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UniProtKB - Q06278 (AOXA_HUMAN)

Protein

Aldehyde oxidase

Gene

AOX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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

<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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
  1. KM=4.6 µM for benzaldehyde (in the presence of 2,6-dichlorophenol indophenol as electron acceptor)1 Publication
  2. KM=45.18 µM for benzaldehyde (in the presence of ferricyanide as electron acceptor)1 Publication
  3. KM=1.3 µM for phthalazine (at 25 degrees Celsius and pH 7.5)1 Publication
  4. KM=8.96 µM for phthalazine (in the presence of 2,6-dichlorophenol indophenol as electron acceptor)1 Publication
  5. KM=125.7 µM for phthalazine (in the presence of ferricyanide as electron acceptor)1 Publication
  6. KM=0.78 µM for phenanthridine (in the pres 2,6-dichlorophenol indophenol as electron acceptor)1 Publication
  7. KM=25.5 µM for phenanthridine (in the presence of ferricyanide as electron acceptor)1 Publication
  8. KM=26.53 µM for phenanthridine (in the presence of molecular oxygen as electron acceptor)1 Publication
  9. KM=3.9 µM for phenanthridine (at 25 degrees Celsius and pH 7.5)1 Publication
  10. KM=5.2 µM for chloroquinazolinone (at 25 degrees Celsius and pH 7.5)1 Publication
  11. KM=0.42 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)1 Publication
  12. KM=0.15 mM for famciclovir (at 37 degrees Celsius and pH 7)1 Publication
  13. KM=6.3 µM for N-[(2-dimethylamino)ethyl]acridine-4-carboxamide (at 37 degrees Celsius and pH 7.4)1 Publication
  1. Vmax=16 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate1 Publication
  2. Vmax=61 nmol/min/mg enzyme with famciclovir as substrate1 Publication
  3. Vmax=2.3 nmol/min/mg enzyme with N-[(2-dimethylamino)ethyl]acridine-4-carboxamide as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi44Iron-sulfur 1 (2Fe-2S)Combined sources1 Publication1
Metal bindingi49Iron-sulfur 1 (2Fe-2S)Combined sources2 Publications1
Metal bindingi52Iron-sulfur 1 (2Fe-2S)Combined sources2 Publications1
Metal bindingi74Iron-sulfur 1 (2Fe-2S)Combined sources2 Publications1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei113MolybdopterinCombined sources1 Publication1
Metal bindingi114Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications1
Metal bindingi117Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications1
Metal bindingi149Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications1
Metal bindingi151Iron-sulfur 2 (2Fe-2S)Combined sources2 Publications1
Binding sitei151MolybdopterinCombined sources2 Publications1
Binding sitei345FAD; via amide nitrogenCombined sources1 Publication1
Binding sitei354FADCombined sources2 Publications1
Binding sitei358FADCombined sources2 Publications1
Binding sitei367FADCombined sources2 Publications1
Binding sitei411FAD; via amide nitrogen and carbonyl oxygenCombined sources2 Publications1
Binding sitei1047Molybdopterin; via carbonyl oxygenCombined sources2 Publications1
Binding sitei1203MolybdopterinCombined sources2 Publications1
Binding sitei1268Molybdopterin; via carbonyl oxygenCombined sources1 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1270Proton acceptor; for azaheterocycle hydroxylase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi264 – 271FADCombined sources2 Publications8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:ENSG00000138356-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.2.3.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-964975 Vitamins B6 activation to pyridoxal phosphate

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q06278

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Aldehyde oxidaseImported (EC:1.2.3.12 Publications)
Alternative name(s):
Aldehyde oxidase 1
Azaheterocycle hydroxylase2 Publications (EC:1.17.3.-2 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AOX1Imported
Synonyms:AO
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000138356.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:553 AOX1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		602841 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q06278

<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 Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi44C → W: Disrupts protein stability. 1 Publication1
Mutagenesisi1269G → R: No effect on dimerization. Loss of oxidase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		316

Open Targets

More...OpenTargetsi		ENSG00000138356

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA24842

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3257

Drug and drug target database

More...DrugBanki		DB00437 Allopurinol
DB00513 Aminocaproic Acid
DB00484 Brimonidine
DB03516 Eniluracil
DB04827 Ethyl carbamate
DB00426 Famciclovir
DB09054 Idelalisib
DB09078 Lenvatinib
DB00170 Menadione
DB01033 Mercaptopurine
DB00563 Methotrexate
DB00157 NADH
DB00339 Pyrazinamide
DB00481 Raloxifene
DB00962 Zaleplon
DB00909 Zonisamide

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		AOX1

Domain mapping of disease mutations (DMDM)

More...DMDMi		215273968

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001661041 – 1338Aldehyde oxidaseAdd BLAST1338

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1068PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q06278

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q06278

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q06278

PeptideAtlas

More...PeptideAtlasi		Q06278

PRoteomics IDEntifications database

More...PRIDEi		Q06278

ProteomicsDB human proteome resource

More...ProteomicsDBi		58430

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q06278

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q06278

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000138356 Expressed in 173 organ(s), highest expression level in adrenal gland

