UniProtKB - Q06278 (AOXA_HUMAN)
Protein
Aldehyde oxidase
Gene
AOX1
Organism
Homo sapiens (Human)
Status
Functioni
Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, 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.9 Publications
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
Catalytic activityi
- EC:1.2.3.12 Publications
Cofactori
Protein has several cofactor binding sites:- [2Fe-2S] cluster3 PublicationsNote: Binds 2 [2Fe-2S] clusters per subunit.2 Publications
- FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications
- Mo-molybdopterin3 PublicationsNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.2 Publications
Activity regulationi
Is very potently inhibited by raloxifene (PubMed:26842593). Also inhibited by estradiol, ethinyl estradiol, hydralazine, menadione, isovanillin and thioridazine. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor (PubMed:22031625, PubMed:22522748, PubMed:22996261, PubMed:9224775, PubMed:26322824).6 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 Publication
- KM=4.6 µM for benzaldehyde (in the presence of 2,6-dichlorophenol indophenol as electron acceptor)1 Publication
- KM=45.18 µM for benzaldehyde (in the presence of ferricyanide as electron acceptor)1 Publication
- KM=1.3 µM for phthalazine (at 25 degrees Celsius and pH 7.5)1 Publication
- KM=8.96 µM for phthalazine (in the presence of 2,6-dichlorophenol indophenol as electron acceptor)1 Publication
- KM=125.7 µM for phthalazine (in the presence of ferricyanide as electron acceptor)1 Publication
- KM=0.78 µM for phenanthridine (in the pres 2,6-dichlorophenol indophenol as electron acceptor)1 Publication
- KM=25.5 µM for phenanthridine (in the presence of ferricyanide as electron acceptor)1 Publication
- KM=26.53 µM for phenanthridine (in the presence of molecular oxygen as electron acceptor)1 Publication
- KM=3.9 µM for phenanthridine (at 25 degrees Celsius and pH 7.5)1 Publication
- KM=5.2 µM for chloroquinazolinone (at 25 degrees Celsius and pH 7.5)1 Publication
- KM=0.42 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)1 Publication
- KM=0.15 mM for famciclovir (at 37 degrees Celsius and pH 7)1 Publication
- KM=6.3 µM for N-[(2-dimethylamino)ethyl]acridine-4-carboxamide (at 37 degrees Celsius and pH 7.4)1 Publication
- Vmax=16 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate1 Publication
- Vmax=61 nmol/min/mg enzyme with famciclovir as substrate1 Publication
- Vmax=2.3 nmol/min/mg enzyme with N-[(2-dimethylamino)ethyl]acridine-4-carboxamide as substrate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 44 | Iron-sulfur 1 (2Fe-2S)Combined sources1 Publication | 1 | |
Metal bindingi | 49 | Iron-sulfur 1 (2Fe-2S)Combined sources2 Publications | 1 | |
Metal bindingi | 52 | Iron-sulfur 1 (2Fe-2S)Combined sources2 Publications | 1 | |
Metal bindingi | 74 | Iron-sulfur 1 (2Fe-2S)Combined sources2 Publications | 1 | |
Binding sitei | 113 | MolybdopterinCombined sources1 Publication | 1 | |
Metal bindingi | 114 | Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications | 1 | |
Metal bindingi | 117 | Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications | 1 | |
Metal bindingi | 149 | Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications | 1 | |
Metal bindingi | 151 | Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications | 1 | |
Binding sitei | 151 | MolybdopterinCombined sources2 Publications | 1 | |
