AOC1

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.

Miscellaneous

Inhibited by amiloride in a competitive manner.By similarity

Catalytic activityⁱ

H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
histamine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O₂
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
H₂O₂
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
imidazole-4-acetaldehyde
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
NH₄⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "Structure and inhibition of human diamine oxidase."
  McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
  Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
EC:1.4.3.22
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "Structure and inhibition of human diamine oxidase."
  McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
  Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
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histamine
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O₂
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=
H₂O₂
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imidazole-4-acetaldehyde
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NH₄⁺
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Cofactorⁱ

Protein has several cofactor binding sites:

Activity regulationⁱ

Inhibited by isoniazid, cimetidine, clonidine, pentamidine, berenil and pentamidine.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	373	Proton acceptor1 Publication	1
Active siteⁱ	461	Schiff-base intermediate with substrate; via topaquinoneCombined sources1 Publication	1
Metal bindingⁱ	510	Copper; via tele nitrogenCombined sources1 Publication	1
Metal bindingⁱ	512	Copper; via tele nitrogenCombined sources1 Publication	1
Metal bindingⁱ	519	Calcium 1Combined sources1 Publication	1
Metal bindingⁱ	520	Calcium 1; via carbonyl oxygenCombined sources1 Publication	1
Metal bindingⁱ	521	Calcium 1Combined sources1 Publication	1
Metal bindingⁱ	562	Calcium 2Combined sources1 Publication	1
Metal bindingⁱ	653	Calcium 2; via carbonyl oxygenCombined sources1 Publication	1
Metal bindingⁱ	656	Calcium 2Combined sources1 Publication	1
Metal bindingⁱ	658	Calcium 2Combined sources1 Publication	1
Metal bindingⁱ	664	Calcium 1Combined sources1 Publication	1
Metal bindingⁱ	665	Calcium 1; via carbonyl oxygenCombined sources1 Publication	1
Metal bindingⁱ	675	Copper; via pros nitrogenCombined sources1 Publication	1

GO - Molecular functionⁱ

calcium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 12072962
- 19764817
copper ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 12072962
- 19764817
diamine oxidase activity
Source: UniProtKB
Inferred from direct assayⁱ
drug binding
Source: UniProtKB
Inferred from direct assayⁱ
- 2217167
- 8144586
heparin binding
Source: UniProtKB
Inferred from direct assayⁱ
- 12072962
- 19764817
histamine oxidase activity Source: Reactome
methylputrescine oxidase activity Source: UniProtKB-EC
primary amine oxidase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19764817
propane-1,3-diamine oxidase activity Source: UniProtKB-EC
protein-containing complex binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19764817
protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 19764817
quinone binding
Source: UniProtKB
Inferred from direct assayⁱ
- 12072962
- 19764817
zinc ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 12072962

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

amine metabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to azide
Source: UniProtKB
Inferred from direct assayⁱ
- 16846222
cellular response to copper ion
Source: UniProtKB
Inferred from direct assayⁱ
- 9399025
cellular response to copper ion starvation
Source: UniProtKB
Inferred from direct assayⁱ
- 9399025
cellular response to heparin
Source: UniProtKB
Traceable author statementⁱ
- 19764817
cellular response to histamine
Source: UniProtKB
Inferred from direct assayⁱ
- 12072962
neutrophil degranulation Source: Reactome
oxidation-reduction process
Source: UniProtKB
Inferred from direct assayⁱ
- 16846222
- 8144586
response to antibiotic
Source: UniProtKB
Inferred from direct assayⁱ
- 19764817
- 7626074
response to drug
Source: UniProtKB
Inferred from direct assayⁱ
- 8144586
xenobiotic metabolic process Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Heparin-binding, Oxidoreductase
Ligand	Calcium, Copper, Metal-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS00083-MONOMER
BRENDAⁱ	1.4.3.22 2681
Reactomeⁱ	R-HSA-211945 Phase I - Functionalization of compounds R-HSA-6798695 Neutrophil degranulation

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Amiloride-sensitive amine oxidase [copper-containing] (EC:1.4.3.221 Publication) 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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 7

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000002726.19
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:80 AOC1
MIMⁱ	104610 gene
neXtProtⁱ	NX_P19801

