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Protein

Aldehyde oxidase

Gene

AOX1

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

Functioni

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N-methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis.8 Publications

Catalytic activityi

An aldehyde + H2O + O2 = a carboxylate + H2O2.2 Publications
Retinal + O2 + H2O = retinoate + H2O2.By similarity

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Is very potently inhibited by raloxifene. Also inhibited by estradiol, ethinyl estradiol, hydralazine, menadione, and isovanillin. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor.4 Publications

Kineticsi

kcat is 6.4 min(-1) for benzaldehyde oxidation, 5.6 min(-1) for phthalazine oxidation, 12.2 min(-1) for phenanthridine oxidation and 5.6 min(-1) for chloroquinazolinone oxidation.

  1. KM=7.1 µM for benzaldehyde (at 25 degrees Celsius and pH 7.5)3 Publications
  2. KM=1.3 µM for phthalazine (at 25 degrees Celsius and pH 7.5)3 Publications
  3. KM=3.9 µM for phenanthridine (at 25 degrees Celsius and pH 7.5)3 Publications
  4. KM=5.2 µM for chloroquinazolinone (at 25 degrees Celsius and pH 7.5)3 Publications
  5. KM=0.42 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)3 Publications
  6. KM=0.15 mM for famciclovir (at 37 degrees Celsius and pH 7)3 Publications
  7. KM=6.3 µM for N-[(2-dimethylamino)ethyl]acridine-4-carboxamide (at 37 degrees Celsius and pH 7.4)3 Publications
  1. Vmax=16 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate3 Publications
  2. Vmax=61 nmol/min/mg enzyme with famciclovir as substrate3 Publications
  3. Vmax=2.3 nmol/min/mg enzyme with N-[(2-dimethylamino)ethyl]acridine-4-carboxamide as substrate3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi44Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi49Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi52Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi74Iron-sulfur 1 (2Fe-2S)By similarity1
Binding sitei113MolybdopterinBy similarity1
Metal bindingi114Iron-sulfur 2 (2Fe-2S)By similarity1
Metal bindingi117Iron-sulfur 2 (2Fe-2S)By similarity1
Metal bindingi149Iron-sulfur 2 (2Fe-2S)By similarity1
Metal bindingi151Iron-sulfur 2 (2Fe-2S)By similarity1
Binding sitei354FADBy similarity1
Binding sitei358FADBy similarity1
Binding sitei367FADBy similarity1
Binding sitei411FAD; via amide nitrogenBy similarity1
Binding sitei806Molybdopterin; via amide nitrogenBy similarity1
Binding sitei1047Molybdopterin; via amide nitrogenBy similarity1
Binding sitei1203MolybdopterinBy similarity1
Active sitei1270Proton acceptor; for azaheterocycle hydroxylase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi264 – 271FADBy similarity8

GO - Molecular functioni

GO - Biological processi

  • inflammatory response Source: ProtInc
  • reactive oxygen species metabolic process Source: ProtInc
  • vitamin B6 metabolic process Source: Reactome
  • xanthine catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138356-MONOMER.
ZFISH:ENSG00000138356-MONOMER.
BRENDAi1.2.3.1. 2681.
ReactomeiR-HSA-964975. Vitamins B6 activation to pyridoxal phosphate.
SABIO-RKQ06278.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde oxidase (EC:1.2.3.12 Publications)
Alternative name(s):
Aldehyde oxidase 1
Azaheterocycle hydroxylase (EC:1.17.3.-)
Gene namesi
Name:AOX1
Synonyms:AO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:553. AOX1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: GO_Central
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi316.
OpenTargetsiENSG00000138356.
PharmGKBiPA24842.

Chemistry databases

ChEMBLiCHEMBL3257.
DrugBankiDB00437. Allopurinol.
DB00513. Aminocaproic Acid.
DB00484. Brimonidine.
DB00426. Famciclovir.
DB09054. Idelalisib.
DB09078. Lenvatinib.
DB00170. Menadione.
DB01033. Mercaptopurine.
DB00563. Methotrexate.
DB00339. Pyrazinamide.
DB00481. Raloxifene.
DB00962. Zaleplon.
DB00909. Zonisamide.

Polymorphism and mutation databases

BioMutaiAOX1.
DMDMi215273968.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001661041 – 1338Aldehyde oxidaseAdd BLAST1338

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1068PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ06278.
MaxQBiQ06278.
PaxDbiQ06278.
PeptideAtlasiQ06278.
PRIDEiQ06278.

