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Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

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

Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro).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:
  • [2Fe-2S] cluster1 PublicationNote: Binds 2 [2Fe-2S] clusters.1 Publication
  • FAD1 Publication
  • Mo-molybdopterin1 PublicationNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.1 Publication

<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

Can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups.By similarity

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 bindingi43Iron-sulfur (2Fe-2S) 11
Metal bindingi48Iron-sulfur (2Fe-2S) 11
Metal bindingi51Iron-sulfur (2Fe-2S) 11
Metal bindingi73Iron-sulfur (2Fe-2S) 11
Metal bindingi113Iron-sulfur (2Fe-2S) 21
Metal bindingi116Iron-sulfur (2Fe-2S) 21
Metal bindingi148Iron-sulfur (2Fe-2S) 21
Metal bindingi150Iron-sulfur (2Fe-2S) 21
<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 sitei337FAD2 Publications1
Binding sitei360FAD2 Publications1
Binding sitei404FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei422FAD2 Publications1
Metal bindingi768Molybdenum1
Metal bindingi799Molybdenum; via carbonyl oxygen1
Binding sitei803SubstrateBy similarity1
Binding sitei881Substrate1
Metal bindingi913Molybdenum; via amide nitrogen1
Binding sitei915SubstrateBy similarity1
Binding sitei1011Substrate1
Metal bindingi1080Molybdenum; via amide nitrogen1
<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 sitei1262Proton acceptor1

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 bindingi257 – 264FAD2 Publications8
Nucleotide bindingi347 – 351FAD2 Publications5

<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

GO - Biological processi

<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, NAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS08270-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.17.1.4 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-74259 Purine catabolism
R-HSA-8851680 Butyrophilin (BTN) family interactions

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P47989

<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:
Xanthine dehydrogenase/oxidase
Including the following 2 domains:
Xanthine dehydrogenase (EC:1.17.1.41 Publication)
Short name:
XD
Xanthine oxidase (EC:1.17.3.22 Publications)
Short name:
XO
Alternative name(s):
Xanthine oxidoreductase
Short name:
XOR
<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:XDH
Synonyms:XDHA
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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:ENSG00000158125.9

Human Gene Nomenclature Database

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HGNCi
HGNC:12805 XDH

Online Mendelian Inheritance in Man (OMIM)

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MIMi
607633 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P47989

<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, Peroxisome, Secreted

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Xanthinuria 1 (XAN1)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. XAN1 is due to isolated xanthine dehydrogenase deficiency. Patients can metabolize allopurinol.
See also OMIM:278300
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_045900149R → C in XAN1. 1 PublicationCorresponds to variant dbSNP:rs72549369EnsemblClinVar.1

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>Mutagenesisi803E → V: Strongly decreased activity towards xanthine and hypoxanthine. Increased affinity and activity towards aromatic aldehydes. 1
Mutagenesisi881R → M: Abolishes xanthine oxidase activity. 1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
7498

MalaCards human disease database

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MalaCardsi
XDH
MIMi278300 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000158125

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
93601 Xanthinuria type I

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37404

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1929

Drug and drug target database

More...
DrugBanki
DB00041 Aldesleukin
DB00437 Allopurinol
DB00993 Azathioprine
DB00958 Carboplatin
DB01136 Carvedilol
DB00856 Chlorphenesin
DB00515 Cisplatin
DB00694 Daunorubicin
DB00746 Deferoxamine
DB03328 dioxothiomolybdenum(VI) ion
DB00997 Doxorubicin
DB03516 Eniluracil
DB04854 Febuxostat
DB03147 Flavin adenine dinucleotide
DB04335 Inosine
DB00583 L-Carnitine
DB00170 Menadione
DB01033 Mercaptopurine
DB00157 NADH
DB00336 Nitrofural
DB05262 Oxypurinol
DB01168 Procarbazine
DB00339 Pyrazinamide
DB00127 Spermine
DB00831 Trifluoperazine
DB03841 Y-700

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2646

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
XDH

Domain mapping of disease mutations (DMDM)

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DMDMi
2506326

<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_00001660841 – 1333Xanthine dehydrogenase/oxidaseAdd BLAST1333

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi509 ↔ 1318In oxidase form1 Publication
Disulfide bondi536 ↔ 993In oxidase form1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Subject to partial proteolysis; this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O).By similarity
Contains sulfhydryl groups that are easily oxidized (in vitro); this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O).By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P47989

