XDH_HUMAN - dbPTM
XDH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XDH_HUMAN
UniProt AC P47989
Protein Name Xanthine dehydrogenase/oxidase
Gene Name XDH
Organism Homo sapiens (Human).
Sequence Length 1333
Subcellular Localization Cytoplasm. Peroxisome. Secreted.
Protein 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. Has also low oxidase activity towards aldehydes (in vitro)..
Protein Sequence MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDRLQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCCMNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQASTLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFGAACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISDLNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSAFKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKEELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLDPTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRYENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDKVTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDLKKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKMLGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGRHPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGRLCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKLEGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGALLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAASVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLGYSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAVGEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVTGVPENCKPWSVRV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
39PhosphorylationRKLGLSGTKLGCGEG
HHHCCCCCCCCCCCC		21.5122067460
188PhosphorylationMNQKKDHSVSLSPSL
CCCCCCCCCCCCHHH		24.4323090842
190PhosphorylationQKKDHSVSLSPSLFK
CCCCCCCCCCHHHCC		26.5823090842
192PhosphorylationKDHSVSLSPSLFKPE
CCCCCCCCHHHCCCH		12.6323090842
194PhosphorylationHSVSLSPSLFKPEEF
CCCCCCHHHCCCHHC		42.9624719451
202PhosphorylationLFKPEEFTPLDPTQE
HCCCHHCCCCCCCCC		26.6523090842
207PhosphorylationEFTPLDPTQEPIFPP
HCCCCCCCCCCCCCH		45.2723090842
222PhosphorylationELLRLKDTPRKQLRF
HHHCCCCCCCCCCEE		24.3320860994
311PhosphorylationPLSIVEKTLVDAVAK
CHHHHHHHHHHHHHC		20.64-
324PhosphorylationAKLPAQKTEVFRGVL
HCCCHHCHHHHHHHH		25.87-
356PhosphorylationGGNIITASPISDLNP
CCCEEEECCHHHCCC		17.7022210691
359PhosphorylationIITASPISDLNPVFM
EEEECCHHHCCCEEE		39.1522210691
368PhosphorylationLNPVFMASGAKLTLV
CCCEEEECCCEEEEE		27.7422210691
396PhosphorylationFFPGYRKTLLSPEEI
CCCCCCCCCCCHHHH		24.7528509920
399PhosphorylationGYRKTLLSPEEILLS
CCCCCCCCHHHHHEE		33.1228509920
406PhosphorylationSPEEILLSIEIPYSR
CHHHHHEEEECCCCC		18.0928509920
443MethylationSGMRVLFKPGTTEVQ
CCCEEEECCCCCHHH		38.07-
552AcetylationSATLLFQKDPPADVQ
HHEEEECCCCCCCCE		65.9419828313
605PhosphorylationPRYENELSLRLVTST
CCCCCCEEEEEHHHC		12.7924719451
804PhosphorylationGGFGGKETRSTVVST
CCCCCCHHHHHHHHH		33.1523532336
810PhosphorylationETRSTVVSTAVALAA
HHHHHHHHHHHHHHH		13.3024719451
818PhosphorylationTAVALAAYKTGRPVR
HHHHHHHHHHCCCEE		11.9522817900
856PhosphorylationVGFMKTGTVVALEVD
EECCCCCEEEEEEEE		19.62-
898PhosphorylationKIPNIRGTGRLCKTN
ECCCCCCCCCCCCCC		14.8522210691
1052PhosphorylationTKMVQVASRALKIPT
HHHHHHHHHHHCCCC		21.16-
1074N-linked_GlycosylationTSTNTVPNTSPTAAS
CCCCCCCCCCCCCEE		49.1818780401
1111PhosphorylationPYKKKNPSGSWEDWV
CCCCCCCCCCHHHHH		55.6525022875
1113PhosphorylationKKKNPSGSWEDWVTA
CCCCCCCCHHHHHHH		31.4625022875
1119PhosphorylationGSWEDWVTAAYMDTV
CCHHHHHHHHHCCCC		11.0025022875
1122PhosphorylationEDWVTAAYMDTVSLS
HHHHHHHHCCCCEEE		7.9625022875
1125PhosphorylationVTAAYMDTVSLSATG
HHHHHCCCCEEEECC		8.7525022875
1127PhosphorylationAAYMDTVSLSATGFY
HHHCCCCEEEECCCC		20.7825022875
1129PhosphorylationYMDTVSLSATGFYRT
HCCCCEEEECCCCCC		19.1125022875
1131PhosphorylationDTVSLSATGFYRTPN
CCCEEEECCCCCCCC		25.1725022875
1134PhosphorylationSLSATGFYRTPNLGY
EEEECCCCCCCCCEE		18.2125022875
1177PhosphorylationGDHKNLRTDIVMDVG
CCCCCCCCEEEEECC		32.9922210691
1185PhosphorylationDIVMDVGSSLNPAID
EEEEECCCCCCCCCC		31.3422210691
1186PhosphorylationIVMDVGSSLNPAIDI
EEEECCCCCCCCCCH		26.6622210691
1208PhosphorylationVQGLGLFTLEELHYS
ECEEEEEEEEEEEEC		38.0022210691
1299PhosphorylationKELFRLDSPATPEKI
HHHHCCCCCCCHHHH		22.4923403867
1320PhosphorylationKFTTLCVTGVPENCK
CCCEEEECCCCCCCC		31.3119413330
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
222TPhosphorylationKinaseCDK5Q00535
PSP
-KUbiquitinationE3 ubiquitin ligaseMIB2Q96AX9
PMID:15824097
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XDH_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of XDH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of XDH_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
278300Xanthinuria 1 (XU1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XDH_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry.";
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
Proteomics 8:3833-3847(2008).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1074, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222, AND MASSSPECTROMETRY.

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