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Q16853

- AOC3_HUMAN

UniProt

Q16853 - AOC3_HUMAN

Protein

Membrane primary amine oxidase

Gene

AOC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.

    Cofactori

    Binds 1 copper ion per subunit.
    Binds 2 calcium ions per subunit.
    Contains 1 topaquinone per subunit.

    Kineticsi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei386 – 3861Proton acceptorBy similarity
    Active sitei471 – 4711Schiff-base intermediate with substrate; via topaquinoneBy similarity
    Metal bindingi520 – 5201Copper1 Publication
    Metal bindingi522 – 5221Copper1 Publication
    Metal bindingi529 – 5291Calcium 1
    Metal bindingi530 – 5301Calcium 1; via carbonyl oxygen
    Metal bindingi531 – 5311Calcium 1
    Metal bindingi572 – 5721Calcium 2
    Metal bindingi638 – 6381Calcium 2
    Metal bindingi663 – 6631Calcium 2; via carbonyl oxygen
    Metal bindingi665 – 6651Calcium 2
    Metal bindingi667 – 6671Calcium 2
    Metal bindingi673 – 6731Calcium 1
    Metal bindingi674 – 6741Calcium 1; via carbonyl oxygen
    Metal bindingi684 – 6841Copper1 Publication

    GO - Molecular functioni

    1. aliphatic-amine oxidase activity Source: UniProtKB-EC
    2. aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
    3. calcium ion binding Source: UniProtKB
    4. cation channel activity Source: UniProtKB
    5. copper ion binding Source: UniProtKB
    6. phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
    7. primary amine oxidase activity Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein heterodimerization activity Source: UniProtKB
    10. protein homodimerization activity Source: UniProtKB
    11. quinone binding Source: UniProtKB
    12. tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC

    GO - Biological processi

    1. amine metabolic process Source: UniProtKB
    2. cation transport Source: GOC
    3. cell adhesion Source: UniProtKB
    4. inflammatory response Source: UniProtKB
    5. response to antibiotic Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Copper, Metal-binding

    Enzyme and pathway databases

    SABIO-RKQ16853.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Membrane primary amine oxidase (EC:1.4.3.21)
    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
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:550. AOC3.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. integral component of membrane Source: UniProtKB
    4. microvillus Source: UniProtKB
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2111M → V: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with N-394 and G-469. 1 Publication
    Mutagenesisi394 – 3941Y → N: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and G-469. 1 Publication
    Mutagenesisi469 – 4691L → G: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and N-394. 1 Publication

    Organism-specific databases

    PharmGKBiPA24840.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 763762Membrane primary amine oxidasePRO_0000064102Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi137 – 1371N-linked (GlcNAc...)2 Publications
    Disulfide bondi198 ↔ 1991 Publication
    Glycosylationi212 – 2121O-linked (GalNAc...)1 Publication
    Glycosylationi232 – 2321N-linked (GlcNAc...)1 Publication
    Glycosylationi294 – 2941N-linked (GlcNAc...)2 Publications
    Modified residuei471 – 47112',4',5'-topaquinone
    Glycosylationi592 – 5921N-linked (GlcNAc...) (complex)4 Publications
    Glycosylationi618 – 6181N-linked (GlcNAc...)3 Publications
    Glycosylationi666 – 6661N-linked (GlcNAc...)3 Publications
    Disulfide bondi734 ↔ 7411 Publication
    Disulfide bondi748 – 748Interchain1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, TPQ

    Proteomic databases

    PaxDbiQ16853.
    PeptideAtlasiQ16853.
    PRIDEiQ16853.

    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

    ArrayExpressiQ16853.
    BgeeiQ16853.
    CleanExiHS_AOC3.
    GenevestigatoriQ16853.

    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

    Protein-protein interaction databases

    BioGridi114192. 2 interactions.
    IntActiQ16853. 2 interactions.
    STRINGi9606.ENSP00000312326.