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P47989

MaxQB - The MaxQuant DataBase

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MaxQBi
P47989

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

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PaxDbi
P47989

PeptideAtlas

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PeptideAtlasi
P47989

PRoteomics IDEntifications database

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PRIDEi
P47989

ProteomicsDB human proteome resource

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ProteomicsDBi
55829

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P47989

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

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PhosphoSitePlusi
P47989

<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

Detected in milk (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000158125 Expressed in 113 organ(s), highest expression level in jejunal mucosa

CleanEx database of gene expression profiles

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CleanExi
HS_XDH

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P47989 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA062641
HPA069323

<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. Interacts with BTN1A1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113335, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P47989

Protein interaction database and analysis system

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IntActi
P47989, 3 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000368727

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P47989

<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

11333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKJX-ray3.59A/B/C/D2-1333[»]
2E1QX-ray2.60A/B/C/D1-1333[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P47989

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

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SMRi
P47989

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P47989

<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>Domaini4 – 912Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini229 – 414FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

<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

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eggNOGi
KOG0430 Eukaryota
COG4630 LUCA
COG4631 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154561

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000191197

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004182

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P47989

KEGG Orthology (KO)

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KOi
K00106

Identification of Orthologs from Complete Genome Data

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OMAi
VPLMYKQ

Database of Orthologous Groups

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OrthoDBi
858819at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P47989

TreeFam database of animal gene trees

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TreeFami
TF353036

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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
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
IPR014307 Xanthine_DH_ssu

Pfam protein domain database

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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

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PIRSFi
PIRSF000127 Xanthine_DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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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

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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

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TIGRFAMsi
TIGR02963 xanthine_xdhA, 1 hit

PROSITE; a protein domain and family database

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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>Sequencei

<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.

P47989-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTADKLVFFV NGRKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA
60 70 80 90 100
CTVMLSKYDR LQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKTRLHP
110 120 130 140 150
VQERIAKSHG SQCGFCTPGI VMSMYTLLRN QPEPTMEEIE NAFQGNLCRC
160 170 180 190 200
TGYRPILQGF RTFARDGGCC GGDGNNPNCC MNQKKDHSVS LSPSLFKPEE
210 220 230 240 250
FTPLDPTQEP IFPPELLRLK DTPRKQLRFE GERVTWIQAS TLKELLDLKA
260 270 280 290 300
QHPDAKLVVG NTEIGIEMKF KNMLFPMIVC PAWIPELNSV EHGPDGISFG
310 320 330 340 350
AACPLSIVEK TLVDAVAKLP AQKTEVFRGV LEQLRWFAGK QVKSVASVGG
360 370 380 390 400
NIITASPISD LNPVFMASGA KLTLVSRGTR RTVQMDHTFF PGYRKTLLSP
410 420 430 440 450
EEILLSIEIP YSREGEYFSA FKQASRREDD IAKVTSGMRV LFKPGTTEVQ
460 470 480 490 500
ELALCYGGMA NRTISALKTT QRQLSKLWKE ELLQDVCAGL AEELHLPPDA
510 520 530 540 550
PGGMVDFRCT LTLSFFFKFY LTVLQKLGQE NLEDKCGKLD PTFASATLLF
560 570 580 590 600
QKDPPADVQL FQEVPKGQSE EDMVGRPLPH LAADMQASGE AVYCDDIPRY
610 620 630 640 650
ENELSLRLVT STRAHAKIKS IDTSEAKKVP GFVCFISADD VPGSNITGIC
660 670 680 690 700
NDETVFAKDK VTCVGHIIGA VVADTPEHTQ RAAQGVKITY EELPAIITIE
710 720 730 740 750
DAIKNNSFYG PELKIEKGDL KKGFSEADNV VSGEIYIGGQ EHFYLETHCT
760 770 780 790 800
IAVPKGEAGE MELFVSTQNT MKTQSFVAKM LGVPANRIVV RVKRMGGGFG
810 820 830 840 850
GKETRSTVVS TAVALAAYKT GRPVRCMLDR DEDMLITGGR HPFLARYKVG
860 870 880 890 900
FMKTGTVVAL EVDHFSNVGN TQDLSQSIME RALFHMDNCY KIPNIRGTGR
910 920 930 940 950
LCKTNLPSNT AFRGFGGPQG MLIAECWMSE VAVTCGMPAE EVRRKNLYKE
960 970 980 990 1000
GDLTHFNQKL EGFTLPRCWE ECLASSQYHA RKSEVDKFNK ENCWKKRGLC
1010 1020 1030 1040 1050
IIPTKFGISF TVPFLNQAGA LLHVYTDGSV LLTHGGTEMG QGLHTKMVQV
1060 1070 1080 1090 1100
ASRALKIPTS KIYISETSTN TVPNTSPTAA SVSADLNGQA VYAACQTILK
1110 1120 1130 1140 1150
RLEPYKKKNP SGSWEDWVTA AYMDTVSLSA TGFYRTPNLG YSFETNSGNP
1160 1170 1180 1190 1200
FHYFSYGVAC SEVEIDCLTG DHKNLRTDIV MDVGSSLNPA IDIGQVEGAF
1210 1220 1230 1240 1250
VQGLGLFTLE ELHYSPEGSL HTRGPSTYKI PAFGSIPIEF RVSLLRDCPN
1260 1270 1280 1290 1300
KKAIYASKAV GEPPLFLAAS IFFAIKDAIR AARAQHTGNN VKELFRLDSP
1310 1320 1330
ATPEKIRNAC VDKFTTLCVT GVPENCKPWS VRV
Length:1,333
Mass (Da):146,424
Last modified:January 23, 2007 - v4
<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:i806FF2C7413F84C5
GO