Binding sitei | 345 | FAD; via amide nitrogenCombined sources1 Publication | 1 | |
Binding sitei | 354 | FADCombined sources2 Publications | 1 | |
Binding sitei | 358 | FADCombined sources2 Publications | 1 | |
Binding sitei | 367 | FADCombined sources2 Publications | 1 | |
Binding sitei | 411 | FAD; via amide nitrogen and carbonyl oxygenCombined sources2 Publications | 1 | |
Binding sitei | 1047 | Molybdopterin; via carbonyl oxygenCombined sources2 Publications | 1 | |
Binding sitei | 1203 | MolybdopterinCombined sources2 Publications | 1 | |
Binding sitei | 1268 | Molybdopterin; via carbonyl oxygenCombined sources1 Publication | 1 | |
Active sitei | 1270 | Proton acceptor; for azaheterocycle hydroxylase activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 264 – 271 | FADCombined sources2 Publications | 8 |
GO - Molecular functioni
- 2 iron, 2 sulfur cluster binding Source: UniProtKB
- aldehyde oxidase activity Source: UniProtKB
- electron transfer activity Source: InterPro
- FAD binding Source: InterPro
- flavin adenine dinucleotide binding Source: UniProtKB
- geranial:oxygen oxidoreductase activity Source: UniProtKB-EC
- heptaldehyde:oxygen oxidoreductase activity Source: UniProtKB-EC
- identical protein binding Source: IntAct
- iron ion binding Source: UniProtKB
- molybdopterin cofactor binding Source: UniProtKB
- NAD binding Source: InterPro
- protein homodimerization activity Source: UniProtKB
- xanthine dehydrogenase activity Source: GO_Central
GO - Biological processi
- drug metabolic process Source: UniProtKB
- vitamin B6 metabolic process Source: Reactome
- xanthine catabolic process Source: GO_Central
Keywordsi
Molecular function | Oxidoreductase |
Ligand | 2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum |
Enzyme and pathway databases
BioCyci | MetaCyc:ENSG00000138356-MONOMER |
BRENDAi | 1.2.3.1, 2681 |
PathwayCommonsi | Q06278 |
Reactomei | R-HSA-964975, Vitamins B6 activation to pyridoxal phosphate |
SABIO-RKi | Q06278 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:553, AOX1 |
MIMi | 602841, gene |
neXtProti | NX_Q06278 |
VEuPathDBi | HostDB:ENSG00000138356.13 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 3 Publications
Cytosol
- cytosol Source: UniProtKB
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 44 | C → W: Disrupts protein stability. 1 Publication | 1 | |
Mutagenesisi | 1269 | G → R: No effect on dimerization. Loss of oxidase activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 316 |
OpenTargetsi | ENSG00000138356 |
PharmGKBi | PA24842 |
Miscellaneous databases
Pharosi | Q06278, Tbio |
Chemistry databases
ChEMBLi | CHEMBL3257 |
DrugBanki | DB00437, Allopurinol DB00513, Aminocaproic acid DB00484, Brimonidine DB11791, Capmatinib DB00924, Cyclobenzaprine DB03516, Eniluracil DB00426, Famciclovir DB12466, Favipiravir DB09054, Idelalisib DB09078, Lenvatinib DB00170, Menadione DB01033, Mercaptopurine DB00563, Methotrexate DB08840, N-methylnicotinamide DB00157, NADH DB00339, Pyrazinamide DB00481, Raloxifene DB04827, Urethane DB00962, Zaleplon DB00246, Ziprasidone DB00909, Zonisamide |
DrugCentrali | Q06278 |
Genetic variation databases
BioMutai | AOX1 |
DMDMi | 215273968 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000166104 | 1 – 1338 | Aldehyde oxidaseAdd BLAST | 1338 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1068 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
EPDi | Q06278 |
