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Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

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

Xanthine + NAD+ + H2O = urate + NADH.1 Publication
Hypoxanthine + NAD+ + H2O = xanthine + NADH.1 Publication
Xanthine + H2O + O2 = urate + H2O2.2 Publications

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

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)DescriptionActionsGraphical viewLength
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
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
Active sitei1262Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi257 – 264FAD2 Publications8
Nucleotide bindingi347 – 351FAD2 Publications5

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB
  • electron carrier activity Source: InterPro
  • flavin adenine dinucleotide binding Source: UniProtKB
  • iron ion binding Source: InterPro
  • molybdopterin cofactor binding Source: UniProtKB
  • oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors Source: GO_Central
  • protein homodimerization activity Source: UniProtKB
  • xanthine dehydrogenase activity Source: UniProtKB
  • xanthine oxidase activity Source: UniProtKB

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • lactation Source: Ensembl
  • negative regulation of endothelial cell differentiation Source: UniProtKB
  • negative regulation of endothelial cell proliferation Source: UniProtKB
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of protein kinase B signaling Source: UniProtKB
  • negative regulation of protein phosphorylation Source: UniProtKB
  • negative regulation of vascular endothelial growth factor signaling pathway Source: UniProtKB
  • negative regulation of vasculogenesis Source: UniProtKB
  • positive regulation of p38MAPK cascade Source: UniProtKB
  • positive regulation of reactive oxygen species metabolic process Source: UniProtKB
  • purine nucleotide catabolic process Source: Reactome
  • 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.
ZFISH:HS08270-MONOMER.
BRENDAi1.17.1.4. 2681.
ReactomeiR-HSA-74259. Purine catabolism.
SABIO-RKP47989.

Names & Taxonomyi

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
Gene namesi
Name:XDH
Synonyms:XDHA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12805. XDH.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GO_Central
  • extracellular space Source: UniProtKB
  • peroxisome Source: UniProtKB-SubCell
  • sarcoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome, Secreted

Pathology & Biotechi

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
Natural variantiVAR_045900149R → C in XAN1. 1 PublicationCorresponds to variant rs72549369dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi7498.
MalaCardsiXDH.
MIMi278300. phenotype.
OpenTargetsiENSG00000158125.
Orphaneti93601. Xanthinuria type I.
PharmGKBiPA37404.

Chemistry databases

ChEMBLiCHEMBL1929.
DrugBankiDB00041. Aldesleukin.
DB00437. Allopurinol.
DB00993. Azathioprine.
DB00958. Carboplatin.
DB01136. Carvedilol.
DB00856. Chlorphenesin.
DB00515. Cisplatin.
DB00694. Daunorubicin.
DB00746. Deferoxamine.
DB00997. Doxorubicin.
DB04854. Febuxostat.
DB03147. Flavin adenine dinucleotide.
DB00583. L-Carnitine.
DB00170. Menadione.
DB01033. Mercaptopurine.
DB00336. Nitrofural.
DB01168. Procarbazine.
DB00339. Pyrazinamide.
DB00127. Spermine.
DB00831. Trifluoperazine.
GuidetoPHARMACOLOGYi2646.

Polymorphism and mutation databases

BioMutaiXDH.
DMDMi2506326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001660842 – 1333Xanthine dehydrogenase/oxidaseAdd BLAST1332

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi509 ↔ 1318In oxidase form1 Publication
Disulfide bondi536 ↔ 993In oxidase form1 Publication
Glycosylationi1074N-linked (GlcNAc...)1 Publication1

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

EPDiP47989.
MaxQBiP47989.
PaxDbiP47989.
PeptideAtlasiP47989.
PRIDEiP47989.

PTM databases

iPTMnetiP47989.
PhosphoSitePlusiP47989.

Expressioni

Tissue specificityi

Detected in milk (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000158125.
CleanExiHS_XDH.
GenevisibleiP47989. HS.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi113335. 3 interactors.
IntActiP47989. 3 interactors.
STRINGi9606.ENSP00000368727.

Chemistry databases

BindingDBiP47989.

