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P47989

- XDH_HUMAN

UniProt

P47989 - XDH_HUMAN

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Protein

Xanthine dehydrogenase/oxidase

Gene

XDH

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.
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
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-KW
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.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

BgeeiP47989.
CleanExiHS_XDH.
ExpressionAtlasiP47989. baseline and differential.
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 – 105Combined sources
Beta strandi13 – 175Combined sources
Helixi26 – 327Combined sources
Beta strandi44 – 485Combined sources
Beta strandi52 – 598Combined sources
Turni60 – 634Combined sources
Beta strandi64 – 718Combined sources
Turni72 – 743Combined sources
Helixi77 – 793Combined sources
Beta strandi84 – 863Combined sources
Helixi88 – 903Combined sources
Helixi100 – 1078Combined sources
Helixi117 – 13014Combined sources
Helixi136 – 1416Combined sources
Turni142 – 1454Combined sources
Beta strandi149 – 1513Combined sources
Helixi154 – 1607Combined sources
Helixi161 – 1633Combined sources
Helixi198 – 2003Combined sources
Helixi206 – 2083Combined sources
Helixi214 – 2185Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi235 – 2384Combined sources
Helixi242 – 25110Combined sources
Helixi264 – 2707Combined sources
Beta strandi276 – 2805Combined sources
Helixi285 – 2884Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi294 – 3007Combined sources
Helixi305 – 31814Combined sources
Helixi321 – 3233Combined sources
Helixi325 – 33511Combined sources
Helixi340 – 3456Combined sources
Helixi348 – 3547Combined sources
Helixi362 – 3676Combined sources
Beta strandi371 – 3755Combined sources
Beta strandi380 – 3845Combined sources
Helixi387 – 3893Combined sources
Beta strandi403 – 4108Combined sources
Beta strandi416 – 4238Combined sources
Beta strandi425 – 4295Combined sources
Beta strandi433 – 44210Combined sources
Beta strandi448 – 46518Combined sources
Helixi467 – 4715Combined sources
Turni472 – 4754Combined sources
Beta strandi477 – 4793Combined sources
Helixi480 – 49314Combined sources
Helixi505 – 52925Combined sources
Turni541 – 5433Combined sources
Helixi544 – 5474Combined sources
Beta strandi556 – 5605Combined sources
Helixi583 – 5875Combined sources
Helixi594 – 5963Combined sources
Beta strandi604 – 6107Combined sources
Beta strandi612 – 62211Combined sources
Helixi626 – 6283Combined sources
Beta strandi632 – 6376Combined sources
Helixi638 – 6403Combined sources
Beta strandi645 – 6484Combined sources
Beta strandi653 – 6564Combined sources
Beta strandi659 – 6613Combined sources
Beta strandi667 – 6759Combined sources
Helixi676 – 6849Combined sources
Beta strandi687 – 6926Combined sources
Helixi699 – 7057Combined sources
Beta strandi708 – 71811Combined sources
Helixi720 – 7267Combined sources
Beta strandi728 – 73710Combined sources
Beta strandi749 – 7546Combined sources
Beta strandi761 – 7655Combined sources
Helixi770 – 78112Combined sources
Helixi785 – 7873Combined sources
Beta strandi788 – 7936Combined sources
Turni799 – 8024Combined sources
Helixi807 – 82014Combined sources
Beta strandi824 – 8274Combined sources
Helixi830 – 8378Combined sources
Beta strandi843 – 8519Combined sources
Beta strandi857 – 87115Combined sources
Helixi875 – 88410Combined sources
Beta strandi893 – 90311Combined sources
Turni913 – 9164Combined sources
Helixi917 – 93519Combined sources
Helixi939 – 9457Combined sources
Helixi965 – 97612Combined sources
Helixi978 – 99114Combined sources
Beta strandi993 – 100917Combined sources
Helixi1013 – 10153Combined sources
Beta strandi1017 – 10248Combined sources
Beta strandi1030 – 10356Combined sources
Beta strandi1039 – 10413Combined sources
Helixi1043 – 105513Combined sources
Helixi1059 – 10613Combined sources
Turni1069 – 10713Combined sources
Helixi1083 – 110826Combined sources
Helixi1114 – 112310Combined sources
Beta strandi1129 – 11357Combined sources
Turni1143 – 11464Combined sources
Beta strandi1152 – 116615Combined sources
Turni1167 – 11693Combined sources
Beta strandi1172 – 118211Combined sources
Helixi1189 – 120820Combined sources
Turni1225 – 12273Combined sources
Helixi1233 – 12353Combined sources
Beta strandi1238 – 12447Combined sources
Helixi1254 – 12563Combined sources
Helixi1263 – 12686Combined sources
Helixi1269 – 128618Combined sources
Helixi1303 – 13097Combined sources
Helixi1315 – 13173Combined sources

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.
GeneTreeiENSGT00390000003772.
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

        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)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 DB00041. Aldesleukin.
DB00437. Allopurinol.
DB00993. Azathioprine.
DB00958. Carboplatin.
DB01136. Carvedilol.
DB00856. Chlorphenesin.
DB00515. Cisplatin.
DB00694. Daunorubicin.
DB00746. Deferoxamine.
DB00997. Doxorubicin.
DB03147. Flavin adenine dinucleotide.
DB00583. L-Carnitine.
DB00170. Menadione.
DB01033. Mercaptopurine.
DB00336. Nitrofural.
DB01168. Procarbazine.
DB00339. Pyrazinamide.
DB00127. Spermine.
DB00831. Trifluoperazine.
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.
GeneTreei ENSGT00390000003772.
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

Bgeei P47989.
CleanExi HS_XDH.
ExpressionAtlasi P47989. baseline and differential.
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: October 29, 2014
This is version 153 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

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