SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P47989

- XDH_HUMAN

UniProt

P47989 - XDH_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Xanthine dehydrogenase/oxidase

Gene
XDH, XDHA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications
Xanthine + H2O + O2 = urate + H2O2.2 Publications

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.1 Publication

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 – 3371FAD
Binding sitei360 – 3601FAD
Binding sitei404 – 4041FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei422 – 4221FAD
Metal bindingi768 – 7681Molybdenum
Metal bindingi799 – 7991Molybdenum; via carbonyl oxygen
Binding sitei803 – 8031Substrate By similarity
Binding sitei881 – 8811Substrate
Metal bindingi913 – 9131Molybdenum; via amide nitrogen
Binding sitei915 – 9151Substrate By similarity
Binding sitei1011 – 10111Substrate
Metal bindingi1080 – 10801Molybdenum; via amide nitrogen
Active sitei1262 – 12621Proton acceptor

Regions

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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 – 11Removed By 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.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiP47989.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591V → E in AAA75287. 1 Publication
Sequence conflicti333 – 3342QL → HV in AAA75287. 1 Publication
Sequence conflicti495 – 4951H → Q in AAA75287. 1 Publication
Sequence conflicti515 – 5173FFF → LLL in AAA75287. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 151 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

Similar proteinsi