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P47989

- XDH_HUMAN

UniProt

P47989 - XDH_HUMAN

Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    Catalytic activityi

    Hypoxanthine + NAD+ + H2O = xanthine + NADH.
    Xanthine + H2O + O2 = urate + H2O2.

    Cofactori

    Binds 2 2Fe-2S clusters.1 Publication
    FAD.1 Publication
    Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit.1 Publication

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi43 – 431Iron-sulfur (2Fe-2S) 1
    Metal bindingi48 – 481Iron-sulfur (2Fe-2S) 1
    Metal bindingi51 – 511Iron-sulfur (2Fe-2S) 1
    Metal bindingi73 – 731Iron-sulfur (2Fe-2S) 1
    Metal bindingi113 – 1131Iron-sulfur (2Fe-2S) 2
    Metal bindingi116 – 1161Iron-sulfur (2Fe-2S) 2
    Metal bindingi148 – 1481Iron-sulfur (2Fe-2S) 2
    Metal bindingi150 – 1501Iron-sulfur (2Fe-2S) 2
    Binding sitei337 – 3371FAD2 Publications
    Binding sitei360 – 3601FAD2 Publications
    Binding sitei404 – 4041FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei422 – 4221FAD2 Publications
    Metal bindingi768 – 7681Molybdenum
    Metal bindingi799 – 7991Molybdenum; via carbonyl oxygen
    Binding sitei803 – 8031SubstrateBy similarity
    Binding sitei881 – 8811Substrate
    Metal bindingi913 – 9131Molybdenum; via amide nitrogen
    Binding sitei915 – 9151SubstrateBy similarity
    Binding sitei1011 – 10111Substrate
    Metal bindingi1080 – 10801Molybdenum; via amide nitrogen
    Active sitei1262 – 12621Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi257 – 2648FAD2 Publications
    Nucleotide bindingi347 – 3515FAD2 Publications

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
    2. electron carrier activity Source: InterPro
    3. flavin adenine dinucleotide binding Source: UniProtKB
    4. iron ion binding Source: InterPro
    5. molybdopterin cofactor binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
    8. xanthine dehydrogenase activity Source: UniProtKB
    9. xanthine oxidase activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    2. lactation Source: Ensembl
    3. negative regulation of endothelial cell differentiation Source: UniProtKB
    4. negative regulation of endothelial cell proliferation Source: UniProtKB
    5. negative regulation of gene expression Source: UniProtKB
    6. negative regulation of protein kinase B signaling Source: UniProtKB
    7. negative regulation of protein phosphorylation Source: UniProtKB
    8. negative regulation of vascular endothelial growth factor signaling pathway Source: UniProtKB
    9. negative regulation of vasculogenesis Source: UniProtKB
    10. nucleobase-containing small molecule metabolic process Source: Reactome
    11. positive regulation of p38MAPK cascade Source: UniProtKB
    12. positive regulation of reactive oxygen species metabolic process Source: UniProtKB
    13. purine nucleobase metabolic process Source: Reactome
    14. purine nucleotide catabolic process Source: Reactome
    15. small molecule metabolic process Source: Reactome
    16. xanthine catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08270-MONOMER.
    ReactomeiREACT_2086. Purine catabolism.
    SABIO-RKP47989.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Xanthine dehydrogenase/oxidase
    Including the following 2 domains:
    Xanthine dehydrogenase (EC:1.17.1.4)
    Short name:
    XD
    Xanthine oxidase (EC:1.17.3.2)
    Short name:
    XO
    Alternative name(s):
    Xanthine oxidoreductase
    Short name:
    XOR
    Gene namesi
    Name:XDH
    Synonyms:XDHA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12805. XDH.

    Subcellular locationi

    Cytoplasm By similarity. Peroxisome By similarity. Secreted

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular space Source: UniProt
    3. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Xanthinuria 1 (XU1) [MIM:278300]: A 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. Xanthinuria 1 is due to isolated xanthine dehydrogenase deficiency. Patients can metabolize allopurinol.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti149 – 1491R → C in XU1. 1 Publication
    VAR_045900

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi803 – 8031E → V: Strongly decreased activity towards xanthine and hypoxanthine. Increased affinity and activity towards aromatic aldehydes.
    Mutagenesisi881 – 8811R → M: Abolishes xanthine oxidase activity.

