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Protein Page:
DPYD (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
DPYD Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil. Homodimer. Found in most tissues with greatest activity found in liver and peripheral blood mononuclear cells. Belongs to the dihydropyrimidine dehydrogenase family. Note: This description may include information from UniProtKB.
Protein type: Other Amino Acids Metabolism - beta-alanine; EC 1.3.1.2; Oxidoreductase; Nucleotide Metabolism - pyrimidine; Xenobiotic Metabolism - drug metabolism - other enzymes; Cofactor and Vitamin Metabolism - pantothenate and CoA biosynthesis
Cellular Component: cytoplasm; cytosol
Molecular Function: protein homodimerization activity; FAD binding; dihydroorotate oxidase activity; 4 iron, 4 sulfur cluster binding; metal ion binding; dihydropyrimidine dehydrogenase (NADP+) activity; NADP binding
Biological Process: pyrimidine nucleoside catabolic process; pyrimidine base metabolic process; nucleobase, nucleoside and nucleotide metabolic process; uracil catabolic process; UMP biosynthetic process; thymine catabolic process; beta-alanine biosynthetic process; purine base catabolic process; thymidine catabolic process; pyrimidine base catabolic process
Reference #:  Q12882 (UniProtKB)
Alt. Names/Synonyms: DHP; DHPDHase; dihydropyrimidine dehydrogenase; Dihydropyrimidine dehydrogenase [NADP+]; Dihydrothymine dehydrogenase; Dihydrouracil dehydrogenase; DPD; DPYD; MGC132008; MGC70799
Gene Symbols: DPYD
Molecular weight: 111,401 Da
Basal Isoelectric point: 6.8  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DPYD

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K54 KNCFNCEKLENNFDD
0 1 K63 ENNFDDIKHTTLGER
0 1 K89 CADAPCQKSCPTNLD
0 1 K98 CPTNLDIKSFITSIA
0 1 K107 FITSIANKNYYGAAK
0 1 K254 LMKDLGVKIICGKsL
0 1 K259 GVKIICGKsLsVNEM
0 1 S260-p VKIICGKsLsVNEMT
0 1 S262-p IICGKsLsVNEMTLS
0 2 K272-u EMTLSTLkEKGYKAA
0 1 K307 DQGFYTSKDFLPLVA
0 1 K315 DFLPLVAKGSKAGMC
0 1 K318 PLVAKGSKAGMCACH
0 1 K381 PEEMELAKEEkCEFL
0 7 K384-a MELAKEEkCEFLPFL
0 1 K384 MELAKEEKCEFLPFL
0 1 R402 KVIVKGGRIVAMQFV
0 1 K446 GSVLSDPKVKEALSP
0 1 K448 VLSDPKVKEALSPIK
0 1 K455 KEALSPIKFNRWGLP
0 2 S577-p FALTKTFsLDKDIVT
0 1 K580 TKTFsLDKDIVTNVS
0 1 K709 VQIPFFAKLTPNVTD
0 1 K725 VSIARAAKEGGANGV
0 2 K875 IAELMDKKLPSFGPY
0 1 K894 KKIIAENKIRLKEQN
0 1 K898 AENKIRLKEQNVAFs
0 5 S905-p KEQNVAFsPLKRNCF
0 1 N910 AFsPLKRNCFIPKRP
0 1 R916 RNCFIPKRPIPTIKD
0 1 K922 KRPIPTIKDVIGKAL
0 2 T962 NCGKCYMTCNDSGYQ
0 1 N1022 RGVPLSVNPVC____
  mouse

