1 hit.
    PF02728. Cu_amine_oxidN3. 1 hit.
    [Graphical view]
    PRINTSiPR00766. CUDAOXIDASE.
    SUPFAMiSSF49998. SSF49998. 1 hit.
    SSF54416. SSF54416. 2 hits.
    PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
    PS01165. COPPER_AMINE_OXID_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    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
    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

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0250355T → R.1 PublicationCorresponds to variant rs33954211dbSNPEnsembl.1
    Natural variantiVAR_05260378R → Q.Corresponds to variant rs402680dbSNPEnsembl.1
    Natural variantiVAR_025027167H → Y.1 PublicationCorresponds to variant rs2228470dbSNPEnsembl.1
    Natural variantiVAR_052604171V → M.Corresponds to variant rs408038dbSNPEnsembl.1
    Natural variantiVAR_052605203H → R.Corresponds to variant rs630079dbSNPEnsembl.1
    Natural variantiVAR_012064317Y → H.Corresponds to variant rs438287dbSNPEnsembl.1
    Natural variantiVAR_024343329R → Q.Corresponds to variant rs2229595dbSNPEnsembl.1
    Natural variantiVAR_025028371I → T.1 PublicationCorresponds to variant rs35097308dbSNPEnsembl.1
    Natural variantiVAR_025029408A → S.1 PublicationCorresponds to variant rs35643019dbSNPEnsembl.1
    Natural variantiVAR_025030426R → H.1 PublicationCorresponds to variant rs33986943dbSNPEnsembl.1
    Natural variantiVAR_025031441R → W.1 PublicationCorresponds to variant rs2229596dbSNPEnsembl.1
    Natural variantiVAR_025032582A → T.1 PublicationCorresponds to variant rs34987927dbSNPEnsembl.1
    Natural variantiVAR_025033700G → S.1 PublicationCorresponds to variant rs477207dbSNPEnsembl.1
    Natural variantiVAR_025034749A → V.1 PublicationCorresponds to variant rs34012919dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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:
    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.

    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]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    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. 8 interactors.
    IntActiQ16853. 4 interactors.
    STRINGi9606.ENSP00000312326.

    Chemistry databases

    BindingDBiQ16853.
    ChEMBLiCHEMBL3437.
    DrugBankiDB01275. Hydralazine.
    DB00780. Phenelzine.
    GuidetoPHARMACOLOGYi2767.

    PTM databases

    iPTMnetiQ16853.
    PhosphoSitePlusiQ16853.

    Polymorphism and mutation databases

    DMDMi2501336.

    Proteomic databases

    PaxDbiQ16853.
    PeptideAtlasiQ16853.
    PRIDEiQ16853.

    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

    CTDi8639.
    DisGeNETi8639.
    GeneCardsiAOC3.
    HGNCiHGNC:550. AOC3.
    HPAiCAB025797.
    HPA000980.
    MIMi603735. gene.
    neXtProtiNX_Q16853.
    OpenTargetsiENSG00000131471.
    PharmGKBiPA24840.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1186. Eukaryota.
    COG3733. LUCA.
    GeneTreeiENSGT00510000046461.
    HOGENOMiHOG000233919.
    HOVERGENiHBG004164.
    InParanoidiQ16853.
    KOiK00276.
    OMAiDEGRFNW.
    OrthoDBiEOG091G02WY.
    PhylomeDBiQ16853.
    TreeFamiTF314750.

    Enzyme and pathway databases

    BioCyciZFISH:HS05534-MONOMER.
    BRENDAi1.4.3.21. 2681.
    ReactomeiR-HSA-211945. Phase 1 - Functionalization of compounds.
    SABIO-RKQ16853.

    Miscellaneous databases

    EvolutionaryTraceiQ16853.
    GeneWikiiAOC3.
    GenomeRNAii8639.
    PROiQ16853.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000131471.
    CleanExiHS_AOC3.
    ExpressionAtlasiQ16853. baseline and differential.
    GenevisibleiQ16853. HS.

    Family and domain databases

    Gene3Di2.70.98.20. 1 hit.
    InterProiIPR000269. Cu_amine_oxidase.
    IPR015798. Cu_amine_oxidase_C.
    IPR016182. Cu_amine_oxidase_N-reg.
    IPR015800. Cu_amine_oxidase_N2.
    IPR015802. Cu_amine_oxidase_N3.
    [Graphical view]
    PANTHERiPTHR10638. PTHR10638. 1 hit.
    PfamiPF01179. Cu_amine_oxid. 1 hit.
    PF02727. Cu_amine_oxidN2. 1 hit.
    PF02728. Cu_amine_oxidN3. 1 hit.
    [Graphical view]
    PRINTSiPR00766. CUDAOXIDASE.
    SUPFAMiSSF49998. SSF49998. 1 hit.
    SSF54416. SSF54416. 2 hits.
    PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
    PS01165. COPPER_AMINE_OXID_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAOC3_HUMAN
    AccessioniPrimary (citable) accession number: Q16853
    Secondary accession number(s): B2RCI5
    , K7ESB3, L0L8N9, Q45F94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: November 30, 2016
    This is version 170 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    Similar proteinsi

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