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P19801

- AOC1_HUMAN

UniProt

P19801 - AOC1_HUMAN

Protein

Amiloride-sensitive amine oxidase [copper-containing]

Gene

AOC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 4 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function.

    Catalytic activityi

    Histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei373 – 3731Proton acceptor1 Publication
    Active sitei461 – 4611Schiff-base intermediate with substrate; via topaquinone1 Publication
    Metal bindingi510 – 5101Copper
    Metal bindingi512 – 5121Copper
    Metal bindingi519 – 5191Calcium 1
    Metal bindingi520 – 5201Calcium 1; via carbonyl oxygen
    Metal bindingi521 – 5211Calcium 1
    Metal bindingi562 – 5621Calcium 2
    Metal bindingi653 – 6531Calcium 2; via carbonyl oxygen
    Metal bindingi656 – 6561Calcium 2
    Metal bindingi658 – 6581Calcium 2
    Metal bindingi664 – 6641Calcium 1
    Metal bindingi665 – 6651Calcium 1; via carbonyl oxygen
    Metal bindingi675 – 6751Copper

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. cation channel activity Source: UniProtKB
    3. copper ion binding Source: UniProtKB
    4. diamine oxidase activity Source: UniProtKB
    5. drug binding Source: UniProtKB
    6. heparin binding Source: UniProtKB
    7. histamine oxidase activity Source: UniProtKB-EC
    8. methylputrescine oxidase activity Source: UniProtKB-EC
    9. primary amine oxidase activity Source: UniProtKB
    10. propane-1,3-diamine oxidase activity Source: UniProtKB-EC
    11. protein complex binding Source: UniProtKB
    12. protein homodimerization activity Source: UniProtKB
    13. quinone binding Source: UniProtKB
    14. receptor activity Source: UniProtKB
    15. sodium channel activity Source: UniProtKB
    16. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. amine metabolic process Source: InterPro
    2. cellular response to azide Source: UniProtKB
    3. cellular response to copper ion Source: UniProtKB
    4. cellular response to copper ion starvation Source: UniProtKB
    5. cellular response to heparin Source: UniProtKB
    6. cellular response to histamine Source: UniProtKB
    7. oxidation-reduction process Source: UniProtKB
    8. response to antibiotic Source: UniProtKB
    9. response to drug Source: UniProtKB
    10. sodium ion transmembrane transport Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Calcium, Copper, Heparin-binding, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00083-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amiloride-sensitive amine oxidase [copper-containing] (EC:1.4.3.22)
    Short name:
    DAO
    Short name:
    Diamine oxidase
    Alternative name(s):
    Amiloride-binding protein 1
    Amine oxidase copper domain-containing protein 1
    Histaminase
    Kidney amine oxidase
    Short name:
    KAO
    Gene namesi
    Name:AOC1
    Synonyms:ABP1, DAO1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:80. AOC1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProtKB
    3. peroxisome Source: UniProtKB
    4. plasma membrane Source: UniProtKB
    5. tight junction Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24416.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 751732Amiloride-sensitive amine oxidase [copper-containing]PRO_0000035666Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi110 – 1101N-linked (GlcNAc...)1 Publication
    Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi177 ↔ 1811 Publication
    Disulfide bondi391 ↔ 4171 Publication
    Modified residuei461 – 46112',4',5'-topaquinone
    Glycosylationi538 – 5381N-linked (GlcNAc...)1 Publication
    Disulfide bondi736 – 736Interchain1 Publication
    Glycosylationi745 – 7451N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, TPQ

    Proteomic databases

    PaxDbiP19801.
    PRIDEiP19801.

    PTM databases

    PhosphoSiteiP19801.

    Expressioni

    Tissue specificityi

    Placenta and kidney.

    Gene expression databases

    ArrayExpressiP19801.
    BgeeiP19801.
    CleanExiHS_ABP1.
    GenevestigatoriP19801.

    Organism-specific databases

    HPAiHPA031032.
    HPA031033.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000354193.