 
K54-u KNCFTCEkLESNFDD
K63-u ESNFDDIkHTTLGER
K89-u CADAPCQkSCPTSLD
K98-u CPTSLDIkSFITSIA
K107-u FITSIANkNYYGAAK
K254-u LMKDLGVkIICGkSL
K259-u GVkIICGkSLSTDEM
S260 VkIICGkSLSTDEMT
S262 IICGkSLSTDEMTLS
K272-u EMTLSSLkENGYRAA
K307-u VQGFYTSkDFLPLVA
K315-u DFLPLVAkSSkTGMC
K318-u PLVAkSSkTGMCACH
K381-u PEEMELAkEEkCEFL
K384-a MELAkEEkCEFLPFL
K384-u MELAkEEkCEFLPFL
K402-u KVIVKDGkIVAMQFV
K446-u GSVLEDPkVkEALSP
K448-u VLEDPkVkEALSPIk
K455-u kEALSPIkFNRWGLP
S577 FALTKTFSLDkDIVT
K580-u TKTFSLDkDIVTNVS
K709-u VRVPFFAkLTPNVTD
K725-u VSIARAAkEGGADGV
K875-u VAELMGQkLPSFGPY
K894-u KKIIAASkIRQkDQN
K898-u AASkIRQkDQNTACs
S905-p kDQNTACsPLQRkHF
K910-u ACsPLQRkHFNSQkP
K916-u RkHFNSQkPIPAIkD
K922-u QkPIPAIkDVIGKSL
T962-p NCGKCYMtCNDSGYQ
K1022-u RGLPLAVkPVC____
  rat

 
K54 KNCFICEKLENNFDD
K63 ENNFDDIKHTTLGER
K89 CADAPCQKSCPTSLD
K98 CPTSLDIKSFITSIA
K107 FITSIANKNYYGAAK
K254 LMKDLGVKIICGKSI
K259 GVKIICGKSISTDEM
S260 VKIICGKSISTDEMT
S262 IICGKSISTDEMTLS
K272 EMTLSTLKENGYKAA
K307 VQGFYTSKDFLPLVA
K315 DFLPLVAKGSKPGMC
K318 PLVAKGSKPGMCACH
K381 PEEMELAKEEKCEFL
K384 MELAKEEKCEFLPFL
K384 MELAKEEKCEFLPFL
K402 KVIVKDGKIVGMQFV
K446 GSVLDDPKVIEALSP
I448 VLDDPKVIEALSPIK
K455 IEALSPIKFNRWGLP
S577 FALTKTFSLDKDIVT
K580 TKTFSLDKDIVTNVS
K709 VRVPFFAKLTPNVTD
K725 VSIARAAKEGGADGV
K875 IAELMGQKLPSFGPY
K894 KKILAASKIRENDQN
N898 AASKIRENDQNRACs
S905-p NDQNRACsPLQRKHF
K910 ACsPLQRKHFNSQKP
K916 RKHFNSQKPIPAIKD
K922 QKPIPAIKDVIGKSL
T962 NCGKCYMTCNDSGYQ
K1022 RGLPLAVKPVC____
  pig

 
K54 KNCFHCEKLENNFGD
K63 ENNFGDIKHTTLGER
K89 CADAPCQKSCPTHLD
K98 CPTHLDIKSFITSIS
K107 FITSISNKNYYGAAK
K254 LMKDLGVKIICGKSL
K259 GVKIICGKSLSENEI
S260 VKIICGKSLSENEIT
S262 IICGKSLSENEITLN
K272 EITLNTLKEEGYKAA
K307 DQGFYTSKDFLPLVA
K315 DFLPLVAKSSKAGMC
K318 PLVAKSSKAGMCACH
K381 PEEVELAKEEKCEFL
K384 VELAKEEKCEFLPFL
K384 VELAKEEKCEFLPFL
R402 KVIVKGGRIVAVQFV
K446 GSVLRDPKVKEALSP
K448 VLRDPKVKEALSPIK
K455 KEALSPIKFNRWDLP
S577 FALTKTFSLDKDIVT
K580 TKTFSLDKDIVTNVS
K709 VQIPFFAKLTPNVTD
K725 VSIARAAKEGGADGV
K875 IAELMGKKLPNFGPY
K894 KKIIAEEKMRLKEQN
K898 AEEKMRLKEQNAAFP
P905 KEQNAAFPPLERKPF
K910 AFPPLERKPFIPKKP
K916 RKPFIPKKPIPAIKD
K922 KKPIPAIKDVIGKAL
T962 NCGKCYMTCNDSGYQ
N1022 RGLPLAVNPVC____
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