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi278300. phenotype.
    Orphaneti93601. Xanthinuria type I.
    PharmGKBiPA37404.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 13331332Xanthine dehydrogenase/oxidasePRO_0000166084Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi509 ↔ 1318In oxidase form1 Publication
    Disulfide bondi536 ↔ 993In oxidase form1 Publication
    Glycosylationi1074 – 10741N-linked (GlcNAc...)1 Publication

    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, Glycoprotein

    Proteomic databases

    MaxQBiP47989.
    PaxDbiP47989.
    PeptideAtlasiP47989.
    PRIDEiP47989.

    PTM databases

    PhosphoSiteiP47989.

    Expressioni

    Tissue specificityi

    Detected in milk (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP47989.
    BgeeiP47989.
    CleanExiHS_XDH.
    GenevestigatoriP47989.

    Organism-specific databases

    HPAiCAB009518.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with BTN1A1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi113335. 4 interactions.
    IntActiP47989. 2 interactions.
    STRINGi9606.ENSP00000368727.

    Structurei

    Secondary structure

    1
    1333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105
    Beta strandi13 – 175
    Helixi26 – 327
    Beta strandi44 – 485
    Beta strandi52 – 598
    Turni60 – 634
    Beta strandi64 – 718
    Turni72 – 743
    Helixi77 – 793
    Beta strandi84 – 863
    Helixi88 – 903
    Helixi100 – 1078
    Helixi117 – 13014
    Helixi136 – 1416
    Turni142 – 1454
    Beta strandi149 – 1513
    Helixi154 – 1607
    Helixi161 – 1633
    Helixi198 – 2003
    Helixi206 – 2083
    Helixi214 – 2185
    Beta strandi227 – 2304
    Beta strandi235 – 2384
    Helixi242 – 25110
    Helixi264 – 2707
    Beta strandi276 – 2805
    Helixi285 – 2884
    Beta strandi290 – 2923
    Beta strandi294 – 3007
    Helixi305 – 31814
    Helixi321 – 3233
    Helixi325 – 33511
    Helixi340 – 3456
    Helixi348 – 3547
    Helixi362 – 3676
    Beta strandi371 – 3755
    Beta strandi380 – 3845
    Helixi387 – 3893
    Beta strandi403 – 4108
    Beta strandi416 – 4238
    Beta strandi425 – 4295
    Beta strandi433 – 44210
    Beta strandi448 – 46518
    Helixi467 – 4715
    Turni472 – 4754
    Beta strandi477 – 4793
    Helixi480 – 49314
    Helixi505 – 52925
    Turni541 – 5433
    Helixi544 – 5474
    Beta strandi556 – 5605
    Helixi583 – 5875
    Helixi594 – 5963
    Beta strandi604 – 6107
    Beta strandi612 – 62211
    Helixi626 – 6283
    Beta strandi632 – 6376
    Helixi638 – 6403
    Beta strandi645 – 6484
    Beta strandi653 – 6564
    Beta strandi659 – 6613
    Beta strandi667 – 6759
    Helixi676 – 6849
    Beta strandi687 – 6926
    Helixi699 – 7057
    Beta strandi708 – 71811
    Helixi720 – 7267
    Beta strandi728 – 73710
    Beta strandi749 – 7546
    Beta strandi761 – 7655
    Helixi770 – 78112
    Helixi785 – 7873
    Beta strandi788 – 7936
    Turni799 – 8024
    Helixi807 – 82014
    Beta strandi824 – 8274
    Helixi830 – 8378
    Beta strandi843 – 8519
    Beta strandi857 – 87115
    Helixi875 – 88410
    Beta strandi893 – 90311
    Turni913 – 9164
    Helixi917 – 93519
    Helixi939 – 9457
    Helixi965 – 97612
    Helixi978 – 99114
    Beta strandi993 – 100917
    Helixi1013 – 10153
    Beta strandi1017 – 10248
    Beta strandi1030 – 10356
    Beta strandi1039 – 10413
    Helixi1043 – 105513
    Helixi1059 – 10613
    Turni1069 – 10713
    Helixi1083 – 110826
    Helixi1114 – 112310
    Beta strandi1129 – 11357
    Turni1143 – 11464
    Beta strandi1152 – 116615
    Turni1167 – 11693
    Beta strandi1172 – 118211
    Helixi1189 – 120820
    Turni1225 – 12273
    Helixi1233 – 12353
    Beta strandi1238 – 12447
    Helixi1254 – 12563
    Helixi1263 – 12686
    Helixi1269 – 128618
    Helixi1303 – 13097
    Helixi1315 – 13173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CKJX-ray3.59A/B/C/D2-1333[»]
    2E1QX-ray2.60A/B/C/D1-1333[»]
    ProteinModelPortaliP47989.
    SMRiP47989. Positions 3-164, 195-528, 572-1316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP47989.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 91882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini229 – 414186FAD-binding PCMH-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG4630.
    HOGENOMiHOG000191197.
    HOVERGENiHBG004182.
    InParanoidiP47989.
    KOiK00106.
    OMAiFHMENSY.
    OrthoDBiEOG7QRQSZ.
    PhylomeDBiP47989.
    TreeFamiTF353036.