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	26
Open Targets More...OpenTargetsⁱ	ENSG00000002726
PharmGKBⁱ	PA24416

Chemistry databases

ChEMBLⁱ	CHEMBL2118
Drug and drug target database More...DrugBankⁱ	DB00594 Amiloride DB03608 Diminazene

Polymorphism and mutation databases

DMDMⁱ	251757489

DMDMⁱ

251757489

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 19	1 PublicationAdd BLAST		19
ChainⁱPRO_0000035666	20 – 751	Amiloride-sensitive amine oxidase [copper-containing]Add BLAST		732

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	110	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1
Glycosylationⁱ	168	N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation	1
Disulfide bondⁱ	177 ↔ 181	Combined sources1 Publication
Disulfide bondⁱ	391 ↔ 417	Combined sources1 Publication
Modified residueⁱ	461	2',4',5'-topaquinone1 Publication	1
Glycosylationⁱ	538	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1
Disulfide bondⁱ	736	InterchainCombined sources1 Publication
Glycosylationⁱ	745	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1

Post-translational modificationⁱ

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

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PaxDbⁱ	P19801
PeptideAtlas More...PeptideAtlasⁱ	P19801
PRIDEⁱ	P19801
ProteomicsDBⁱ	53688 53689 [P19801-2]
TopDownProteomicsⁱ	P19801-1 [P19801-1]

PTM databases

iPTMnetⁱ	P19801
PhosphoSitePlusⁱ	P19801

Expressionⁱ

Tissue specificityⁱ

Placenta and kidney.

Gene expression databases

Bgeeⁱ	ENSG00000002726 Expressed in 98 organ(s), highest expression level in decidua
CleanExⁱ	HS_ABP1
ExpressionAtlasⁱ	P19801 baseline and differential
Genevisibleⁱ	P19801 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA031032 HPA031033

HPAⁱ

HPA031032
HPA031033

Interactionⁱ

Subunit structureⁱ

Homodimer; disulfide-linked.1 Publication

GO - Molecular functionⁱ

protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 19764817

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	106544, 1 interactor
IntActⁱ	P19801, 10 interactors
STRINGⁱ	9606.ENSP00000354193

