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P19801

- AOC1_HUMAN

UniProt

P19801 - AOC1_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP19801.
CleanExiHS_ABP1.
ExpressionAtlasiP19801. baseline and differential.
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.
GeneTreeiENSGT00510000046461.
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

        10         20         30         40         50
MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS
60 70 80 90 100
KKELRLQPSS TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV
110 120 130 140 150
IFFGDQEHPN VTEFAVGPLP GPCYMRALSP RPGYQSSWAS RPISTAEYAL
160 170 180 190 200
LYHTLQEATK PLHQFFLNTT GFSFQDCHDR CLAFTDVAPR GVASGQRRSW
210 220 230 240 250
LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG KFYGSPEELA
260 270 280 290 300
RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP
310 320 330 340 350
RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV
360 370 380 390 400
SVQEAVALYG GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT
410 420 430 440 450
FHYYDADDPV HYPRALCLFE MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL
460 470 480 490 500
VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH ATGYVHATFY TPEGLRHGTR
510 520 530 540 550
LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT NPWSPRHRVV
560 570 580 590 600
QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM
610 620 630 640 650
ADQVLPPGWQ EEQAITWARY PLAVTKYRES ELCSSSIYHQ NDPWHPPVVF
660 670 680 690 700
EQFLHNNENI ENEDLVAWVT VGFLHIPHSE DIPNTATPGN SVGFLLRPFN
710 720 730 740 750
FFPEDPSLAS RDTVIVWPRD NGPNYVQRWI PEDRDCSMPP PFSYNGTYRP

V
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. [P19801-2]
XP_005250024.1. XM_005249967.2. [P19801-1]
XP_006715981.1. XM_006715918.1. [P19801-2]
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. [P19801-2 ]
XP_005250024.1. XM_005249967.2. [P19801-1 ]
XP_006715981.1. XM_006715918.1. [P19801-2 ]
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.

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.
GeneTreei ENSGT00510000046461.
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

Bgeei P19801.
CleanExi HS_ABP1.
ExpressionAtlasi P19801. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 154 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