    Family and domain databases

    Gene3Di1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    3.30.365.10. 6 hits.
    3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    3.90.1170.50. 1 hit.
    InterProiIPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR016208. Ald_Oxase/xanthine_DH.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR012675. Beta-grasp_dom.
    IPR005107. CO_DH_flav_C.
    IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR002346. Mopterin_DH_FAD-bd.
    IPR022407. OxRdtase_Mopterin_BS.
    IPR014307. Xanthine_DH_ssu.
    [Graphical view]
    PfamiPF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    PF03450. CO_deh_flav_C. 1 hit.
    PF00941. FAD_binding_5. 1 hit.
    PF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
    SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
    SM01092. CO_deh_flav_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    SSF54665. SSF54665. 1 hit.
    SSF55447. SSF55447. 1 hit.
    SSF56003. SSF56003. 1 hit.
    SSF56176. SSF56176. 1 hit.
    TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
    PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51387. FAD_PCMH. 1 hit.
    PS00559. MOLYBDOPTERIN_EUK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P47989-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTADKLVFFV NGRKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA     50
    CTVMLSKYDR LQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKTRLHP 100
    VQERIAKSHG SQCGFCTPGI VMSMYTLLRN QPEPTMEEIE NAFQGNLCRC 150
    TGYRPILQGF RTFARDGGCC GGDGNNPNCC MNQKKDHSVS LSPSLFKPEE 200
    FTPLDPTQEP IFPPELLRLK DTPRKQLRFE GERVTWIQAS TLKELLDLKA 250
    QHPDAKLVVG NTEIGIEMKF KNMLFPMIVC PAWIPELNSV EHGPDGISFG 300
    AACPLSIVEK TLVDAVAKLP AQKTEVFRGV LEQLRWFAGK QVKSVASVGG 350
    NIITASPISD LNPVFMASGA KLTLVSRGTR RTVQMDHTFF PGYRKTLLSP 400
    EEILLSIEIP YSREGEYFSA FKQASRREDD IAKVTSGMRV LFKPGTTEVQ 450
    ELALCYGGMA NRTISALKTT QRQLSKLWKE ELLQDVCAGL AEELHLPPDA 500
    PGGMVDFRCT LTLSFFFKFY LTVLQKLGQE NLEDKCGKLD PTFASATLLF 550
    QKDPPADVQL FQEVPKGQSE EDMVGRPLPH LAADMQASGE AVYCDDIPRY 600
    ENELSLRLVT STRAHAKIKS IDTSEAKKVP GFVCFISADD VPGSNITGIC 650
    NDETVFAKDK VTCVGHIIGA VVADTPEHTQ RAAQGVKITY EELPAIITIE 700
    DAIKNNSFYG PELKIEKGDL KKGFSEADNV VSGEIYIGGQ EHFYLETHCT 750
    IAVPKGEAGE MELFVSTQNT MKTQSFVAKM LGVPANRIVV RVKRMGGGFG 800
    GKETRSTVVS TAVALAAYKT GRPVRCMLDR DEDMLITGGR HPFLARYKVG 850
    FMKTGTVVAL EVDHFSNVGN TQDLSQSIME RALFHMDNCY KIPNIRGTGR 900
    LCKTNLPSNT AFRGFGGPQG MLIAECWMSE VAVTCGMPAE EVRRKNLYKE 950
    GDLTHFNQKL EGFTLPRCWE ECLASSQYHA RKSEVDKFNK ENCWKKRGLC 1000
    IIPTKFGISF TVPFLNQAGA LLHVYTDGSV LLTHGGTEMG QGLHTKMVQV 1050
    ASRALKIPTS KIYISETSTN TVPNTSPTAA SVSADLNGQA VYAACQTILK 1100
    RLEPYKKKNP SGSWEDWVTA AYMDTVSLSA TGFYRTPNLG YSFETNSGNP 1150
    FHYFSYGVAC SEVEIDCLTG DHKNLRTDIV MDVGSSLNPA IDIGQVEGAF 1200
    VQGLGLFTLE ELHYSPEGSL HTRGPSTYKI PAFGSIPIEF RVSLLRDCPN 1250