CleanEx database of gene expression profiles

More...CleanExi		HS_AOX1

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q06278 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q06278 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA040199
HPA040215

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-3926368,EBI-3926368

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		106813, 7 interactors

Database of interacting proteins

More...DIPi		DIP-61698N

Protein interaction database and analysis system

More...IntActi		Q06278, 4 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000363832

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q06278

<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

11338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q06278

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q06278

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini5 – 922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini236 – 421FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni806 – 807Molybdopterin bindingCombined sources2 Publications2
Regioni1088 – 1091Molybdopterin bindingCombined sources2 Publications4

<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

Belongs to the xanthine dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0430 Eukaryota
COG4630 LUCA
COG4631 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153396

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000191197

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG004182

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q06278

KEGG Orthology (KO)

More...KOi		K00157

Identification of Orthologs from Complete Genome Data

More...OMAi		ISVNIPY

Database of Orthologous Groups

More...OrthoDBi		EOG091G01AW

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q06278

TreeFam database of animal gene trees

More...TreeFami		TF353036

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...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

Pfam protein domain database

More...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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000127 Xanthine_DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01008 Ald_Xan_dh_C, 1 hit
SM01092 CO_deh_flav_C, 1 hit

Superfamily database of structural and functional annotation

More...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

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02969 mam_aldehyde_ox, 1 hit

PROSITE; a protein domain and family database

More...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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
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MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG 
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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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2AB5E543F18C9261
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9J244C9J244_HUMAN
Aldehyde oxidase
AOX1
151Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C3Q1H7C3Q1_HUMAN
Aldehyde oxidase
AOX1
190Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7BXF7H7BXF7_HUMAN
Aldehyde oxidase
AOX1
193Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<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

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
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_061136314Q → R. Corresponds to variant dbSNP:rs58185012Ensembl.1
Natural variantiVAR_047517802R → C Decreases homodimerization but nearly no effect on kinetic parameters. 1 PublicationCorresponds to variant dbSNP:rs41309768Ensembl.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 dbSNP:rs56199635Ensembl.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 dbSNP:rs55754655Ensembl.1
Natural variantiVAR_0702581271S → L No effect on dimerization; no effect on oxidase activity. 2 PublicationsCorresponds to variant dbSNP:rs141786030Ensembl.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 dbSNP:rs3731722Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS33360.1

Protein sequence database of the Protein Information Resource

More...PIRi		A49634

NCBI Reference Sequences

More...RefSeqi		NP_001150.3, NM_001159.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.406238

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000374700; ENSP00000363832; ENSG00000138356

Database of genes from NCBI RefSeq genomes

More...GeneIDi		316

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:316

UCSC genome browser

More...UCSCi		uc002uvx.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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, 7 interactors
DIPiDIP-61698N
IntActiQ06278, 4 interactors
STRINGi9606.ENSP00000363832

Chemistry databases

BindingDBiQ06278
ChEMBLiCHEMBL3257
DrugBankiDB00437 Allopurinol
DB00513 Aminocaproic Acid
DB00484 Brimonidine
DB03516 Eniluracil
DB04827 Ethyl carbamate
DB00426 Famciclovir
DB09054 Idelalisib
DB09078 Lenvatinib
DB00170 Menadione
DB01033 Mercaptopurine
DB00563 Methotrexate
DB00157 NADH
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
ProteomicsDBi58430

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		316
DisGeNETi316
EuPathDBiHostDB:ENSG00000138356.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		AOX1

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0029780
HGNCiHGNC:553 AOX1
HPAiHPA040199
HPA040215
MIMi602841 gene
neXtProtiNX_Q06278
OpenTargetsiENSG00000138356
PharmGKBiPA24842

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0430 Eukaryota
COG4630 LUCA
COG4631 LUCA
GeneTreeiENSGT00940000153396
HOGENOMiHOG000191197
HOVERGENiHBG004182
InParanoidiQ06278
KOiK00157
OMAiISVNIPY
OrthoDBiEOG091G01AW
PhylomeDBiQ06278
TreeFamiTF353036

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138356-MONOMER
BRENDAi1.2.3.1 2681
ReactomeiR-HSA-964975 Vitamins B6 activation to pyridoxal phosphate
SABIO-RKiQ06278

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		AOX1 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Aldehyde_oxidase_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		316

Protein Ontology

More...PROi		PR:Q06278

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000138356 Expressed in 173 organ(s), highest expression level in adrenal gland
CleanExiHS_AOX1
ExpressionAtlasiQ06278 baseline and differential
GenevisibleiQ06278 HS

Family and domain databases

InterProiView 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
PfamiView 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
PIRSFiPIRSF000127 Xanthine_DH, 1 hit
SMARTiView protein in SMART
SM01008 Ald_Xan_dh_C, 1 hit
SM01092 CO_deh_flav_C, 1 hit
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
PROSITEiView 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAOXA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q06278
Secondary accession number(s): O14765
, Q53RR8, Q53TV3, Q9BYF0, Q9UPG6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 25, 2008
Last modified: December 5, 2018
This is version 184 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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