jPOSTi | Q06278 |
MassIVEi | Q06278 |
MaxQBi | Q06278 |
PaxDbi | Q06278 |
PeptideAtlasi | Q06278 |
PRIDEi | Q06278 |
ProteomicsDBi | 58430 |
PTM databases
iPTMneti | Q06278 |
PhosphoSitePlusi | Q06278 |
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
Bgeei | ENSG00000138356, Expressed in adrenal gland and 194 other tissues |
ExpressionAtlasi | Q06278, baseline and differential |
Genevisiblei | Q06278, HS |
Organism-specific databases
HPAi | ENSG00000138356, Tissue enriched (liver) |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsBinary interactionsi
Q06278
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-3926368,EBI-3926368 |
GO - Molecular functioni
- identical protein binding Source: IntAct
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 106813, 10 interactors |
DIPi | DIP-61698N |
IntActi | Q06278, 5 interactors |
STRINGi | 9606.ENSP00000363832 |
Chemistry databases
BindingDBi | Q06278 |
Miscellaneous databases
RNActi | Q06278, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q06278 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 5 – 92 | 2Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST | 88 | |
Domaini | 236 – 421 | FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST | 186 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 806 – 807 | Molybdopterin bindingCombined sources2 Publications | 2 | |
Regioni | 1088 – 1091 | Molybdopterin bindingCombined sources2 Publications | 4 |
Sequence similaritiesi
Belongs to the xanthine dehydrogenase family.Curated
Phylogenomic databases
eggNOGi | KOG0430, Eukaryota |
GeneTreei | ENSGT00950000183114 |
HOGENOMi | CLU_001681_1_2_1 |
InParanoidi | Q06278 |
OMAi | FRFWHEV |
OrthoDBi | 48717at2759 |
PhylomeDBi | Q06278 |
TreeFami | TF353036 |
Family and domain databases
InterProi | View protein in InterPro IPR002888, 2Fe-2S-bd IPR036884, 2Fe-2S-bd_dom_sf IPR036010, 2Fe-2S_ferredoxin-like_sf IPR001041, 2Fe-2S_ferredoxin-type IPR006058, 2Fe2S_fd_BS IPR000674, Ald_Oxase/Xan_DH_a/b IPR036856, Ald_Oxase/Xan_DH_a/b_sf IPR016208, Ald_Oxase/xanthine_DH IPR014313, Aldehyde_oxidase IPR008274, AldOxase/xan_DH_Mopterin-bd IPR037165, AldOxase/xan_DH_Mopterin-bd_sf IPR005107, CO_DH_flav_C IPR036683, CO_DH_flav_C_dom_sf IPR016166, FAD-bd_PCMH IPR036318, FAD-bd_PCMH-like_sf IPR002346, Mopterin_DH_FAD-bd IPR022407, OxRdtase_Mopterin_BS |
Pfami | View protein in Pfam PF01315, 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 |
PIRSFi | PIRSF000127, Xanthine_DH, 1 hit |
SMARTi | View protein in SMART SM01008, Ald_Xan_dh_C, 1 hit SM01092, CO_deh_flav_C, 1 hit |
SUPFAMi | SSF47741, SSF47741, 1 hit SSF54292, SSF54292, 1 hit SSF54665, SSF54665, 1 hit SSF55447, SSF55447, 1 hit SSF56003, SSF56003, 1 hit SSF56176, SSF56176, 1 hit |
TIGRFAMsi | TIGR02969, mam_aldehyde_ox, 1 hit |
PROSITEi | View protein in PROSITE PS00197, 2FE2S_FER_1, 1 hit PS51085, 2FE2S_FER_2, 1 hit PS51387, FAD_PCMH, 1 hit PS00559, MOLYBDOPTERIN_EUK, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
Q06278-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketC9J244 | C9J244_HUMAN | Aldehyde oxidase | AOX1 | 151 | Annotation score: | ||
H7C3Q1 | H7C3Q1_HUMAN | Aldehyde oxidase | AOX1 | 190 | Annotation score: | ||
H7BXF7 | H7BXF7_HUMAN | Aldehyde oxidase | AOX1 | 193 | Annotation score: |
Sequence cautioni
The sequence AAA96650 differs from that shown. Reason: Frameshift.Curated