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 conflicti259V → E in AAA75287 (PubMed:8135849).Curated1
Sequence conflicti333 – 334QL → HV in AAA75287 (PubMed:8135849).Curated2
Sequence conflicti495H → Q in AAA75287 (PubMed:8135849).Curated1
Sequence conflicti515 – 517FFF → LLL in AAA75287 (PubMed:8135849).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023976133E → K1 PublicationCorresponds to variant dbSNP:rs45447191Ensembl.1
Natural variantiVAR_045900149R → C in XAN1. 1 PublicationCorresponds to variant dbSNP:rs72549369EnsemblClinVar.1
Natural variantiVAR_023977172G → R2 PublicationsCorresponds to variant dbSNP:rs45523133EnsemblClinVar.1
Natural variantiVAR_023978235T → M1 PublicationCorresponds to variant dbSNP:rs45469499Ensembl.1
Natural variantiVAR_023979395K → M1 PublicationCorresponds to variant dbSNP:rs34929837EnsemblClinVar.1
Natural variantiVAR_023980555P → S1 PublicationCorresponds to variant dbSNP:rs45577338Ensembl.1
Natural variantiVAR_023981584D → A1 PublicationCorresponds to variant dbSNP:rs45491693EnsemblClinVar.1
Natural variantiVAR_023982607R → Q1 PublicationCorresponds to variant dbSNP:rs45442092EnsemblClinVar.1
Natural variantiVAR_023983617K → N1 PublicationCorresponds to variant dbSNP:rs45442398Ensembl.1
Natural variantiVAR_023984623T → I1 PublicationCorresponds to variant dbSNP:rs45448694Ensembl.1
Natural variantiVAR_023985646I → V1 PublicationCorresponds to variant dbSNP:rs17323225EnsemblClinVar.1
Natural variantiVAR_023986703I → V1 PublicationCorresponds to variant dbSNP:rs17011368EnsemblClinVar.1
Natural variantiVAR_035899763L → F in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_035900791R → G in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs775646772Ensembl.1
Natural variantiVAR_023987910T → M1 PublicationCorresponds to variant dbSNP:rs669884Ensembl.1
Natural variantiVAR_0239881091V → L1 PublicationCorresponds to variant dbSNP:rs45619033EnsemblClinVar.1
Natural variantiVAR_0239891109N → T1 PublicationCorresponds to variant dbSNP:rs45547640Ensembl.1
Natural variantiVAR_0459011150P → R1 PublicationCorresponds to variant dbSNP:rs1042036Ensembl.1
Natural variantiVAR_0239901176R → C1 PublicationCorresponds to variant dbSNP:rs45624433Ensembl.1
Natural variantiVAR_0239911296R → W1 PublicationCorresponds to variant dbSNP:rs45564939Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D11456 mRNA Translation: BAA02013.2
U06117 mRNA Translation: AAA75287.1
U39487 mRNA Translation: AAB08399.1
DQ089481 Genomic DNA Translation: AAY68219.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1775.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S66573 XOHUDH