    KKAIYASKAV GEPPLFLAAS IFFAIKDAIR AARAQHTGNN VKELFRLDSP 1300
    ATPEKIRNAC VDKFTTLCVT GVPENCKPWS VRV 1333
    Length:1,333
    Mass (Da):146,424
    Last modified:January 23, 2007 - v4
    Checksum:i806FF2C7413F84C5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti259 – 2591V → E in AAA75287. (PubMed:8135849)Curated
    Sequence conflicti333 – 3342QL → HV in AAA75287. (PubMed:8135849)Curated
    Sequence conflicti495 – 4951H → Q in AAA75287. (PubMed:8135849)Curated
    Sequence conflicti515 – 5173FFF → LLL in AAA75287. (PubMed:8135849)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti133 – 1331E → K.1 Publication
    Corresponds to variant rs45447191 [ dbSNP | Ensembl ].
    VAR_023976
    Natural varianti149 – 1491R → C in XU1. 1 Publication
    VAR_045900
    Natural varianti172 – 1721G → R.2 Publications
    Corresponds to variant rs45523133 [ dbSNP | Ensembl ].
    VAR_023977
    Natural varianti235 – 2351T → M.1 Publication
    Corresponds to variant rs45469499 [ dbSNP | Ensembl ].
    VAR_023978
    Natural varianti395 – 3951K → M.1 Publication
    Corresponds to variant rs34929837 [ dbSNP | Ensembl ].
    VAR_023979
    Natural varianti555 – 5551P → S.1 Publication
    Corresponds to variant rs45577338 [ dbSNP | Ensembl ].
    VAR_023980
    Natural varianti584 – 5841D → A.1 Publication
    Corresponds to variant rs45491693 [ dbSNP | Ensembl ].
    VAR_023981
    Natural varianti607 – 6071R → Q.1 Publication
    Corresponds to variant rs45442092 [ dbSNP | Ensembl ].
    VAR_023982
    Natural varianti617 – 6171K → N.1 Publication
    Corresponds to variant rs45442398 [ dbSNP | Ensembl ].
    VAR_023983
    Natural varianti623 – 6231T → I.1 Publication
    Corresponds to variant rs45448694 [ dbSNP | Ensembl ].
    VAR_023984
    Natural varianti646 – 6461I → V.1 Publication
    Corresponds to variant rs17323225 [ dbSNP | Ensembl ].
    VAR_023985
    Natural varianti703 – 7031I → V.1 Publication
    Corresponds to variant rs17011368 [ dbSNP | Ensembl ].
    VAR_023986
    Natural varianti763 – 7631L → F in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035899
    Natural varianti791 – 7911R → G in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035900
    Natural varianti910 – 9101T → M.1 Publication
    Corresponds to variant rs669884 [ dbSNP | Ensembl ].
    VAR_023987
    Natural varianti1091 – 10911V → L.1 Publication
    Corresponds to variant rs45619033 [ dbSNP | Ensembl ].
    VAR_023988
    Natural varianti1109 – 11091N → T.1 Publication
    Corresponds to variant rs45547640 [ dbSNP | Ensembl ].
    VAR_023989
    Natural varianti1150 – 11501P → R.1 Publication
    Corresponds to variant rs1042036 [ dbSNP | Ensembl ].
    VAR_045901
    Natural varianti1176 – 11761R → C.1 Publication
    Corresponds to variant rs45624433 [ dbSNP | Ensembl ].
    VAR_023990
    Natural varianti1296 – 12961R → W.1 Publication
    Corresponds to variant rs45564939 [ dbSNP | Ensembl ].
    VAR_023991