Structurei

Secondary structure

11333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Beta strandi13 – 17Combined sources5
Helixi26 – 32Combined sources7
Beta strandi44 – 48Combined sources5
Beta strandi52 – 59Combined sources8
Turni60 – 63Combined sources4
Beta strandi64 – 71Combined sources8
Turni72 – 74Combined sources3
Helixi77 – 79Combined sources3
Beta strandi84 – 86Combined sources3
Helixi88 – 90Combined sources3
Helixi100 – 107Combined sources8
Helixi117 – 130Combined sources14
Helixi136 – 141Combined sources6
Turni142 – 145Combined sources4
Beta strandi149 – 151Combined sources3
Helixi154 – 160Combined sources7
Helixi161 – 163Combined sources3
Helixi198 – 200Combined sources3
Helixi206 – 208Combined sources3
Helixi214 – 218Combined sources5
Beta strandi227 – 230Combined sources4
Beta strandi235 – 238Combined sources4
Helixi242 – 251Combined sources10
Helixi264 – 270Combined sources7
Beta strandi276 – 280Combined sources5
Helixi285 – 288Combined sources4
Beta strandi290 – 292Combined sources3
Beta strandi294 – 300Combined sources7
Helixi305 – 318Combined sources14
Helixi321 – 323Combined sources3
Helixi325 – 335Combined sources11
Helixi340 – 345Combined sources6
Helixi348 – 354Combined sources7
Helixi362 – 367Combined sources6
Beta strandi371 – 375Combined sources5
Beta strandi380 – 384Combined sources5
Helixi387 – 389Combined sources3
Beta strandi403 – 410Combined sources8
Beta strandi416 – 423Combined sources8
Beta strandi425 – 429Combined sources5
Beta strandi433 – 442Combined sources10
Beta strandi448 – 465Combined sources18
Helixi467 – 471Combined sources5
Turni472 – 475Combined sources4
Beta strandi477 – 479Combined sources3
Helixi480 – 493Combined sources14
Helixi505 – 529Combined sources25
Turni541 – 543Combined sources3
Helixi544 – 547Combined sources4
Beta strandi556 – 560Combined sources5
Helixi583 – 587Combined sources5
Helixi594 – 596Combined sources3
Beta strandi604 – 610Combined sources7
Beta strandi612 – 622Combined sources11
Helixi626 – 628Combined sources3
Beta strandi632 – 637Combined sources6
Helixi638 – 640Combined sources3
Beta strandi645 – 648Combined sources4
Beta strandi653 – 656Combined sources4
Beta strandi659 – 661Combined sources3
Beta strandi667 – 675Combined sources9
Helixi676 – 684Combined sources9
Beta strandi687 – 692Combined sources6
Helixi699 – 705Combined sources7
Beta strandi708 – 718Combined sources11
Helixi720 – 726Combined sources7
Beta strandi728 – 737Combined sources10
Beta strandi749 – 754Combined sources6
Beta strandi761 – 765Combined sources5
Helixi770 – 781Combined sources12
Helixi785 – 787Combined sources3
Beta strandi788 – 793Combined sources6
Turni799 – 802Combined sources4
Helixi807 – 820Combined sources14
Beta strandi824 – 827Combined sources4
Helixi830 – 837Combined sources8
Beta strandi843 – 851Combined sources9
Beta strandi857 – 871Combined sources15
Helixi875 – 884Combined sources10
Beta strandi893 – 903Combined sources11
Turni913 – 916Combined sources4
Helixi917 – 935Combined sources19
Helixi939 – 945Combined sources7
Helixi965 – 976Combined sources12
Helixi978 – 991Combined sources14
Beta strandi993 – 1009Combined sources17
Helixi1013 – 1015Combined sources3
Beta strandi1017 – 1024Combined sources8
Beta strandi1030 – 1035Combined sources6
Beta strandi1039 – 1041Combined sources3
Helixi1043 – 1055Combined sources13
Helixi1059 – 1061Combined sources3
Turni1069 – 1071Combined sources3
Helixi1083 – 1108Combined sources26
Helixi1114 – 1123Combined sources10
Beta strandi1129 – 1135Combined sources7
Turni1143 – 1146Combined sources4
Beta strandi1152 – 1166Combined sources15
Turni1167 – 1169Combined sources3
Beta strandi1172 – 1182Combined sources11
Helixi1189 – 1208Combined sources20
Turni1225 – 1227Combined sources3
Helixi1233 – 1235Combined sources3
Beta strandi1238 – 1244Combined sources7
Helixi1254 – 1256Combined sources3
Helixi1263 – 1268Combined sources6
Helixi1269 – 1286Combined sources18
Helixi1303 – 1309Combined sources7
Helixi1315 – 1317Combined sources3

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...