NCBI Reference Sequences

More...
RefSeqi
NP_000370.2, NM_000379.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.250

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000379416; ENSP00000368727; ENSG00000158125

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7498

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7498

UCSC genome browser

More...
UCSCi
uc002rnv.2 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

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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11456 mRNA Translation: BAA02013.2
U06117 mRNA Translation: AAA75287.1
U39487 mRNA Translation: AAB08399.1
DQ089481 Genomic DNA Translation: AAY68219.1
CCDSiCCDS1775.1
PIRiS66573 XOHUDH
RefSeqiNP_000370.2, NM_000379.3
UniGeneiHs.250

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKJX-ray3.59A/B/C/D2-1333[»]
2E1QX-ray2.60A/B/C/D1-1333[»]
ProteinModelPortaliP47989
SMRiP47989
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113335, 3 interactors
CORUMiP47989
IntActiP47989, 3 interactors
STRINGi9606.ENSP00000368727

Chemistry databases

BindingDBiP47989
ChEMBLiCHEMBL1929
DrugBankiDB00041 Aldesleukin
DB00437 Allopurinol
DB00993 Azathioprine
DB00958 Carboplatin
DB01136 Carvedilol
DB00856 Chlorphenesin
DB00515 Cisplatin
DB00694 Daunorubicin
DB00746 Deferoxamine
DB03328 dioxothiomolybdenum(VI) ion
DB00997 Doxorubicin
DB03516 Eniluracil
DB04854 Febuxostat
DB03147 Flavin adenine dinucleotide
DB04335 Inosine
DB00583 L-Carnitine
DB00170 Menadione
DB01033 Mercaptopurine
DB00157 NADH
DB00336 Nitrofural
DB05262 Oxypurinol
DB01168 Procarbazine
DB00339 Pyrazinamide
DB00127 Spermine
DB00831 Trifluoperazine
DB03841 Y-700
GuidetoPHARMACOLOGYi2646

PTM databases

iPTMnetiP47989
PhosphoSitePlusiP47989

Polymorphism and mutation databases

BioMutaiXDH
DMDMi2506326

Proteomic databases

EPDiP47989
jPOSTiP47989
MaxQBiP47989
PaxDbiP47989
PeptideAtlasiP47989
PRIDEiP47989
ProteomicsDBi55829

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7498
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379416; ENSP00000368727; ENSG00000158125
GeneIDi7498
KEGGihsa:7498
UCSCiuc002rnv.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7498
DisGeNETi7498
EuPathDBiHostDB:ENSG00000158125.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
XDH

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0117690
HGNCiHGNC:12805 XDH
HPAiHPA062641
HPA069323
MalaCardsiXDH
MIMi278300 phenotype
607633 gene
neXtProtiNX_P47989
OpenTargetsiENSG00000158125
Orphaneti93601 Xanthinuria type I
PharmGKBiPA37404

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0430 Eukaryota
COG4630 LUCA
COG4631 LUCA
GeneTreeiENSGT00940000154561
HOGENOMiHOG000191197
HOVERGENiHBG004182
InParanoidiP47989
KOiK00106
OMAiVPLMYKQ
OrthoDBi858819at2759
PhylomeDBiP47989
TreeFamiTF353036

Enzyme and pathway databases

BioCyciMetaCyc:HS08270-MONOMER
BRENDAi1.17.1.4 2681
ReactomeiR-HSA-74259 Purine catabolism
R-HSA-8851680 Butyrophilin (BTN) family interactions
SABIO-RKiP47989

Miscellaneous databases

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

More...
ChiTaRSi
XDH human
EvolutionaryTraceiP47989

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Xanthine_dehydrogenase

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

More...
GenomeRNAii
7498

Protein Ontology

More...
PROi
PR:P47989

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000158125 Expressed in 113 organ(s), highest expression level in jejunal mucosa
CleanExiHS_XDH
GenevisibleiP47989 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
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
IPR014307 Xanthine_DH_ssu
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
TIGRFAMsiTIGR02963 xanthine_xdhA, 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 nameiXDH_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: P47989
Secondary accession number(s): Q16681, Q16712, Q4PJ16
<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: February 1, 1996
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 195 of the entry and version 4 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
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