PTM databases

iPTMnetiQ06278.
PhosphoSitePlusiQ06278.

Expressioni

Tissue specificityi

Abundant in liver, expressed in adipose tissue and at lower levels in lung, skeletal muscle, pancreas. In contrast to mice, no significant gender difference in AOX1 expression level (at protein level).7 Publications

Developmental stagei

Not detected in preadipocytes but strongly induced in mature adipocytes.1 Publication

Inductioni

In liver, is down-regulated by adiponectin and by the PPARA agonist, fenofibric acid.1 Publication

Gene expression databases

BgeeiENSG00000138356.
CleanExiHS_AOX1.
ExpressionAtlasiQ06278. baseline and differential.
GenevisibleiQ06278. HS.

Organism-specific databases

HPAiHPA040199.
HPA040215.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi106813. 5 interactors.
DIPiDIP-61698N.
IntActiQ06278. 4 interactors.
STRINGi9606.ENSP00000363832.

Chemistry databases

BindingDBiQ06278.

Structurei

Secondary structure

11338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Beta strandi14 – 20Combined sources7
Helixi27 – 33Combined sources7
Beta strandi45 – 49Combined sources5
Beta strandi53 – 60Combined sources8
Turni61 – 64Combined sources4
Beta strandi65 – 72Combined sources8
Helixi73 – 75Combined sources3
Helixi78 – 81Combined sources4
Beta strandi85 – 87Combined sources3
Helixi89 – 92Combined sources4
Beta strandi95 – 97Combined sources3
Helixi101 – 108Combined sources8
Helixi118 – 131Combined sources14
Helixi137 – 143Combined sources7
Helixi144 – 146Combined sources3
Beta strandi150 – 152Combined sources3
Helixi155 – 162Combined sources8
Helixi204 – 206Combined sources3
Helixi212 – 214Combined sources3
Helixi220 – 226Combined sources7
Beta strandi234 – 237Combined sources4
Beta strandi242 – 245Combined sources4
Helixi249 – 258Combined sources10
Helixi271 – 277Combined sources7
Beta strandi283 – 286Combined sources4
Helixi292 – 295Combined sources4
Beta strandi297 – 299Combined sources3
Beta strandi301 – 307Combined sources7
Helixi312 – 325Combined sources14
Turni328 – 330Combined sources3
Helixi332 – 343Combined sources12
Helixi347 – 352Combined sources6
Helixi355 – 361Combined sources7
Helixi369 – 374Combined sources6
Beta strandi378 – 382Combined sources5
Beta strandi387 – 391Combined sources5
Helixi394 – 397Combined sources4
Turni401 – 403Combined sources3
Beta strandi410 – 417Combined sources8
Beta strandi423 – 430Combined sources8
Beta strandi432 – 437Combined sources6
Beta strandi440 – 448Combined sources9
Beta strandi451 – 453Combined sources3
Beta strandi458 – 469Combined sources12
Helixi474 – 480Combined sources7
Helixi487 – 498Combined sources12
Helixi512 – 537Combined sources26
Turni539 – 541Combined sources3
Turni547 – 549Combined sources3
Helixi550 – 552Combined sources3
Beta strandi562 – 566Combined sources5
Beta strandi572 – 574Combined sources3
Helixi589 – 593Combined sources5
Helixi600 – 602Combined sources3
Beta strandi610 – 616Combined sources7
Beta strandi620 – 628Combined sources9
Helixi630 – 633Combined sources4
Beta strandi638 – 642Combined sources5
Helixi644 – 646Combined sources3
Helixi648 – 650Combined sources3
Beta strandi666 – 668Combined sources3
Beta strandi674 – 682Combined sources9
Helixi683 – 690Combined sources8
Beta strandi694 – 699Combined sources6
Helixi709 – 711Combined sources3
Beta strandi721 – 726Combined sources6
Helixi728 – 731Combined sources4
Helixi732 – 734Combined sources3
Beta strandi736 – 745Combined sources10
Beta strandi756 – 762Combined sources7
Beta strandi769 – 773Combined sources5
Helixi778 – 789Combined sources12
Helixi793 – 795Combined sources3
Beta strandi796 – 801Combined sources6
Helixi812 – 828Combined sources17
Beta strandi832 – 835Combined sources4
Helixi838 – 844Combined sources7
Beta strandi851 – 859Combined sources9
Beta strandi865 – 878Combined sources14
Helixi884 – 893Combined sources10
Turni894 – 897Combined sources4
Beta strandi901 – 911Combined sources11