Chemistry databases

BindingDBⁱ

P19801

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	29 – 33	Combined sources	5
Helixⁱ	38 – 49	Combined sources	12
Helixⁱ	52 – 54	Combined sources	3
Beta strandⁱ	64 – 75	Combined sources	12
Helixⁱ	79 – 88	Combined sources	10
Beta strandⁱ	96 – 103	Combined sources	8
Beta strandⁱ	105 – 108	Combined sources	4
Beta strandⁱ	110 – 117	Combined sources	8
Beta strandⁱ	119 – 121	Combined sources	3
Beta strandⁱ	124 – 129	Combined sources	6
Helixⁱ	137 – 140	Combined sources	4
Helixⁱ	145 – 158	Combined sources	14
Helixⁱ	160 – 162	Combined sources	3
Helixⁱ	163 – 170	Combined sources	8
Beta strandⁱ	173 – 176	Combined sources	4
Beta strandⁱ	178 – 186	Combined sources	9
Beta strandⁱ	191 – 193	Combined sources	3
Beta strandⁱ	198 – 205	Combined sources	8
Helixⁱ	210 – 212	Combined sources	3
Beta strandⁱ	214 – 222	Combined sources	9
Beta strandⁱ	225 – 227	Combined sources	3
Helixⁱ	228 – 230	Combined sources	3
Beta strandⁱ	232 – 238	Combined sources	7
Helixⁱ	246 – 254	Combined sources	9
Beta strandⁱ	301 – 303	Combined sources	3
Beta strandⁱ	309 – 313	Combined sources	5
Beta strandⁱ	316 – 320	Combined sources	5
Beta strandⁱ	322 – 329	Combined sources	8
Turnⁱ	330 – 332	Combined sources	3
Beta strandⁱ	333 – 341	Combined sources	9
Beta strandⁱ	344 – 359	Combined sources	16
Helixⁱ	364 – 368	Combined sources	5
Beta strandⁱ	370 – 372	Combined sources	3
Helixⁱ	373 – 376	Combined sources	4
Helixⁱ	378 – 380	Combined sources	3
Turnⁱ	387 – 389	Combined sources	3
Beta strandⁱ	395 – 405	Combined sources	11
Beta strandⁱ	410 – 422	Combined sources	13
Beta strandⁱ	427 – 433	Combined sources	7
Beta strandⁱ	435 – 445	Combined sources	11
Beta strandⁱ	448 – 456	Combined sources	9
Beta strandⁱ	458 – 469	Combined sources	12
Beta strandⁱ	475 – 483	Combined sources	9
Beta strandⁱ	487 – 489	Combined sources	3
Helixⁱ	492 – 496	Combined sources	5
Beta strandⁱ	497 – 502	Combined sources	6
Beta strandⁱ	505 – 508	Combined sources	4
Beta strandⁱ	510 – 520	Combined sources	11
Beta strandⁱ	524 – 540	Combined sources	17
Beta strandⁱ	547 – 559	Combined sources	13
Helixⁱ	562 – 565	Combined sources	4
Beta strandⁱ	569 – 571	Combined sources	3
Beta strandⁱ	575 – 584	Combined sources	10
Beta strandⁱ	590 – 598	Combined sources	9
Helixⁱ	610 – 619	Combined sources	10
Beta strandⁱ	621 – 626	Combined sources	6
Helixⁱ	629 – 631	Combined sources	3
Turnⁱ	637 – 641	Combined sources	5
Beta strandⁱ	643 – 645	Combined sources	3
Helixⁱ	652 – 655	Combined sources	4
Beta strandⁱ	661 – 675	Combined sources	15
Helixⁱ	679 – 681	Combined sources	3
Beta strandⁱ	691 – 704	Combined sources	14
Helixⁱ	706 – 709	Combined sources	4
Beta strandⁱ	714 – 717	Combined sources	4
Beta strandⁱ	720 – 723	Combined sources	4
Beta strandⁱ	725 – 727	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P19801
SMRⁱ	P19801
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P19801

EvolutionaryTraceⁱ

P19801

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	371 – 381	Substrate bindingCombined sources1 PublicationAdd BLAST	11
Regionⁱ	458 – 463	Substrate bindingCombined sources1 Publication	6
Regionⁱ	568 – 575	Heparin-bindingBy similarity	8

Sequence similaritiesⁱ

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	KOG1186 Eukaryota COG3733 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000154676
HOGENOMⁱ	HOG000233919
HOVERGENⁱ	HBG004164
InParanoidⁱ	P19801
KEGG Orthology (KO) More...KOⁱ	K11182
OMAⁱ	GIDCPEI
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0C1O
PhylomeDBⁱ	P19801
TreeFamⁱ	TF314750

Family and domain databases

Gene3Dⁱ	2.70.98.20, 1 hit
InterProⁱ	View protein in InterPro IPR000269 Cu_amine_oxidase IPR015798 Cu_amine_oxidase_C IPR036460 Cu_amine_oxidase_C_sf IPR016182 Cu_amine_oxidase_N-reg IPR015800 Cu_amine_oxidase_N2 IPR015802 Cu_amine_oxidase_N3
PANTHERⁱ	PTHR10638 PTHR10638, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01179 Cu_amine_oxid, 1 hit PF02727 Cu_amine_oxidN2, 1 hit PF02728 Cu_amine_oxidN3, 1 hit
PRINTSⁱ	PR00766 CUDAOXIDASE
SUPFAMⁱ	SSF49998 SSF49998, 1 hit SSF54416 SSF54416, 2 hits
PROSITEⁱ	View protein in PROSITE PS01164 COPPER_AMINE_OXID_1, 1 hit PS01165 COPPER_AMINE_OXID_2, 1 hit

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 Add to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P19801-1) [UniParc]FASTA Add 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]FASTA Add to basket

Also known as: DAO2

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

« 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 EEQAITWART EGGQPRALSQ AASPVPGRYP LAVTKYRESE 
       660        670        680        690        700
LCSSSIYHQN DPWHPPVVFE QFLHNNENIE NEDLVAWVTV GFLHIPHSED 
       710        720        730        740        750
IPNTATPGNS VGFLLRPFNF FPEDPSLASR DTVIVWPRDN GPNYVQRWIP 
       760        770
EDRDCSMPPP FSYNGTYRPV