    Structurei

    Secondary structure

    1
    751
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi29 – 335
    Helixi38 – 4912
    Helixi52 – 543
    Beta strandi64 – 7512
    Helixi79 – 8810
    Beta strandi96 – 1038
    Beta strandi105 – 1084
    Beta strandi110 – 1178
    Beta strandi119 – 1213
    Beta strandi124 – 1296
    Helixi137 – 1404
    Helixi145 – 15814
    Helixi160 – 1623
    Helixi163 – 1708
    Beta strandi173 – 1764
    Beta strandi178 – 1869
    Beta strandi191 – 1933
    Beta strandi198 – 2058
    Helixi210 – 2123
    Beta strandi214 – 2229
    Beta strandi225 – 2273
    Helixi228 – 2303
    Beta strandi232 – 2387
    Helixi246 – 2549
    Beta strandi301 – 3033
    Beta strandi309 – 3135
    Beta strandi316 – 3205
    Beta strandi322 – 3298
    Turni330 – 3323
    Beta strandi333 – 3419
    Beta strandi344 – 35916
    Helixi364 – 3685
    Beta strandi370 – 3723
    Helixi373 – 3764
    Helixi378 – 3803
    Turni387 – 3893
    Beta strandi395 – 40511
    Beta strandi410 – 42213
    Beta strandi427 – 4337
    Beta strandi435 – 44511
    Beta strandi448 – 4569
    Beta strandi458 – 46912
    Beta strandi475 – 4839
    Beta strandi487 – 4893
    Helixi492 – 4965
    Beta strandi497 – 5026
    Beta strandi505 – 5084
    Beta strandi510 – 52011
    Beta strandi524 – 54017
    Beta strandi547 – 55913
    Helixi562 – 5654
    Beta strandi569 – 5713
    Beta strandi575 – 58410
    Beta strandi590 – 5989
    Helixi610 – 61910
    Beta strandi621 – 6266
    Helixi629 – 6313
    Turni637 – 6415
    Beta strandi643 – 6453
    Helixi652 – 6554
    Beta strandi661 – 67515
    Helixi679 – 6813
    Beta strandi691 – 70414
    Helixi706 – 7094
    Beta strandi714 – 7174
    Beta strandi720 – 7234
    Beta strandi725 – 7273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HI7X-ray1.80A/B21-751[»]
    3HIGX-ray2.09A/B21-751[»]
    3HIIX-ray2.15A/B21-751[»]
    3K5TX-ray2.11A21-751[»]
    3MPHX-ray2.05A/B21-751[»]
    ProteinModelPortaliP19801.
    SMRiP19801. Positions 27-751.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19801.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni568 – 5758Heparin-bindingBy similarity

    Sequence similaritiesi

    Belongs to the copper/topaquinone oxidase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3733.
    HOGENOMiHOG000233919.
    HOVERGENiHBG004164.
    InParanoidiP19801.
    KOiK11182.
    OrthoDBiEOG78WKR2.
    PhylomeDBiP19801.
    TreeFamiTF314750.

    Family and domain databases

    Gene3Di2.70.98.20. 1 hit.
    3.10.450.40. 1 hit.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P19801-1) [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

    MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS    50
    KKELRLQPSS TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV 100
    IFFGDQEHPN VTEFAVGPLP GPCYMRALSP RPGYQSSWAS RPISTAEYAL 150
    LYHTLQEATK PLHQFFLNTT GFSFQDCHDR CLAFTDVAPR GVASGQRRSW 200
    LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG KFYGSPEELA 250
    RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP 300
    RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV 350
    SVQEAVALYG GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT 400
    FHYYDADDPV HYPRALCLFE MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL 450
    VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH ATGYVHATFY TPEGLRHGTR 500
    LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT NPWSPRHRVV 550
    QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM 600
    ADQVLPPGWQ EEQAITWARY PLAVTKYRES ELCSSSIYHQ NDPWHPPVVF 650
    EQFLHNNENI ENEDLVAWVT VGFLHIPHSE DIPNTATPGN SVGFLLRPFN 700
    FFPEDPSLAS RDTVIVWPRD NGPNYVQRWI PEDRDCSMPP PFSYNGTYRP 750
    V 751
    Length:751
    Mass (Da):85,378
    Last modified:July 7, 2009 - v4
    Checksum:i37114CD0D446639C
    GO
    Isoform 2 (identifier: P19801-2) [UniParc]FASTAAdd to Basket