Turni921 – 924Combined sources4
Helixi925 – 943Combined sources19
Helixi947 – 954Combined sources8
Beta strandi958 – 961Combined sources4
Beta strandi967 – 969Combined sources3
Helixi971 – 984Combined sources14
Helixi986 – 999Combined sources14
Beta strandi1001 – 1016Combined sources16
Helixi1022 – 1024Combined sources3
Beta strandi1026 – 1032Combined sources7
Beta strandi1038 – 1043Combined sources6
Beta strandi1047 – 1049Combined sources3
Helixi1051 – 1062Combined sources12
Helixi1067 – 1069Combined sources3
Turni1077 – 1079Combined sources3
Helixi1091 – 1115Combined sources25
Helixi1122 – 1131Combined sources10
Beta strandi1137 – 1142Combined sources6
Beta strandi1148 – 1150Combined sources3
Turni1151 – 1154Combined sources4
Beta strandi1155 – 1157Combined sources3
Beta strandi1160 – 1174Combined sources15
Turni1175 – 1177Combined sources3
Beta strandi1180 – 1190Combined sources11
Helixi1197 – 1215Combined sources19
Helixi1232 – 1234Combined sources3
Helixi1241 – 1243Combined sources3
Beta strandi1246 – 1252Combined sources7
Helixi1262 – 1264Combined sources3
Helixi1271 – 1276Combined sources6
Helixi1277 – 1293Combined sources17
Helixi1308 – 1314Combined sources7
Helixi1318 – 1322Combined sources5
Helixi1328 – 1330Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UHWX-ray2.60A1-1338[»]
4UHXX-ray2.70A1-1338[»]
5EPGX-ray3.39A1-1338[»]
ProteinModelPortaliQ06278.
SMRiQ06278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini236 – 421FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiQ06278.
KOiK00157.
OMAiMDPVHYP.
OrthoDBiEOG091G01AW.
PhylomeDBiQ06278.
TreeFamiTF353036.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR014313. Aldehyde_oxidase.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG
60 70 80 90 100
ACTVMISRYN PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH
110 120 130 140 150
PVQERIAKCH GTQCGFCTPG MVMSIYTLLR NHPEPTLDQL TDALGGNLCR
160 170 180 190 200
CTGYRPIIDA CKTFCKTSGC CQSKENGVCC LDQGINGLPE FEEGSKTSPK
210 220 230 240 250
LFAEEEFLPL DPTQELIFPP ELMIMAEKQS QRTRVFGSER MMWFSPVTLK
260 270 280 290 300
ELLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPVIISPDR IEELSVVNHA
310 320 330 340 350
YNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYHALLKH LGTLAGSQIR
360 370 380 390 400
NMASLGGHII SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC
410 420 430 440 450
PNADLKPQEI LVSVNIPYSR KWEFVSAFRQ AQRQENALAI VNSGMRVFFG
460 470 480 490 500
EGDGIIRELC ISYGGVGPAT ICAKNSCQKL IGRHWNEQML DIACRLILNE
510 520 530 540 550
VSLLGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKMDPV HYPSLADKYE
560 570 580 590 600
SALEDLHSKH HCSTLKYQNI GPKQHPEDPI GHPIMHLSGV KHATGEAIYC
610 620 630 640 650
DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD IMTAEHLSDV
660 670 680 690 700
NSFCFFTEAE KFLATDKVFC VGQLVCAVLA DSEVQAKRAA KRVKIVYQDL
710 720 730 740 750
EPLILTIEES IQHNSSFKPE RKLEYGNVDE AFKVVDQILE GEIHMGGQEH
760 770 780 790 800
FYMETQSMLV VPKGEDQEMD VYVSTQFPKY IQDIVASTLK LPANKVMCHV
810 820 830 840 850
RRVGGAFGGK VLKTGIIAAV TAFAANKHGR AVRCVLERGE DMLITGGRHP
860 870 880 890 900
YLGKYKAGFM NDGRILALDM EHYSNAGASL DESLFVIEMG LLKMDNAYKF
910 920 930 940 950
PNLRCRGWAC RTNLPSNTAF RGFGFPQAAL ITESCITEVA AKCGLSPEKV
960 970 980 990 1000
RIINMYKEID QTPYKQEINA KNLIQCWREC MAMSSYSLRK VAVEKFNAEN
1010 1020 1030 1040 1050
YWKKKGLAMV PLKFPVGLGS RAAGQAAALV HIYLDGSVLV THGGIEMGQG
1060 1070 1080 1090 1100
VHTKMIQVVS RELRMPMSNV HLRGTSTETV PNANISGGSV VADLNGLAVK
1110 1120 1130 1140 1150
DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESINLSAVG YFRGYESDMN
1160 1170 1180 1190 1200
WEKGEGQPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID
1210 1220 1230 1240 1250
IGQIEGAFIQ GMGLYTIEEL NYSPQGILHT RGPDQYKIPA ICDMPTELHI
1260 1270 1280 1290 1300
ALLPPSQNSN TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RQERGLHGPL
1310 1320 1330
TLNSPLTPEK IRMACEDKFT KMIPRDEPGS YVPWNVPI
Length:1,338
Mass (Da):147,918
Last modified:November 25, 2008 - v2
Checksum:i2AB5E543F18C9261
GO

