DPYD_HUMAN - dbPTM
DPYD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPYD_HUMAN
UniProt AC Q12882
Protein Name Dihydropyrimidine dehydrogenase [NADP(+)]
Gene Name DPYD
Organism Homo sapiens (Human).
Sequence Length 1025
Subcellular Localization Cytoplasm.
Protein Description Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil..
Protein Sequence MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFDDIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPEKMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQDQGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWNEDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQNVAFSPLKRNCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLSVNPVC
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
31PhosphorylationTHATLCSTSAKKLDK
CCCEECCCCCHHHCH		31.54-
32PhosphorylationHATLCSTSAKKLDKK
CCEECCCCCHHHCHH		23.07-
35AcetylationLCSTSAKKLDKKHWK
ECCCCCHHHCHHHHH		62.737822267
38AcetylationTSAKKLDKKHWKRNP
CCCHHHCHHHHHHCC		57.907822277
39AcetylationSAKKLDKKHWKRNPD
CCHHHCHHHHHHCCC		55.137822287
52UbiquitinationPDKNCFNCEKLENNF
CCCCCCCHHHHHHCC		2.1521963094
63UbiquitinationENNFDDIKHTTLGER
HHCCHHHCCCCHHHH		41.7229967540
81UbiquitinationREAMRCLKCADAPCQ
HHHHHHHHHCCCCCC		30.88-
89UbiquitinationCADAPCQKSCPTNLD
HCCCCCCCCCCCCCC		61.8221963094
98UbiquitinationCPTNLDIKSFITSIA
CCCCCCHHHHHHHHH		38.69-
99PhosphorylationPTNLDIKSFITSIAN
CCCCCHHHHHHHHHC		23.40-
102PhosphorylationLDIKSFITSIANKNY
CCHHHHHHHHHCCCC		16.45-
103PhosphorylationDIKSFITSIANKNYY
CHHHHHHHHHCCCCC		18.19-
107UbiquitinationFITSIANKNYYGAAK
HHHHHHCCCCCCCCE		36.9929967540
175PhosphorylationIPQIRNPSLPPPEKM
CCCCCCCCCCCCHHH		57.9922210691
181UbiquitinationPSLPPPEKMSEAYSA
CCCCCCHHHCHHHHH		54.20-
183PhosphorylationLPPPEKMSEAYSAKI
CCCCHHHCHHHHHHH		30.0922985185
186PhosphorylationPEKMSEAYSAKIALF
CHHHCHHHHHHHHHH		12.7122210691
201PhosphorylationGAGPASISCASFLAR
CCCHHHHHHHHHHHH		10.9222210691
204PhosphorylationPASISCASFLARLGY
HHHHHHHHHHHHCCC		25.7224719451
222PhosphorylationTIFEKQEYVGGLSTS
EEEECEEECCCCCHH		11.2525072903
227PhosphorylationQEYVGGLSTSEIPQF
EEECCCCCHHCCCCC		32.9125072903
228PhosphorylationEYVGGLSTSEIPQFR
EECCCCCHHCCCCCC		35.1125072903
229PhosphorylationYVGGLSTSEIPQFRL
ECCCCCHHCCCCCCC		30.1025072903
259UbiquitinationGVKIICGKSLSVNEM
CCEEEECCCCCCCCC		43.76-
260PhosphorylationVKIICGKSLSVNEMT
CEEEECCCCCCCCCC		15.9119664995
260O-linked_GlycosylationVKIICGKSLSVNEMT
CEEEECCCCCCCCCC		15.9130379171
262PhosphorylationIICGKSLSVNEMTLS
EEECCCCCCCCCCHH		29.9519664995
269PhosphorylationSVNEMTLSTLKEKGY
CCCCCCHHHHHHCCC		23.6425627689
270PhosphorylationVNEMTLSTLKEKGYK
CCCCCHHHHHHCCCC		44.9928509920
272UbiquitinationEMTLSTLKEKGYKAA
CCCHHHHHHCCCCEE		58.4229967540
274UbiquitinationTLSTLKEKGYKAAFI
CHHHHHHCCCCEEEE		66.99-
307UbiquitinationDQGFYTSKDFLPLVA
CCCCCCCHHHHHHEE		44.7029967540
315AcetylationDFLPLVAKGSKAGMC
HHHHHEECCCCCEEE		57.1225953088
315UbiquitinationDFLPLVAKGSKAGMC
HHHHHEECCCCCEEE		57.1229967540
318UbiquitinationPLVAKGSKAGMCACH
HHEECCCCCEEEECC		58.59-
326PhosphorylationAGMCACHSPLPSIRG
CEEEECCCCCCCCCE		28.1927251275
330PhosphorylationACHSPLPSIRGVVIV
ECCCCCCCCCEEEEE		32.3824719451
365UbiquitinationRVFIVFRKGFVNIRA
EEEEEEECCCCCEEE		45.28-
377SulfoxidationIRAVPEEMELAKEEK
EEECCHHHHHHHHHC		4.9530846556
381AcetylationPEEMELAKEEKCEFL
CHHHHHHHHHCCCCC		78.1423749302
381UbiquitinationPEEMELAKEEKCEFL
CHHHHHHHHHCCCCC		78.14-
384UbiquitinationMELAKEEKCEFLPFL
HHHHHHHCCCCCCCC		39.9119608861