Miscellaneous databases

EvolutionaryTraceiP47989.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 912Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST88
Domaini229 – 414FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST186

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

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiP47989.
KOiK00106.
OMAiLAQADHT.
OrthoDBiEOG091G01AW.
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

        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
Checksum:i806FF2C7413F84C5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 → K.1 PublicationCorresponds to variant rs45447191dbSNPEnsembl.1
Natural variantiVAR_045900149R → C in XAN1. 1 PublicationCorresponds to variant rs72549369dbSNPEnsembl.1
Natural variantiVAR_023977172G → R.2 PublicationsCorresponds to variant rs45523133dbSNPEnsembl.1
Natural variantiVAR_023978235T → M.1 PublicationCorresponds to variant rs45469499dbSNPEnsembl.1
Natural variantiVAR_023979395K → M.1 PublicationCorresponds to variant rs34929837dbSNPEnsembl.1
Natural variantiVAR_023980555P → S.1 PublicationCorresponds to variant rs45577338dbSNPEnsembl.1
Natural variantiVAR_023981584D → A.1 PublicationCorresponds to variant rs45491693dbSNPEnsembl.1
Natural variantiVAR_023982607R → Q.1 PublicationCorresponds to variant rs45442092dbSNPEnsembl.1
Natural variantiVAR_023983617K → N.1 PublicationCorresponds to variant rs45442398dbSNPEnsembl.1
Natural variantiVAR_023984623T → I.1 PublicationCorresponds to variant rs45448694dbSNPEnsembl.1
Natural variantiVAR_023985646I → V.1 PublicationCorresponds to variant rs17323225dbSNPEnsembl.1
Natural variantiVAR_023986703I → V.1 PublicationCorresponds to variant rs17011368dbSNPEnsembl.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 rs775646772dbSNPEnsembl.1
Natural variantiVAR_023987910T → M.1 PublicationCorresponds to variant rs669884dbSNPEnsembl.1
Natural variantiVAR_0239881091V → L.1 PublicationCorresponds to variant rs45619033dbSNPEnsembl.1
Natural variantiVAR_0239891109N → T.1 PublicationCorresponds to variant rs45547640dbSNPEnsembl.1
Natural variantiVAR_0459011150P → R.1 PublicationCorresponds to variant rs1042036dbSNPEnsembl.1
Natural variantiVAR_0239901176R → C.1 PublicationCorresponds to variant rs45624433dbSNPEnsembl.1
Natural variantiVAR_0239911296R → W.1 PublicationCorresponds to variant rs45564939dbSNPEnsembl.1

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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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.
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.
DB00997. Doxorubicin.
DB04854. Febuxostat.
DB03147. Flavin adenine dinucleotide.
DB00583. L-Carnitine.
DB00170. Menadione.
DB01033. Mercaptopurine.
DB00336. Nitrofural.
DB01168. Procarbazine.
DB00339. Pyrazinamide.
DB00127. Spermine.
DB00831. Trifluoperazine.
GuidetoPHARMACOLOGYi2646.

PTM databases

iPTMnetiP47989.
PhosphoSitePlusiP47989.

Polymorphism and mutation databases

BioMutaiXDH.
DMDMi2506326.

Proteomic databases

EPDiP47989.
MaxQBiP47989.
PaxDbiP47989.
PeptideAtlasiP47989.
PRIDEiP47989.

Protocols and materials databases

DNASUi7498.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7498.
DisGeNETi7498.
GeneCardsiXDH.
H-InvDBHIX0117690.
HGNCiHGNC:12805. XDH.
MalaCardsiXDH.
MIMi278300. phenotype.
607633. gene.
neXtProtiNX_P47989.
OpenTargetsiENSG00000158125.
Orphaneti93601. Xanthinuria type I.
PharmGKBiPA37404.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
GeneTreeiENSGT00390000003772.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
InParanoidiP47989.
KOiK00106.
OMAiLAQADHT.
OrthoDBiEOG091G01AW.
PhylomeDBiP47989.
TreeFamiTF353036.

Enzyme and pathway databases

BioCyciMetaCyc:HS08270-MONOMER.
ZFISH:HS08270-MONOMER.
BRENDAi1.17.1.4. 2681.
ReactomeiR-HSA-74259. Purine catabolism.
SABIO-RKP47989.

Miscellaneous databases

ChiTaRSiXDH. human.
EvolutionaryTraceiP47989.
GeneWikiiXanthine_dehydrogenase.
GenomeRNAii7498.
PROiP47989.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000158125.
CleanExiHS_XDH.
GenevisibleiP47989. HS.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 175 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.