Sequence cautioni

The sequence AAA96650 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302.Curated
The sequence AAB83966 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41K → P in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti41K → P in AAB83966 (Ref. 2) Curated1
Sequence conflicti127T → P in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti127T → P in AAB83966 (Ref. 2) Curated1
Sequence conflicti152T → H in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti152T → H in AAB83966 (Ref. 2) Curated1
Sequence conflicti227E → D in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti227E → D in AAB83966 (Ref. 2) Curated1
Sequence conflicti251E → D in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti418Y → I in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti418Y → I in AAB83966 (Ref. 2) Curated1
Sequence conflicti501V → L in AAB83966 (Ref. 2) Curated1
Sequence conflicti627I → N in AAB83966 (Ref. 2) Curated1
Sequence conflicti929A → V in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti929A → V in AAB83966 (Ref. 2) Curated1
Sequence conflicti1019G → A in AAA96650 (PubMed:8248161).Curated1
Sequence conflicti1019G → A in AAB83966 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_061136314Q → R.Corresponds to variant rs58185012dbSNPEnsembl.1
Natural variantiVAR_047517802R → C Decreases homodimerization but nearly no effect on kinetic parameters. 1 PublicationCorresponds to variant rs41309768dbSNPEnsembl.1
Natural variantiVAR_070256921R → H Increases homodimerization; abolishes enzymatic activity on phenanthridine; decreases turnover number with benzaldehyde, phtalazine and chloroquinazolinone as substrate, while nearly no effect on the KM. 1 PublicationCorresponds to variant rs56199635dbSNPEnsembl.1
Natural variantiVAR_0702571135N → S Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. 1 PublicationCorresponds to variant rs55754655dbSNPEnsembl.1
Natural variantiVAR_0702581271S → L.1 PublicationCorresponds to variant rs141786030dbSNPEnsembl.1
Natural variantiVAR_0475181297H → R Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. 1 PublicationCorresponds to variant rs3731722dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11005 mRNA. Translation: AAA96650.1. Frameshift.
AF017060
, AF009441, AF009442, AF009443, AF009444, AF009445, AF009446, AF009447, AF009448, AF009449, AF009450, AF009451, AF009452, AF009453, AF009454, AF009455, AF009456, AF009457, AF009458, AF009459, AF009460, AF009461, AF009462, AF009463, AF009464, AF009465, AF009466, AF009467, AF009468, AF009469, AF009470, AF009471, AF009472, AF009473, AF009474 Genomic DNA. Translation: AAB83966.1. Frameshift.
AF010260 Genomic DNA. Translation: AAB83968.1.
AB046692 mRNA. Translation: BAB40305.1.
AC007163 Genomic DNA. Translation: AAX93285.1.
AC080164 Genomic DNA. Translation: AAY24265.1.
CH471063 Genomic DNA. Translation: EAW70209.1.
BC117179 mRNA. Translation: AAI17180.1.
BC117181 mRNA. Translation: AAI17182.1.
CCDSiCCDS33360.1.
PIRiA49634.
RefSeqiNP_001150.3. NM_001159.3.
UniGeneiHs.406238.