384AcetylationMELAKEEKCEFLPFL
HHHHHHHCCCCCCCC		39.9119608861
392PhosphorylationCEFLPFLSPRKVIVK
CCCCCCCCCCEEEEE		24.0424719451
418UbiquitinationTEQDETGKWNEDEDQ
CCCCCCCCCCCCHHH		55.0229967540
436PhosphorylationLKADVVISAFGSVLS
HHHCCHHHCCCHHHC		13.11-
440PhosphorylationVVISAFGSVLSDPKV
CHHHCCCHHHCCHHH		17.27-
448UbiquitinationVLSDPKVKEALSPIK
HHCCHHHHHHCCCCC		43.3129967540
452PhosphorylationPKVKEALSPIKFNRW
HHHHHHCCCCCCCCC		31.4628102081
455UbiquitinationKEALSPIKFNRWGLP
HHHCCCCCCCCCCCC		39.71-
544UbiquitinationMAGLKFINPFGLASA
HCCCEEECCCCCCCC		29.0421987572
573PhosphorylationAGWGFALTKTFSLDK
CCCCEEEEEEEECCC		25.30-
575PhosphorylationWGFALTKTFSLDKDI
CCEEEEEEEECCCCH		17.1429449344
577PhosphorylationFALTKTFSLDKDIVT
EEEEEEEECCCCHHC		40.6722817900
580UbiquitinationTKTFSLDKDIVTNVS
EEEEECCCCHHCCCC		55.43-
584PhosphorylationSLDKDIVTNVSPRII
ECCCCHHCCCCCCEE		30.1823403867
587PhosphorylationKDIVTNVSPRIIRGT
CCHHCCCCCCEEECC		15.5529255136
614PhosphorylationFLNIELISEKTAAYW
CEEEEECCHHHHHHH		45.7424719451
624PhosphorylationTAAYWCQSVTELKAD
HHHHHHHCHHHHHCC		28.0626437602
637UbiquitinationADFPDNIVIASIMCS
CCCCCCEEEEEEEEE		3.6121987572
655UbiquitinationNDWTELAKKSEDSGA
CCHHHHHHHCCCCCC		70.2529967540
656UbiquitinationDWTELAKKSEDSGAD
CHHHHHHHCCCCCCC		54.17-
672UbiquitinationLELNLSCPHGMGERG
EEECCCCCCCCCCCC		24.5621987572
709UbiquitinationVQIPFFAKLTPNVTD
HHCCHHHCCCCCHHH		47.9721987572
725UbiquitinationVSIARAAKEGGANGV
HHHHHHHHHCCCCCE		56.77-
743UbiquitinationNTVSGLMGLKSDGTP
CCHHHHCCCCCCCCC		34.6922505724
758UbiquitinationWPAVGIAKRTTYGGV
CCCEEEEEECCCCCC		48.64-
762PhosphorylationGIAKRTTYGGVSGTA
EEEEECCCCCCCCCC		15.9825839225
766PhosphorylationRTTYGGVSGTAIRPI
ECCCCCCCCCCHHHH		33.43-
768PhosphorylationTYGGVSGTAIRPIAL
CCCCCCCCCHHHHHH		16.05-
780PhosphorylationIALRAVTSIARALPG
HHHHHHHHHHHHCCC		13.9823312004
836UbiquitinationDYCTGLKALLYLKSI
HHHHHHHHHHHHHCH		14.0822505724
841UbiquitinationLKALLYLKSIEELQD
HHHHHHHHCHHHHHC		35.51-
871UbiquitinationPVPRIAELMDKKLPS
CCCCHHHHHHCCCCC		3.8822505724
874UbiquitinationRIAELMDKKLPSFGP
CHHHHHHCCCCCCHH		42.09-
875UbiquitinationIAELMDKKLPSFGPY
HHHHHHCCCCCCHHH		62.4629967540
888UbiquitinationPYLEQRKKIIAENKI
HHHHHHHHHHHHCCH		41.3529967540
894UbiquitinationKKIIAENKIRLKEQN
HHHHHHCCHHHHHCC		22.2529967540
898MethylationAENKIRLKEQNVAFS
HHCCHHHHHCCCCCC		47.61-
898UbiquitinationAENKIRLKEQNVAFS
HHCCHHHHHCCCCCC		47.61-
905PhosphorylationKEQNVAFSPLKRNCF
HHCCCCCCCCCCCCC		21.4225159151
908UbiquitinationNVAFSPLKRNCFIPK
CCCCCCCCCCCCCCC		44.9722505724
908MethylationNVAFSPLKRNCFIPK
CCCCCCCCCCCCCCC		44.97-
915UbiquitinationKRNCFIPKRPIPTIK
CCCCCCCCCCCCCHH		67.02-
922UbiquitinationKRPIPTIKDVIGKAL
CCCCCCHHHHHHHHH		48.71-
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

Oops, there are no upstream regulatory protein records of DPYD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPYD_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 DPYD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOPC_HUMANGOPCphysical
24722188
LXN_HUMANLXNphysical
25416956
GOPC_HUMANGOPCphysical
25416956
RPE_HUMANRPEphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
274270Dihydropyrimidine dehydrogenase deficiency (DPYDD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01101Capecitabine
DB03147Flavin adenine dinucleotide
DB00544Fluorouracil
Regulatory Network of DPYD_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577, AND MASSSPECTROMETRY.

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