    Structurei

    Secondary structure

    1
    763
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi65 – 7814
    Beta strandi83 – 853
    Helixi86 – 883
    Beta strandi93 – 10210
    Helixi106 – 11510
    Beta strandi123 – 1308
    Beta strandi132 – 1354
    Beta strandi137 – 1448
    Beta strandi146 – 1483
    Beta strandi151 – 1544
    Helixi156 – 1605
    Helixi166 – 1683
    Helixi173 – 18513
    Helixi188 – 1914
    Helixi192 – 1998
    Turni203 – 2064
    Beta strandi208 – 2114
    Beta strandi217 – 2193
    Beta strandi224 – 2318
    Beta strandi234 – 2363
    Helixi238 – 2403
    Beta strandi242 – 2509
    Beta strandi253 – 2553
    Helixi256 – 2583
    Beta strandi260 – 2667
    Beta strandi269 – 2724
    Helixi274 – 2829
    Turni283 – 2853
    Turni298 – 3003
    Beta strandi314 – 3163
    Beta strandi318 – 3203
    Beta strandi322 – 3265
    Beta strandi329 – 34214
    Turni343 – 3453
    Beta strandi346 – 3549
    Beta strandi357 – 37216
    Helixi377 – 3804
    Beta strandi383 – 3853
    Helixi386 – 3883
    Turni391 – 3944
    Turni400 – 4023
    Beta strandi408 – 42114
    Beta strandi423 – 44523
    Beta strandi447 – 4493
    Beta strandi451 – 46818
    Beta strandi471 – 4799
    Turni481 – 4833
    Beta strandi485 – 4939
    Beta strandi497 – 4993
    Beta strandi506 – 5127
    Beta strandi515 – 5184
    Beta strandi520 – 53011
    Beta strandi534 – 55118
    Beta strandi554 – 56916
    Helixi572 – 5754
    Beta strandi577 – 5815
    Beta strandi585 – 59410
    Beta strandi600 – 6089
    Beta strandi617 – 6193
    Helixi622 – 6298
    Beta strandi630 – 6367
    Turni647 – 6515
    Beta strandi653 – 6553
    Helixi660 – 6634
    Beta strandi670 – 68415
    Helixi688 – 6903
    Beta strandi700 – 71314
    Helixi715 – 7184
    Beta strandi723 – 7297
    Turni734 – 7363
    Helixi738 – 7414
    Helixi742 – 7454

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 58-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16853.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 54CytoplasmicSequence Analysis
    Topological domaini27 – 763737ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei6 – 2621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the copper/topaquinone oxidase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3733.
    HOGENOMiHOG000233919.
    HOVERGENiHBG004164.
    InParanoidiQ16853.
    KOiK00276.
    OMAiSWERYQL.
    OrthoDBiEOG7353W8.
    PhylomeDBiQ16853.
    TreeFamiTF314750.

    Family and domain databases

    Gene3Di2.70.98.20. 1 hit.
    3.10.450.40. 2 hits.
    InterProiIPR000269. Cu_amine_oxidase.
    IPR015798. Cu_amine_oxidase_C.
    IPR016182. Cu_amine_oxidase_N-reg.
    IPR015800. Cu_amine_oxidase_N2.
    IPR015801. Cu_amine_oxidase_N2/3.
    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. Align

    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

    MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSVSPSAQP    50
    WTHPGQSQLF ADLSREELTA VMRFLTQRLG PGLVDAAQAR PSDNCVFSVE 100
    LQLPPKAAAL AHLDRGSPPP AREALAIVFF GRQPQPNVSE LVVGPLPHPS 150
    YMRDVTVERH GGPLPYHRRP VLFQEYLDID QMIFNRELPQ ASGLLHHCCF 200
    YKHRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL HHVGLELLVN 250
    HKALDPARWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW 300
    SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF 350
    DVRFQGERLV YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYTTPLTR 400
    GVDCPYLATY VDWHFLLESQ APKTIRDAFC VFEQNQGLPL RRHHSDLYSH 450
    YFGGLAETVL VVRSMSTLLN YDYVWDTVFH PSGAIEIRFY ATGYISSAFL 500
    FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DVAGLENWVW AEDMVFVPMA 550
    VPWSPEHQLQ RLQVTRKLLE MEEQAAFLVG SATPRYLYLA SNHSNKWGHP 600
    RGYRIQMLSF AGEPLPQNSS MARGFSWERY QLAVTQRKEE EPSSSSVFNQ 650
    NDPWAPTVDF SDFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG 700
    VGFFLRPYNF FDEDPSFYSA DSIYFRGDQD AGACEVNPLA CLPQAAACAP 750
    DLPAFSHGGF SHN 763
    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51T → R.1 Publication
    Corresponds to variant rs33954211 [ dbSNP | Ensembl ].
    VAR_025035
    Natural varianti78 – 781R → Q.
    Corresponds to variant rs402680 [ dbSNP | Ensembl ].
    VAR_052603
    Natural varianti167 – 1671H → Y.1 Publication
    Corresponds to variant rs2228470 [ dbSNP | Ensembl ].
    VAR_025027
    Natural varianti171 – 1711V → M.
    Corresponds to variant rs408038 [ dbSNP | Ensembl ].
    VAR_052604
    Natural varianti203 – 2031H → R.
    Corresponds to variant rs630079 [ dbSNP | Ensembl ].
    VAR_052605
    Natural varianti317 – 3171Y → H.
    Corresponds to variant rs438287 [ dbSNP | Ensembl ].
    VAR_012064
    Natural varianti329 – 3291R → Q.
    Corresponds to variant rs2229595 [ dbSNP | Ensembl ].
    VAR_024343
    Natural varianti371 – 3711I → T.1 Publication
    Corresponds to variant rs35097308 [ dbSNP | Ensembl ].
    VAR_025028
    Natural varianti408 – 4081A → S.1 Publication
    Corresponds to variant rs35643019 [ dbSNP | Ensembl ].
    VAR_025029
    Natural varianti426 – 4261R → H.1 Publication
    Corresponds to variant rs33986943 [ dbSNP | Ensembl ].
    VAR_025030
    Natural varianti441 – 4411R → W.1 Publication
    Corresponds to variant rs2229596 [ dbSNP | Ensembl ].
    VAR_025031
    Natural varianti582 – 5821A → T.1 Publication
    Corresponds to variant rs34987927 [ dbSNP | Ensembl ].
    VAR_025032
    Natural varianti700 – 7001G → S.1 Publication
    Corresponds to variant rs477207 [ dbSNP | Ensembl ].
    VAR_025033
    Natural varianti749 – 7491A → V.1 Publication
    Corresponds to variant rs34012919 [ dbSNP | Ensembl ].
    VAR_025034