Show »

Length:770

Mass (Da):87,239

Checksum:ⁱCA4864D23DB6D7CC

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

C9J2J4	C9J2J4_HUMAN	Amine oxidase Amine oxidase, EC 1.4.3.-	AOC1	337	Annotation score:
C9J0G8	C9J0G8_HUMAN	Amine oxidase Amine oxidase, EC 1.4.3.-	AOC1	249	Annotation score:

Sequence cautionⁱ

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	28	R → A AA sequence (PubMed:8144586).Curated	1
Sequence conflictⁱ	280	P → A in AAA58358 (PubMed:2217167).Curated	1
Sequence conflictⁱ	290	D → T in AAA58358 (PubMed:2217167).Curated	1
Sequence conflictⁱ	572	K → R in AAA58358 (PubMed:2217167).Curated	1
Sequence conflictⁱ	592	T → S in AAA58358 (PubMed:2217167).Curated	1
Sequence conflictⁱ	592	T → S in CAA55046 (PubMed:8182053).Curated	1
Sequence conflictⁱ	592	T → S in AAC50270 (PubMed:8595053).Curated	1
Sequence conflictⁱ	592	T → S in AAB60381 (PubMed:8595053).Curated	1
Sequence conflictⁱ	592	T → S in AAH14093 (PubMed:15489334).Curated	1
Isoform 2 (identifier: P19801-2)
Sequence conflictⁱ	632	A → R in AAB60381 (PubMed:8595053).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_025078	16	T → M1 PublicationCorresponds to variant dbSNP:rs10156191Ensembl.	1
Natural variantⁱVAR_025079	332	S → F2 PublicationsCorresponds to variant dbSNP:rs1049742Ensembl.	1
Natural variantⁱVAR_025080	479	M → I1 PublicationCorresponds to variant dbSNP:rs45558339Ensembl.	1
Natural variantⁱVAR_007542	645	H → D4 PublicationsCorresponds to variant dbSNP:rs1049793Ensembl.	1
Natural variantⁱVAR_025081	659	N → H1 PublicationCorresponds to variant dbSNP:rs35070995Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_055190	618	A → ARTEGGQPRALSQAASPVPG in isoform 2. 1 Publication		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS43679.1 [P19801-1] CCDS64797.1 [P19801-2]
PIRⁱ	A54053
NCBI Reference Sequences More...RefSeqⁱ	NP_001082.2, NM_001091.3 [P19801-1] NP_001259001.1, NM_001272072.1 [P19801-2] XP_016867433.1, XM_017011944.1 [P19801-2] XP_016867434.1, XM_017011945.1 [P19801-2] XP_016867435.1, XM_017011946.1 [P19801-2] XP_016867436.1, XM_017011947.1 [P19801-1]
UniGeneⁱ	Hs.647097 Hs.733889

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
UCSC genome browser More...UCSCⁱ	uc003whz.3 human [P19801-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P19801	Amine oxidase		SAIBB		770	UniRef90_P19801
Amine oxidase		PANTR		770
Amine oxidase		CALJA		763
Amine oxidase		PONAB		755
Amine oxidase		PANPA		755
+16
P19801-2	Amine oxidase (Fragment)		HUMAN		249	UniRef90_P19801-2
Amine oxidase		PONAB		770
Amine oxidase		PAPAN		755
Amine oxidase		CERAT		755
Amine oxidase		CHLSB		755
+22

Protein	Similar proteins		Species	Score	Length	Source
P19801	Amine oxidase		PANTR		770	UniRef50_P19801
Amine oxidase		SAIBB		770
Amine oxidase		CALJA		763
Amine oxidase		PANPA		755
Amine oxidase		AOTNA		755
+110
P19801-2	Amiloride-sensitive amine oxidase [copper-containing]		MOUSE		751	UniRef50_P19801-2
Amiloride-sensitive amine oxidase [copper-containing]		RAT		746
Amiloride-sensitive amine oxidase [copper-containing]		PIG		755
Amine oxidase (Fragment)		HUMAN		249
Amine oxidase		PONAB		770
+197

