Reviewed,
UniProtKB/Swiss-Prot Q06278 (ADO_HUMAN)
Last modified
November 25, 2008.
Version 82.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aldehyde oxidase EC=1.2.3.1 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1338 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Catalytic activity | An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2). |
| Cofactor | Binds 2 2Fe-2S clusters. FAD. Molybdopterin. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Tissue specificity | Abundant in liver, lower levels in lung, skeletal muscle, pancreas. Undetected in heart, brain and kidney. |
| Sequence similarities | Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain. |
| Caution | Was originally (Ref.1) thought to be a xanthine dehydrogenase. |
| Sequence caution | The sequence AAA96650.1 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302. The sequence AAB83966.1 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1338 | 1338 | Aldehyde oxidase | PRO_0000166104 | |||||
Regions | |||||||||
| Domain | 5 – 92 | 88 | 2Fe-2S ferredoxin-type | ||||||
| Domain | 236 – 421 | 186 | FAD-binding PCMH-type | ||||||
Sites | |||||||||
| Metal binding | 44 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 49 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 52 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 802 | 1 | R → C: dbSNP rs41309768. | VAR_047517 | |||||
| Natural variant | 1297 | 1 | H → R: dbSNP rs3731722. | VAR_047518 | |||||
Experimental info | |||||||||
| Sequence conflict | 41 | 1 | K → P in AAA96650. Ref.1 | ||||||
| Sequence conflict | 41 | 1 | K → P in AAB83966. Ref.2 | ||||||
| Sequence conflict | 127 | 1 | T → P in AAA96650. Ref.1 | ||||||
| Sequence conflict | 127 | 1 | T → P in AAB83966. Ref.2 | ||||||
| Sequence conflict | 152 | 1 | T → H in AAA96650. Ref.1 | ||||||
| Sequence conflict | 152 | 1 | T → H in AAB83966. Ref.2 | ||||||
| Sequence conflict | 227 | 1 | E → D in AAA96650. Ref.1 | ||||||
| Sequence conflict | 227 | 1 | E → D in AAB83966. Ref.2 | ||||||
| Sequence conflict | 251 | 1 | E → D in AAA96650. Ref.1 | ||||||
| Sequence conflict | 418 | 1 | Y → I in AAA96650. Ref.1 | ||||||
| Sequence conflict | 418 | 1 | Y → I in AAB83966. Ref.2 | ||||||
| Sequence conflict | 501 | 1 | V → L in AAB83966. Ref.2 | ||||||
| Sequence conflict | 627 | 1 | I → N in AAB83966. Ref.2 | ||||||
| Sequence conflict | 929 | 1 | A → V in AAA96650. Ref.1 | ||||||
| Sequence conflict | 929 | 1 | A → V in AAB83966. Ref.2 | ||||||
| Sequence conflict | 1019 | 1 | G → A in AAA96650. Ref.1 | ||||||
| Sequence conflict | 1019 | 1 | G → A in AAB83966. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase." Wright R.M., Vaitaitis G.M., Wilson C.M., Repine T.B., Terada L.S., Repine J.E. Proc. Natl. Acad. Sci. U.S.A. 90:10690-10694(1993) [PubMed: 8248161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Molecular cloning, refined chromosomal mapping, and structural analysis of the human gene encoding aldehyde oxidase (AOX1), a candidate for the ALS2 gene." Wright R.M., Weigel L.K., Varella-Garcia M., Vaitaitis G., Repine J.E. Redox Rep. 3:135-144(1997) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| L11005 mRNA. Translation: AAA96650.1. Frameshift. AF017060 AF009474 Genomic DNA. Translation: AAB83966.1. Frameshift.AF010260 Genomic DNA. Translation: AAB83968.1. AC007163 Genomic DNA. Translation: AAX93285.1. AC080164 Genomic DNA. Translation: AAY24265.1. | |
| PIR | A49634. |
| UniGene | Hs.406238 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FO4 based on UniProtKB P80457. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q06278. |
Genome annotation databases | |
| Ensembl | ENSG00000138356. Homo sapiens. [Contig view] |
Organism-specific databases | |
| H-InvDB | HIX0029780. |
| HGNC | HGNC:553. AOX1. |
| MIM | 602841. gene. |
| PharmGKB | PA24842. |
| GenAtlas | Search... |
| GeneCards | Search... |
Phylogenomic databases | |
| HOVERGEN | Q06278. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:ENSG00000138356-MON. |
Gene expression databases | |
| ArrayExpress | Q06278. |
| CleanEx | HS_AOX1. |
| GermOnline | ENSG00000138356. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DHase_a/b. IPR016208. Ald_Oxase/xanthine_DHase. IPR014313. Aldehyde_oxidase. IPR008274. AldOxase/xan_DHase_Mopterin-bd. IPR012675. b-grasp_ferredoxin-like. IPR005107. CO_DHase_flav_C. IPR016169. CO_DHase_flavot_FAD-bd_sub2. IPR016167. FAD-bd_2_sub1. IPR001041. Ferredoxin. IPR002346. Mopterin_DHase_FAD-bd. IPR000572. OxRdtase_Mopterin-bd. [Graphical view] |
| Gene3D | G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit. G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. |
| 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. [Graphical view] |
| PIRSF | PIRSF000127. Xanthine_DH. 1 hit. |
| ProDom | PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR02969. mam_aldehyde_ox. 1 hit. |
| PROSITE | PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00484. Brimonidine. DB00477. Chlorpromazine. DB00426. Famciclovir. DB00170. Menadione. DB00563. Methotrexate. DB00157. NADH. DB00377. Palonosetron. DB00299. Penciclovir. DB00481. Raloxifene. DB00962. Zaleplon. DB00909. Zonisamide. |
| LinkHub | Q06278. |
| SOURCE | Search... |
Entry information
| Entry name | ADO_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q06278 Secondary accession number(s): O14765 Q9UPG6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 2 Human chromosome 2: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