The sequence AAB83966 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 41 | K → P in AAA96650 (PubMed:8248161).Curated | 1 | |
Sequence conflicti | 41 | K → P in AAB83966 (Ref. 2) Curated | 1 | |
Sequence conflicti | 127 | T → P in AAA96650 (PubMed:8248161).Curated | 1 | |
Sequence conflicti | 127 | T → P in AAB83966 (Ref. 2) Curated | 1 | |
Sequence conflicti | 152 | T → H in AAA96650 (PubMed:8248161).Curated | 1 | |
Sequence conflicti | 152 | T → H in AAB83966 (Ref. 2) Curated | 1 | |
Sequence conflicti | 227 | E → D in AAA96650 (PubMed:8248161).Curated | 1 | |
Sequence conflicti | 227 | E → D in AAB83966 (Ref. 2) Curated | 1 | |
Sequence conflicti | 251 | E → D in AAA96650 (PubMed:8248161).Curated | 1 | |
Sequence conflicti | 418 | Y → I in AAA96650 (PubMed:8248161).Curated | 1 | |
Sequence conflicti | 418 | Y → I in AAB83966 (Ref. 2) Curated | 1 | |
Sequence conflicti | 501 | V → L in AAB83966 (Ref. 2) Curated | 1 | |
Sequence conflicti | 627 | I → N in AAB83966 (Ref. 2) Curated | 1 | |
Sequence conflicti | 929 | A → V in AAA96650 (PubMed:8248161).Curated | 1 | |
Sequence conflicti | 929 | A → V in AAB83966 (Ref. 2) Curated | 1 | |
Sequence conflicti | 1019 | G → A in AAA96650 (PubMed:8248161).Curated | 1 | |
Sequence conflicti | 1019 | G → A in AAB83966 (Ref. 2) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_061136 | 314 | Q → R. Corresponds to variant dbSNP:rs58185012EnsemblClinVar. | 1 | |
Natural variantiVAR_047517 | 802 | R → C Decreases homodimerization but nearly no effect on kinetic parameters. 1 PublicationCorresponds to variant dbSNP:rs41309768Ensembl. | 1 | |
Natural variantiVAR_070256 | 921 | R → 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 dbSNP:rs56199635Ensembl. | 1 | |
Natural variantiVAR_070257 | 1135 | N → 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 dbSNP:rs55754655Ensembl. | 1 | |
Natural variantiVAR_070258 | 1271 | S → L No effect on dimerization; no effect on oxidase activity. 2 PublicationsCorresponds to variant dbSNP:rs141786030Ensembl. | 1 | |
Natural variantiVAR_047518 | 1297 | H → 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 dbSNP:rs3731722Ensembl. | 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 |
CCDSi | CCDS33360.1 |
PIRi | A49634 |
RefSeqi | NP_001150.3, NM_001159.3 |
Genome annotation databases
Ensembli | ENST00000374700; ENSP00000363832; ENSG00000138356 |
GeneIDi | 316 |
KEGGi | hsa:316 |
UCSCi | uc002uvx.4, human |
Similar proteinsi
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 |
CCDSi | CCDS33360.1 |
PIRi | A49634 |
RefSeqi | NP_001150.3, NM_001159.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4UHW | X-ray | 2.60 | A | 1-1338 | [»] | |
4UHX | X-ray | 2.70 | A | 1-1338 | [»] | |
5EPG | X-ray | 3.39 | A | 1-1338 | [»] | |
6Q6Q | X-ray | 3.10 | A | 1-1338 | [»] | |
SMRi | Q06278 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 106813, 10 interactors |
DIPi | DIP-61698N |
IntActi | Q06278, 5 interactors |
STRINGi | 9606.ENSP00000363832 |
Chemistry databases
BindingDBi | Q06278 |
ChEMBLi | CHEMBL3257 |
DrugBanki | DB00437, Allopurinol DB00513, Aminocaproic acid DB00484, Brimonidine DB11791, Capmatinib DB00924, Cyclobenzaprine DB03516, Eniluracil DB00426, Famciclovir DB12466, Favipiravir DB09054, Idelalisib DB09078, Lenvatinib DB00170, Menadione DB01033, Mercaptopurine DB00563, Methotrexate DB08840, N-methylnicotinamide DB00157, NADH DB00339, Pyrazinamide DB00481, Raloxifene DB04827, Urethane DB00962, Zaleplon DB00246, Ziprasidone DB00909, Zonisamide |