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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_016867433.1, XM_017011944.1 [P19801-2] XP_016867434.1, XM_017011945.1 [P19801-2] XP_016867435.1, XM_017011946.1 [P19801-2] XP_016867436.1, XM_017011947.1 [P19801-1]
UniGeneⁱ	Hs.647097 Hs.733889

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	106544, 1 interactor
IntActⁱ	P19801, 10 interactors
STRINGⁱ	9606.ENSP00000354193

Chemistry databases

BindingDBⁱ	P19801
ChEMBLⁱ	CHEMBL2118
DrugBankⁱ	DB00594 Amiloride DB03608 Diminazene

PTM databases

iPTMnetⁱ	P19801
PhosphoSitePlusⁱ	P19801

Polymorphism and mutation databases

DMDMⁱ	251757489

DMDMⁱ

251757489

Proteomic databases

PaxDbⁱ	P19801
PeptideAtlasⁱ	P19801
PRIDEⁱ	P19801
ProteomicsDBⁱ	53688 53689 [P19801-2]
TopDownProteomicsⁱ	P19801-1 [P19801-1]

Protocols and materials databases

The DNASU plasmid repository More...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	uc003whz.3 human [P19801-1]

Organism-specific databases

CTDⁱ	26
DisGeNETⁱ	26
EuPathDBⁱ	HostDB:ENSG00000002726.19
GeneCardsⁱ	AOC1
H-InvDBⁱ	HIX0007216
HGNCⁱ	HGNC:80 AOC1
HPAⁱ	HPA031032 HPA031033
MIMⁱ	104610 gene
neXtProtⁱ	NX_P19801
OpenTargetsⁱ	ENSG00000002726
PharmGKBⁱ	PA24416
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1186 Eukaryota COG3733 LUCA
GeneTreeⁱ	ENSGT00940000154676
HOGENOMⁱ	HOG000233919
HOVERGENⁱ	HBG004164
InParanoidⁱ	P19801
KOⁱ	K11182
OMAⁱ	GIDCPEI
OrthoDBⁱ	EOG091G0C1O
PhylomeDBⁱ	P19801
TreeFamⁱ	TF314750

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS00083-MONOMER
BRENDAⁱ	1.4.3.22 2681
Reactomeⁱ	R-HSA-211945 Phase I - Functionalization of compounds R-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRSⁱ	AOC1 human
EvolutionaryTraceⁱ	P19801
GenomeRNAiⁱ	26
Protein Ontology More...PROⁱ	PR:P19801
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000002726 Expressed in 98 organ(s), highest expression level in decidua
CleanExⁱ	HS_ABP1
ExpressionAtlasⁱ	P19801 baseline and differential
Genevisibleⁱ	P19801 HS

Family and domain databases

Gene3Dⁱ	2.70.98.20, 1 hit
InterProⁱ	View protein in InterPro IPR000269 Cu_amine_oxidase IPR015798 Cu_amine_oxidase_C IPR036460 Cu_amine_oxidase_C_sf IPR016182 Cu_amine_oxidase_N-reg IPR015800 Cu_amine_oxidase_N2 IPR015802 Cu_amine_oxidase_N3
PANTHERⁱ	PTHR10638 PTHR10638, 1 hit
Pfamⁱ	View protein in Pfam PF01179 Cu_amine_oxid, 1 hit PF02727 Cu_amine_oxidN2, 1 hit PF02728 Cu_amine_oxidN3, 1 hit
PRINTSⁱ	PR00766 CUDAOXIDASE
SUPFAMⁱ	SSF49998 SSF49998, 1 hit SSF54416 SSF54416, 2 hits
PROSITEⁱ	View protein in PROSITE PS01164 COPPER_AMINE_OXID_1, 1 hit PS01165 COPPER_AMINE_OXID_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AOC1_HUMAN
Accessionⁱ	P19801Primary (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:	December 5, 2018
	This is version 189 of the entry and version 4 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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UniProtKB - P19801 (AOC1_HUMAN)

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Amiloride-sensitive amine oxidase [copper-containing]

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted

Extracellular region or secreted

Peroxisome

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Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

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<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

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<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

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Protocols and materials databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