CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010761
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Xanthine dehydrogenase/oxidase 
Protein Synonyms/Alias
 Xanthine dehydrogenase; XD; Xanthine oxidase; XO; Xanthine oxidoreductase; XOR 
Gene Name
 Xdh 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
16LVFFVNGKKVVEKNAubiquitination[1]
21NGKKVVEKNADPETTubiquitination[1]
342QLRWFAGKQVKSVASubiquitination[1]
373VLMASRAKLTLASRGubiquitination[1]
424GEFFSAFKQASRREDubiquitination[1]
470DRTVSALKTTPKQLSubiquitination[1]
540DLEGMCGKLDPTFASubiquitination[1]
568QLFQEVPKGQSEEDMubiquitination[1]
781KTQSFIAKMLGVPDNubiquitination[1]
893FHMDNAYKIPNIRGTubiquitination[1]
905RGTGRICKTNLPSNTubiquitination[1]
951VRRKNMYKEGDLTHFubiquitination[1]
961DLTHFNQKLEGFTLPubiquitination[1]
1231TRGPSTYKIPAFGSIubiquitination[1]
1294QHGDSNAKQLFQLDSubiquitination[1]
1307DSPATPEKIRNACVDubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 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 (By similarity). 
Sequence Annotation
 DOMAIN 7 94 2Fe-2S ferredoxin-type.
 DOMAIN 231 416 FAD-binding PCMH-type.
 NP_BIND 259 266 FAD (By similarity).
 NP_BIND 349 353 FAD (By similarity).
 ACT_SITE 1264 1264 Proton acceptor (By similarity).
 METAL 46 46 Iron-sulfur 1 (By similarity).
 METAL 51 51 Iron-sulfur 1 (By similarity).
 METAL 54 54 Iron-sulfur 1 (By similarity).
 METAL 76 76 Iron-sulfur 1 (By similarity).
 METAL 115 115 Iron-sulfur 2 (By similarity).
 METAL 118 118 Iron-sulfur 2 (By similarity).
 METAL 150 150 Iron-sulfur 2 (By similarity).
 METAL 152 152 Iron-sulfur 2 (By similarity).
 METAL 770 770 Molybdenum (By similarity).
 METAL 801 801 Molybdenum; via carbonyl oxygen (By
 METAL 915 915 Molybdenum; via amide nitrogen (By
 METAL 1082 1082 Molybdenum; via amide nitrogen (By
 BINDING 339 339 FAD (By similarity).
 BINDING 362 362 FAD (By similarity).
 BINDING 406 406 FAD; via amide nitrogen and carbonyl
 BINDING 424 424 FAD (By similarity).
 BINDING 805 805 Substrate (By similarity).
 BINDING 883 883 Substrate (By similarity).
 BINDING 917 917 Substrate (By similarity).
 BINDING 1013 1013 Substrate; via amide nitrogen (By
 CARBOHYD 1076 1076 N-linked (GlcNAc...) (Potential).
 DISULFID 538 995 In oxidase form (By similarity).  