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 543543Missing in isoform 3. 1 PublicationVSP_055201Add
    BLAST
    Alternative sequencei630 – 6345YQLAV → IWWPG in isoform 2. 1 PublicationVSP_053751
    Alternative sequencei635 – 763129Missing in isoform 2. 1 PublicationVSP_053752Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    PIRiJC5234.
    RefSeqiNP_001264660.1. NM_001277731.1. [Q16853-2]
    NP_001264661.1. NM_001277732.1.
    NP_003725.1. NM_003734.3. [Q16853-1]
    UniGeneiHs.198241.

    Genome annotation databases

    EnsembliENST00000308423; ENSP00000312326; ENSG00000131471. [Q16853-1]
    ENST00000591562; ENSP00000468632; ENSG00000131471. [Q16853-3]
    GeneIDi8639.
    KEGGihsa:8639.
    UCSCiuc002ibv.4. human. [Q16853-1]

    Polymorphism databases

    DMDMi2501336.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11444.1. [Q16853-1 ]
    CCDS62198.1. [Q16853-3 ]
    PIRi JC5234.
    RefSeqi NP_001264660.1. NM_001277731.1. [Q16853-2 ]
    NP_001264661.1. NM_001277732.1.
    NP_003725.1. NM_003734.3. [Q16853-1 ]
    UniGenei Hs.198241.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PU4 X-ray 3.20 A/B 1-763 [» ]
    1US1 X-ray 2.90 A/B 1-763 [» ]
    2C10 X-ray 2.50 A/B/C/D 29-763 [» ]
    2C11 X-ray 2.90 A/B/C/D 29-763 [» ]
    2Y73 X-ray 2.60 A/B 1-763 [» ]
    2Y74 X-ray 2.95 A/B 1-763 [» ]
    3ALA X-ray 2.90 A/B/C/D/E/F/G 33-763 [» ]
    4BTW X-ray 2.80 A/B 27-763 [» ]
    4BTX X-ray 2.78 A/B 27-763 [» ]
    4BTY X-ray 3.10 A/B 27-763 [» ]
    ProteinModelPortali Q16853.
    SMRi Q16853. Positions 58-761.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114192. 2 interactions.
    IntActi Q16853. 2 interactions.
    STRINGi 9606.ENSP00000312326.

    Chemistry

    BindingDBi Q16853.
    ChEMBLi CHEMBL3437.
    DrugBanki DB01275. Hydralazine.
    DB00780. Phenelzine.
    GuidetoPHARMACOLOGYi 2767.

    Polymorphism databases

    DMDMi 2501336.