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

    EnsembliENST00000379416; ENSP00000368727; ENSG00000158125.
    GeneIDi7498.
    KEGGihsa:7498.
    UCSCiuc002rnv.1. human.

    Polymorphism databases

    DMDMi2506326.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D11456 mRNA. Translation: BAA02013.2 .
    U06117 mRNA. Translation: AAA75287.1 .
    U39487 mRNA. Translation: AAB08399.1 .
    DQ089481 Genomic DNA. Translation: AAY68219.1 .
    CCDSi CCDS1775.1.
    PIRi S66573. XOHUDH.
    RefSeqi NP_000370.2. NM_000379.3.
    UniGenei Hs.250.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CKJ X-ray 3.59 A/B/C/D 2-1333 [» ]
    2E1Q X-ray 2.60 A/B/C/D 1-1333 [» ]
    ProteinModelPortali P47989.
    SMRi P47989. Positions 3-164, 195-528, 572-1316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113335. 4 interactions.
    IntActi P47989. 2 interactions.
    STRINGi 9606.ENSP00000368727.

    Chemistry

    BindingDBi P47989.
    ChEMBLi CHEMBL1929.
    DrugBanki DB00437. Allopurinol.
    DB01136. Carvedilol.
    DB00694. Daunorubicin.
    DB00746. Deferoxamine.
    DB01189. Desflurane.
    DB00170. Menadione.
    DB01033. Mercaptopurine.
    DB00563. Methotrexate.
    DB00157. NADH.
    DB00336. Nitrofurazone.
    DB01113. Papaverine.
    DB01168. Procarbazine.
    DB00339. Pyrazinamide.
    DB00049. Rasburicase.
    DB00127. Spermine.
    DB00831. Trifluoperazine.
    DB00163. Vitamin E.
    GuidetoPHARMACOLOGYi 2646.

    PTM databases

    PhosphoSitei P47989.

    Polymorphism databases

    DMDMi 2506326.

    Proteomic databases

    MaxQBi P47989.
    PaxDbi P47989.
    PeptideAtlasi P47989.
    PRIDEi P47989.

    Protocols and materials databases

    DNASUi 7498.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379416 ; ENSP00000368727 ; ENSG00000158125 .
    GeneIDi 7498.
    KEGGi hsa:7498.
    UCSCi uc002rnv.1. human.

    Organism-specific databases

    CTDi 7498.
    GeneCardsi GC02M031470.
    H-InvDB HIX0117690.
    HGNCi HGNC:12805. XDH.
    HPAi CAB009518.
    MIMi 278300. phenotype.
    607633. gene.
    neXtProti NX_P47989.
    Orphaneti 93601. Xanthinuria type I.
    PharmGKBi PA37404.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4630.
    HOGENOMi HOG000191197.
    HOVERGENi HBG004182.
    InParanoidi P47989.
    KOi K00106.
    OMAi FHMENSY.
    OrthoDBi EOG7QRQSZ.
    PhylomeDBi P47989.
    TreeFami TF353036.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08270-MONOMER.
    Reactomei REACT_2086. Purine catabolism.
    SABIO-RK P47989.

    Miscellaneous databases

    ChiTaRSi XDH. human.
    EvolutionaryTracei P47989.
    GeneWikii Xanthine_dehydrogenase.
    GenomeRNAii 7498.
    NextBioi 29364.
    PROi P47989.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47989.
    Bgeei P47989.
    CleanExi HS_XDH.
    Genevestigatori P47989.