    Also known as: DAO2

    The sequence of this isoform differs from the canonical sequence as follows:
         618-618: A → ARTEGGQPRALSQAASPVPG

    Show »
    Length:770
    Mass (Da):87,239
    Checksum:iCA4864D23DB6D7CC
    GO

    Sequence cautioni

    The sequence AAA58358.1 differs from that shown. Reason: Frameshift at positions 266, 284, 328, 494, 497, 514, 707 and 729.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281R → A AA sequence (PubMed:8144586)Curated
    Sequence conflicti280 – 2801P → A in AAA58358. (PubMed:2217167)Curated
    Sequence conflicti290 – 2901D → T in AAA58358. (PubMed:2217167)Curated
    Sequence conflicti572 – 5721K → R in AAA58358. (PubMed:2217167)Curated
    Sequence conflicti592 – 5921T → S in AAA58358. (PubMed:2217167)Curated
    Sequence conflicti592 – 5921T → S in CAA55046. (PubMed:8182053)Curated
    Sequence conflicti592 – 5921T → S in AAC50270. (PubMed:8595053)Curated
    Sequence conflicti592 – 5921T → S in AAB60381. (PubMed:8595053)Curated
    Sequence conflicti592 – 5921T → S in AAH14093. (PubMed:15489334)Curated
    Isoform 2 (identifier: P19801-2)
    Sequence conflicti632 – 6321A → R in AAB60381. (PubMed:8595053)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161T → M.1 Publication
    Corresponds to variant rs10156191 [ dbSNP | Ensembl ].
    VAR_025078
    Natural varianti332 – 3321S → F.2 Publications
    Corresponds to variant rs1049742 [ dbSNP | Ensembl ].
    VAR_025079
    Natural varianti479 – 4791M → I.1 Publication
    Corresponds to variant rs45558339 [ dbSNP | Ensembl ].
    VAR_025080
    Natural varianti645 – 6451H → D.4 Publications
    Corresponds to variant rs1049793 [ dbSNP | Ensembl ].
    VAR_007542
    Natural varianti659 – 6591N → H.1 Publication
    Corresponds to variant rs35070995 [ dbSNP | Ensembl ].
    VAR_025081

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei618 – 6181A → ARTEGGQPRALSQAASPVPG in isoform 2. 1 PublicationVSP_055190

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55602 mRNA. Translation: AAA58358.1. Frameshift.
    X78212 Genomic DNA. Translation: CAA55046.1.
    U11862 mRNA. Translation: AAC50270.1.
    U11863 mRNA. Translation: AAB60381.1.
    AY948960 Genomic DNA. Translation: AAX81409.1.
    AC006343 Genomic DNA. No translation available.
    AC006479 Genomic DNA. No translation available.
    BC014093 mRNA. Translation: AAH14093.1.
    CCDSiCCDS43679.1. [P19801-1]
    CCDS64797.1. [P19801-2]
    PIRiA54053.
    RefSeqiNP_001082.2. NM_001091.3. [P19801-1]
    NP_001259001.1. NM_001272072.1.
    XP_005250024.1. XM_005249967.2. [P19801-1]
    XP_006715981.1. XM_006715918.1.
    UniGeneiHs.647097.
    Hs.733889.

    Genome annotation databases

    EnsembliENST00000360937; ENSP00000354193; ENSG00000002726. [P19801-1]
    ENST00000416793; ENSP00000411613; ENSG00000002726. [P19801-2]
    ENST00000467291; ENSP00000418328; ENSG00000002726. [P19801-1]
    ENST00000493429; ENSP00000418614; ENSG00000002726. [P19801-1]
    GeneIDi26.
    KEGGihsa:26.
    UCSCiuc003why.1. human. [P19801-1]