Keyword
 2Fe-2S; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase; Peroxisome; Reference proteome; Secreted. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1335 AA 
Protein Sequence
MTRTTVDELV FFVNGKKVVE KNADPETTLL VYLRRKLGLC GTKLGCGEGG CGACTVMISK 60
YDRLQNKIVH FSVNACLTPI CSLHHVAVTT VEGIGNTKKL HPVQERIAKS HGSQCGFCTP 120
GIVMSMYTLL RNKPEPTVEE IENAFQGNLC RCTGYRPILQ GFRTFAKDGG CCGGSGNNPN 180
CCMSQTKDQT IAPSSSLFNP EDFKPLDPTQ EPIFPPELLR LKDTPRKTLR FEGERVTWIQ 240
VSTMEELLDL KAQHPDAKLV VGNTEIGIEM KFKNMLFPLI ICPAWILELT SVAHGPEGIS 300
FGAACPLSLV ESVLADAIAT LPEQRTEVFR GVMEQLRWFA GKQVKSVASI GGNIITASPI 360
SDLNPVLMAS RAKLTLASRG TKRTVWMDHT FFPGYRRTLL SPEEILVSIV IPYSRKGEFF 420
SAFKQASRRE DDIAKVTSGM RVLFKPGTTE VQELSLCFGG MADRTVSALK TTPKQLSKSW 480
NEELLQDVCA GLAEELHLAP DAPGGMVEFR RTLTLSFFFK FYLTVLQKLG RADLEGMCGK 540
LDPTFASATL LFQKDPPANV QLFQEVPKGQ SEEDMVGRPM PHLAADMQAS GEAVYCDDIP 600
RYENELSLRL VTSTRAHAKI MSIDTSEAKK VPGFVCFLTS EDVPGSNITG IFNDETVFAK 660
DEVTCVGHII GAVVADTPEH AHRAARGVKI TYEDLPAIIT IQDAIKNNSF YGPEVKIEKG 720
DLKKGFSEAD NVVSGELYIG GQEHFYLETH CTIAVPKGEA GEMELFVSTQ NTMKTQSFIA 780
KMLGVPDNRI VVRVKRMGGG FGGKETRSTL ISTAVALAAY KTGRPVRCML DRDEDMLITG 840
GRHPFLAKYK VGFMKTGTIV ALEVAHFSNG GNSEDLSRSI MERAVFHMDN AYKIPNIRGT 900
GRICKTNLPS NTAFRGFGGP QGMLIAEYWM SEVAVTCGLP AEEVRRKNMY KEGDLTHFNQ 960
KLEGFTLPRC WDECIASSQY QARKMEVEKF NRENCWKKRG LCIIPTKFGI SFTLSFLNQG 1020
GALVHVYTDG SVLLTHGGTE MGQGLHTKMV QVASRALKIP TSKIHITETS TNTVPNTSPT 1080
AASASADLNG QAIYEACQTI LKRLEPFKKK NPSGSWESWV MDAYTSAVSL SATGFYKTPN 1140
LGYSFETNSG NPFHYFSYGV ACSEVEIDCL TGDHKNLRTD IVMDVGSSLN PAIDIGQVEG 1200
AFVQGLGLFT MEELHYSPEG SLHTRGPSTY KIPAFGSIPI EFRVSLLRDC PNKRAIYASK 1260
AVGEPPLFLA SSIFFAIKDA IRAARAQHGD SNAKQLFQLD SPATPEKIRN ACVDQFTTLC 1320
ATGTPENCKS WSVRI 1335 
Gene Ontology
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
 GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0030151; F:molybdenum ion binding; IEA:InterPro.
 GO:0043546; F:molybdopterin cofactor binding; ISS:UniProtKB.
 GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
 GO:0004854; F:xanthine dehydrogenase activity; ISS:UniProtKB.
 GO:0004855; F:xanthine oxidase activity; ISS:UniProtKB.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
 GO:0007595; P:lactation; IMP:MGI.
 GO:0045602; P:negative regulation of endothelial cell differentiation; IEA:Compara.
 GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Compara.
 GO:0010629; P:negative regulation of gene expression; IEA:Compara.
 GO:0051898; P:negative regulation of protein kinase B signaling cascade; IEA:Compara.
 GO:0001933; P:negative regulation of protein phosphorylation; IEA:Compara.
 GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Compara.
 GO:2001213; P:negative regulation of vasculogenesis; IEA:Compara.
 GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Compara.
 GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Compara.
 GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
 GO:0009115; P:xanthine catabolic process; ISS:UniProtKB. 
Interpro
 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.
 IPR014309; Xanthine_DH_Mopterin-bd_su.
 IPR014307; Xanthine_DH_ssu. 
Pfam
 PF01315; Ald_Xan_dh_C
 PF02738; Ald_Xan_dh_C2
 PF03450; CO_deh_flav_C
 PF00941; FAD_binding_5
 PF00111; Fer2
 PF01799; Fer2_2 
SMART
 SM01008; Ald_Xan_dh_C
 SM01092; CO_deh_flav_C 
PROSITE
 PS00197; 2FE2S_FER_1
 PS51085; 2FE2S_FER_2
 PS51387; FAD_PCMH
 PS00559; MOLYBDOPTERIN_EUK 
PRINTS