    Family and domain databases

    Gene3Di 1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    3.30.365.10. 6 hits.
    3.30.43.10. 1 hit.
    3.30.465.10. 1 hit.
    3.90.1170.50. 1 hit.
    InterProi IPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR016208. Ald_Oxase/xanthine_DH.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR012675. Beta-grasp_dom.
    IPR005107. CO_DH_flav_C.
    IPR016169. CO_DH_flavot_FAD-bd_sub2.
    IPR016166. FAD-bd_2.
    IPR016167. FAD-bd_2_sub1.
    IPR002346. Mopterin_DH_FAD-bd.
    IPR022407. OxRdtase_Mopterin_BS.
    IPR014307. Xanthine_DH_ssu.
    [Graphical view ]
    Pfami 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 ]
    PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
    SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
    SM01092. CO_deh_flav_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    SSF54665. SSF54665. 1 hit.
    SSF55447. SSF55447. 1 hit.
    SSF56003. SSF56003. 1 hit.
    SSF56176. SSF56176. 1 hit.
    TIGRFAMsi TIGR02963. xanthine_xdhA. 1 hit.
    PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    PS51387. FAD_PCMH. 1 hit.
    PS00559. MOLYBDOPTERIN_EUK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene."
      Ichida K., Amaya Y., Noda K., Minoshima S., Hosoya T., Sakai O., Shimizu N., Nishino T.
      Gene 133:279-284(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. Ichida K.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 191; 231 AND 1150.
    3. "Molecular cloning, tissue expression of human xanthine dehydrogenase."
      Xu P., Huecksteadt T.P., Harrison R., Hoidal J.R.
      Biochem. Biophys. Res. Commun. 199:998-1004(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-172.
      Tissue: Liver.
    4. "Cloning and expression in vitro of human xanthine dehydrogenase/oxidase."
      Saksela M., Raivio K.O.
      Biochem. J. 315:235-239(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
      Tissue: Small intestine.
    5. NIEHS SNPs program
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-133; ARG-172; MET-235; MET-395; SER-555; ALA-584; GLN-607; ASN-617; ILE-623; VAL-646; VAL-703; MET-910; LEU-1091; THR-1109; CYS-1176 AND TRP-1296.
    6. "Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria."
      Ichida K., Amaya Y., Kamatani N., Nishino T., Hosoya T., Sakai O.
      J. Clin. Invest. 99:2391-2397(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN XU1, VARIANT ARG-1150.
    7. "XDH gene mutation is the underlying cause of classical xanthinuria: a second report."
      Levartovsky D., Lagziel A., Sperling O., Liberman U., Yaron M., Hosoya T., Ichida K., Peretz H.
      Kidney Int. 57:2215-2220(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN XU1.
    8. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
      Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
      Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1074.
      Tissue: Milk.
    9. "Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate."
      Yamaguchi Y., Matsumura T., Ichida K., Okamoto K., Nishino T.
      J. Biochem. 141:513-524(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANT VAL-803 IN COMPLEX WITH FAD; 2FE-2S IRON-SULFUR CENTERS; SALICYLATE; MOLYBDOPTERIN AND CALCIUM IONS, COFACTOR, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.
    10. "Human milk xanthine dehydrogenase is incompletely converted to the oxidase form in the absence of proteolysis. A structural explanation."
      Pearson A.R., Godber B.L.J., Eisenthal R., Taylor G.L., Harrison R.
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) IN COMPLEX WITH FAD AND IRON-SULFUR CENTERS, TISSUE SPECIFICITY, ENZYME REGULATION, DISULFIDE BONDS.
    11. "Identification of a new point mutation in the human xanthine dehydrogenase gene responsible for a case of classical type I xanthinuria."
      Sakamoto N., Yamamoto T., Moriwaki Y., Teranishi T., Toyoda M., Onishi Y., Kuroda S., Sakaguchi K., Fujisawa T., Maeda M., Hada T.
      Hum. Genet. 108:279-283(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT XU1 CYS-149.
    12. "Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria."
      Gok F., Ichida K., Topaloglu R.
      Nephrol. Dial. Transplant. 18:2278-2283(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN XU1.
    13. Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-763 AND GLY-791.

    Entry informationi

    Entry nameiXDH_HUMAN
    AccessioniPrimary (citable) accession number: P47989
    Secondary accession number(s): Q16681, Q16712, Q4PJ16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3