    Polymorphism databases

    DMDMi251757489.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55602 mRNA. Translation: AAA58358.1 . Frameshift.
    X78212 Genomic DNA. Translation: CAA55046.1 .
    U11862 mRNA. Translation: AAC50270.1 .
    U11863 mRNA. Translation: AAB60381.1 .
    AY948960 Genomic DNA. Translation: AAX81409.1 .
    AC006343 Genomic DNA. No translation available.
    AC006479 Genomic DNA. No translation available.
    BC014093 mRNA. Translation: AAH14093.1 .
    CCDSi CCDS43679.1. [P19801-1 ]
    CCDS64797.1. [P19801-2 ]
    PIRi A54053.
    RefSeqi NP_001082.2. NM_001091.3. [P19801-1 ]
    NP_001259001.1. NM_001272072.1.
    XP_005250024.1. XM_005249967.2. [P19801-1 ]
    XP_006715981.1. XM_006715918.1.
    UniGenei Hs.647097.
    Hs.733889.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HI7 X-ray 1.80 A/B 21-751 [» ]
    3HIG X-ray 2.09 A/B 21-751 [» ]
    3HII X-ray 2.15 A/B 21-751 [» ]
    3K5T X-ray 2.11 A 21-751 [» ]
    3MPH X-ray 2.05 A/B 21-751 [» ]
    ProteinModelPortali P19801.
    SMRi P19801. Positions 27-751.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000354193.

    Chemistry

    BindingDBi P19801.
    ChEMBLi CHEMBL2118.
    DrugBanki DB00594. Amiloride.
    DB00127. Spermine.

    PTM databases

    PhosphoSitei P19801.

    Polymorphism databases

    DMDMi 251757489.

    Proteomic databases

    PaxDbi P19801.
    PRIDEi P19801.

    Protocols and materials databases

    DNASUi 26.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360937 ; ENSP00000354193 ; ENSG00000002726 . [P19801-1 ]
    ENST00000416793 ; ENSP00000411613 ; ENSG00000002726 . [P19801-2 ]
    ENST00000467291 ; ENSP00000418328 ; ENSG00000002726 . [P19801-1 ]
    ENST00000493429 ; ENSP00000418614 ; ENSG00000002726 . [P19801-1 ]
    GeneIDi 26.
    KEGGi hsa:26.
    UCSCi uc003why.1. human. [P19801-1 ]

    Organism-specific databases

    CTDi 26.
    GeneCardsi GC07P150523.
    H-InvDB HIX0007216.
    HGNCi HGNC:80. AOC1.
    HPAi HPA031032.
    HPA031033.
    MIMi 104610. gene.
    neXtProti NX_P19801.
    PharmGKBi PA24416.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3733.
    HOGENOMi HOG000233919.
    HOVERGENi HBG004164.
    InParanoidi P19801.
    KOi K11182.
    OrthoDBi EOG78WKR2.
    PhylomeDBi P19801.
    TreeFami TF314750.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00083-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P19801.
    GenomeRNAii 26.
    NextBioi 35485176.
    PROi P19801.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19801.
    Bgeei P19801.
    CleanExi HS_ABP1.
    Genevestigatori P19801.

    Family and domain databases

    Gene3Di 2.70.98.20. 1 hit.
    3.10.450.40. 1 hit.
    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT ASP-645.
      Tissue: Kidney.
    2. "The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter."
      Chassande O., Renard S., Barbry P., Lazdunski M.
      J. Biol. Chem. 269:14484-14489(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "cDNA sequences of variant forms of human placenta diamine oxidase."
      Zhang X., Kim J., McIntire W.S.
      Biochem. Genet. 33:261-268(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS PHE-332 AND ASP-645.
      Tissue: Placenta.
    4. NIEHS SNPs program
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-16; PHE-332; ILE-479; ASP-645 AND HIS-659.
    5. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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), VARIANT ASP-645.
      Tissue: Colon.
    7. "Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues."
      Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.
      J. Biol. Chem. 269:9921-9925(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-39, CHARACTERIZATION.
      Tissue: Placenta.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, COFACTOR, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS.

    Entry informationi

    Entry nameiAOC1_HUMAN
    AccessioniPrimary (citable) accession number: P19801
    Secondary accession number(s): C9J690
    , Q16683, Q16684, Q56II4, Q6GU42
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 153 of the entry and version 4 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

    Miscellaneous

    Inhibited by amiloride in a competitive manner.By similarity

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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