Genome annotation databases

EnsembliENST00000374700; ENSP00000363832; ENSG00000138356.
GeneIDi316.
KEGGihsa:316.
UCSCiuc002uvx.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11005 mRNA. Translation: AAA96650.1. Frameshift.
AF017060
, AF009441, AF009442, AF009443, AF009444, AF009445, AF009446, AF009447, AF009448, AF009449, AF009450, AF009451, AF009452, AF009453, AF009454, AF009455, AF009456, AF009457, AF009458, AF009459, AF009460, AF009461, AF009462, AF009463, AF009464, AF009465, AF009466, AF009467, AF009468, AF009469, AF009470, AF009471, AF009472, AF009473, AF009474 Genomic DNA. Translation: AAB83966.1. Frameshift.
AF010260 Genomic DNA. Translation: AAB83968.1.
AB046692 mRNA. Translation: BAB40305.1.
AC007163 Genomic DNA. Translation: AAX93285.1.
AC080164 Genomic DNA. Translation: AAY24265.1.
CH471063 Genomic DNA. Translation: EAW70209.1.
BC117179 mRNA. Translation: AAI17180.1.
BC117181 mRNA. Translation: AAI17182.1.
CCDSiCCDS33360.1.
PIRiA49634.
RefSeqiNP_001150.3. NM_001159.3.
UniGeneiHs.406238.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UHWX-ray2.60A1-1338[»]
4UHXX-ray2.70A1-1338[»]
5EPGX-ray3.39A1-1338[»]
ProteinModelPortaliQ06278.
SMRiQ06278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106813. 5 interactors.
DIPiDIP-61698N.
IntActiQ06278. 4 interactors.
STRINGi9606.ENSP00000363832.

Chemistry databases

BindingDBiQ06278.
ChEMBLiCHEMBL3257.
DrugBankiDB00437. Allopurinol.
DB00513. Aminocaproic Acid.
DB00484. Brimonidine.
DB00426. Famciclovir.
DB09054. Idelalisib.
DB09078. Lenvatinib.
DB00170. Menadione.
DB01033. Mercaptopurine.
DB00563. Methotrexate.
DB00339. Pyrazinamide.
DB00481. Raloxifene.
DB00962. Zaleplon.
DB00909. Zonisamide.

PTM databases

iPTMnetiQ06278.
PhosphoSitePlusiQ06278.

Polymorphism and mutation databases

BioMutaiAOX1.
DMDMi215273968.

Proteomic databases

EPDiQ06278.
MaxQBiQ06278.
PaxDbiQ06278.
PeptideAtlasiQ06278.
PRIDEiQ06278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374700; ENSP00000363832; ENSG00000138356.
GeneIDi316.
KEGGihsa:316.
UCSCiuc002uvx.4. human.

Organism-specific databases

CTDi316.
DisGeNETi316.
GeneCardsiAOX1.
H-InvDBHIX0029780.
HGNCiHGNC:553. AOX1.
HPAiHPA040199.
HPA040215.
MIMi602841. gene.
neXtProtiNX_Q06278.
OpenTargetsiENSG00000138356.
PharmGKBiPA24842.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiQ06278.
KOiK00157.
OMAiMDPVHYP.
OrthoDBiEOG091G01AW.
PhylomeDBiQ06278.
TreeFamiTF353036.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138356-MONOMER.
ZFISH:ENSG00000138356-MONOMER.
BRENDAi1.2.3.1. 2681.
ReactomeiR-HSA-964975. Vitamins B6 activation to pyridoxal phosphate.
SABIO-RKQ06278.

Miscellaneous databases

ChiTaRSiAOX1. human.
GeneWikiiAldehyde_oxidase_1.
GenomeRNAii316.
PROiQ06278.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138356.
CleanExiHS_AOX1.
ExpressionAtlasiQ06278. baseline and differential.
GenevisibleiQ06278. HS.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR014313. Aldehyde_oxidase.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAOXA_HUMAN
AccessioniPrimary (citable) accession number: Q06278
Secondary accession number(s): O14765
, Q53RR8, Q53TV3, Q9BYF0, Q9UPG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 25, 2008
Last modified: November 2, 2016
This is version 167 of the entry and version 2 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

AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:22335465).1 Publication

Caution

Was originally thought to be a xanthine dehydrogenase.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

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