DrugCentrali | Q06278 |
PTM databases
iPTMneti | Q06278 |
PhosphoSitePlusi | Q06278 |
Genetic variation databases
BioMutai | AOX1 |
DMDMi | 215273968 |
Proteomic databases
EPDi | Q06278 |
jPOSTi | Q06278 |
MassIVEi | Q06278 |
MaxQBi | Q06278 |
PaxDbi | Q06278 |
PeptideAtlasi | Q06278 |
PRIDEi | Q06278 |
ProteomicsDBi | 58430 |
Protocols and materials databases
Antibodypediai | 34105, 228 antibodies |
Genome annotation databases
Ensembli | ENST00000374700; ENSP00000363832; ENSG00000138356 |
GeneIDi | 316 |
KEGGi | hsa:316 |
UCSCi | uc002uvx.4, human |
Organism-specific databases
CTDi | 316 |
DisGeNETi | 316 |
GeneCardsi | AOX1 |
HGNCi | HGNC:553, AOX1 |
HPAi | ENSG00000138356, Tissue enriched (liver) |
MIMi | 602841, gene |
neXtProti | NX_Q06278 |
OpenTargetsi | ENSG00000138356 |
PharmGKBi | PA24842 |
VEuPathDBi | HostDB:ENSG00000138356.13 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0430, Eukaryota |
GeneTreei | ENSGT00950000183114 |
HOGENOMi | CLU_001681_1_2_1 |
InParanoidi | Q06278 |
OMAi | FRFWHEV |
OrthoDBi | 48717at2759 |
PhylomeDBi | Q06278 |
TreeFami | TF353036 |
Enzyme and pathway databases
BioCyci | MetaCyc:ENSG00000138356-MONOMER |
BRENDAi | 1.2.3.1, 2681 |
PathwayCommonsi | Q06278 |
Reactomei | R-HSA-964975, Vitamins B6 activation to pyridoxal phosphate |
SABIO-RKi | Q06278 |
Miscellaneous databases
BioGRID-ORCSi | 316, 5 hits in 988 CRISPR screens |
ChiTaRSi | AOX1, human |
GeneWikii | Aldehyde_oxidase_1 |
GenomeRNAii | 316 |
Pharosi | Q06278, Tbio |
PROi | PR:Q06278 |
RNActi | Q06278, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000138356, Expressed in adrenal gland and 194 other tissues |
ExpressionAtlasi | Q06278, baseline and differential |
Genevisiblei | Q06278, HS |
Family and domain databases
InterProi | View protein in InterPro IPR002888, 2Fe-2S-bd IPR036884, 2Fe-2S-bd_dom_sf IPR036010, 2Fe-2S_ferredoxin-like_sf IPR001041, 2Fe-2S_ferredoxin-type IPR006058, 2Fe2S_fd_BS IPR000674, Ald_Oxase/Xan_DH_a/b IPR036856, Ald_Oxase/Xan_DH_a/b_sf IPR016208, Ald_Oxase/xanthine_DH IPR014313, Aldehyde_oxidase IPR008274, AldOxase/xan_DH_Mopterin-bd IPR037165, AldOxase/xan_DH_Mopterin-bd_sf IPR005107, CO_DH_flav_C IPR036683, CO_DH_flav_C_dom_sf IPR016166, FAD-bd_PCMH IPR036318, FAD-bd_PCMH-like_sf IPR002346, Mopterin_DH_FAD-bd IPR022407, OxRdtase_Mopterin_BS |
Pfami | View protein in Pfam PF01315, 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 |
PIRSFi | PIRSF000127, Xanthine_DH, 1 hit |
SMARTi | View protein in SMART SM01008, Ald_Xan_dh_C, 1 hit SM01092, CO_deh_flav_C, 1 hit |
SUPFAMi | SSF47741, SSF47741, 1 hit SSF54292, SSF54292, 1 hit SSF54665, SSF54665, 1 hit SSF55447, SSF55447, 1 hit SSF56003, SSF56003, 1 hit SSF56176, SSF56176, 1 hit |
TIGRFAMsi | TIGR02969, mam_aldehyde_ox, 1 hit |
PROSITEi | View protein in PROSITE PS00197, 2FE2S_FER_1, 1 hit PS51085, 2FE2S_FER_2, 1 hit PS51387, FAD_PCMH, 1 hit PS00559, MOLYBDOPTERIN_EUK, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | AOXA_HUMAN | |
Accessioni | Q06278Primary (citable) accession number: Q06278 Secondary accession number(s): O14765 Q9UPG6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | November 25, 2008 | |
Last modified: | April 7, 2021 | |
This is version 201 of the entry and version 2 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, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families