    Proteomic databases

    PaxDbi Q16853.
    PeptideAtlasi Q16853.
    PRIDEi Q16853.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308423 ; ENSP00000312326 ; ENSG00000131471 . [Q16853-1 ]
    ENST00000591562 ; ENSP00000468632 ; ENSG00000131471 . [Q16853-3 ]
    GeneIDi 8639.
    KEGGi hsa:8639.
    UCSCi uc002ibv.4. human. [Q16853-1 ]

    Organism-specific databases

    CTDi 8639.
    GeneCardsi GC17P041003.
    HGNCi HGNC:550. AOC3.
    HPAi CAB025797.
    HPA000980.
    MIMi 603735. gene.
    neXtProti NX_Q16853.
    PharmGKBi PA24840.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3733.
    HOGENOMi HOG000233919.
    HOVERGENi HBG004164.
    InParanoidi Q16853.
    KOi K00276.
    OMAi SWERYQL.
    OrthoDBi EOG7353W8.
    PhylomeDBi Q16853.
    TreeFami TF314750.

    Enzyme and pathway databases

    SABIO-RK Q16853.

    Miscellaneous databases

    EvolutionaryTracei Q16853.
    GeneWikii AOC3.
    GenomeRNAii 8639.
    NextBioi 32389.
    PROi Q16853.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16853.
    Bgeei Q16853.
    CleanExi HS_AOC3.
    Genevestigatori Q16853.

    Family and domain databases

    Gene3Di 2.70.98.20. 1 hit.
    3.10.450.40. 2 hits.
    InterProi IPR000269. Cu_amine_oxidase.
    IPR015798. Cu_amine_oxidase_C.
    IPR016182. Cu_amine_oxidase_N-reg.
    IPR015800. Cu_amine_oxidase_N2.
    IPR015801. Cu_amine_oxidase_N2/3.
    IPR015802. Cu_amine_oxidase_N3.
    [Graphical view ]
    PANTHERi PTHR10638. PTHR10638. 1 hit.
    Pfami PF01179. Cu_amine_oxid. 1 hit.
    PF02727. Cu_amine_oxidN2. 1 hit.
    PF02728. Cu_amine_oxidN3. 1 hit.
    [Graphical view ]
    PRINTSi PR00766. CUDAOXIDASE.
    SUPFAMi SSF49998. SSF49998. 1 hit.
    SSF54416. SSF54416. 2 hits.
    PROSITEi PS01164. COPPER_AMINE_OXID_1. 1 hit.
    PS01165. COPPER_AMINE_OXID_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a copper-containing, topaquinone-containing monoamine oxidase from human placenta."
      Zhang X., McIntire W.S.
      Gene 179:279-286(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule."
      Smith D.J., Salmi M., Bono P., Hellman J., Leu T., Jalkanen S.
      J. Exp. Med. 188:17-27(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Lung.
    3. "Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina."
      Zhang Q., Mashima Y., Noda S., Imamura Y., Kudoh J., Shimizu N., Nishiyama T., Umeda S., Oguchi Y., Tanaka Y., Iwata T.
      Gene 318:45-53(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Functional modulation of vascular adhesion protein-1 by a novel splice variant."
      Kaitaniemi S., Gron K., Elovaara H., Salmi M., Jalkanen S., Elima K.
      PLoS ONE 8:E54151-E54151(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Placenta.
    6. NIEHS SNPs program
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-5; TYR-167; THR-371; SER-408; HIS-426; TRP-441; THR-582; SER-700 AND VAL-749.
    7. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: PNS.
    9. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
      Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
      Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 79-90 AND 123-132.
      Tissue: Adipocyte.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-592; ASN-618 AND ASN-666.
      Tissue: Plasma.
    11. "Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes."
      Bour S., Daviaud D., Gres S., Lefort C., Prevot D., Zorzano A., Wabitsch M., Saulnier-Blache J.-S., Valet P., Carpene C.
      Biochimie 89:916-925(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    12. "The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase."
      Kaitaniemi S., Elovaara H., Groen K., Kidron H., Liukkonen J., Salminen T., Salmi M., Jalkanen S., Elima K.
      Cell. Mol. Life Sci. 66:2743-2757(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF MET-211; TYR-394 AND LEU-469.
    13. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137; ASN-294; ASN-592; ASN-618 AND ASN-666.
      Tissue: Liver.
    14. Cited for: GLYCOSYLATION AT ASN-592.
    15. "Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications."
      Airenne T.T., Nymalm Y., Kidron H., Smith D.J., Pihlavisto M., Salmi M., Jalkanen S., Johnson M.S., Salminen T.A.
      Protein Sci. 14:1964-1974(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH COPPER AND CALCIUM IONS, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.

    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: October 1, 2014
    This is version 151 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

    External Data

    Dasty 3