Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydropyrimidine dehydrogenase [NADP(+)]

Gene

DPYD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil.

Catalytic activityi

5,6-dihydrouracil + NADP+ = uracil + NADPH.

Cofactori

Protein has several cofactor binding sites:
  • FADNote: Binds 2 FAD.
  • FMNNote: Binds 2 FMN.
  • [4Fe-4S] clusterBy similarityNote: Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron atoms per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi82 – 821Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi87 – 871Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi91 – 911Iron-sulfur 2 (4Fe-4S)By similarity
Binding sitei129 – 1291FAD; via carbonyl oxygenBy similarity
Metal bindingi130 – 1301Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi136 – 1361Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi140 – 1401Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi156 – 1561Iron-sulfur 2 (4Fe-4S)By similarity
Binding sitei235 – 2351FADBy similarity
Binding sitei261 – 2611FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei371 – 3711NADPBy similarity
Binding sitei550 – 5501FMNBy similarity
Binding sitei609 – 6091SubstrateBy similarity
Active sitei671 – 6711Proton acceptorBy similarity
Binding sitei709 – 7091FMNBy similarity
Binding sitei767 – 7671FMN; via amide nitrogenBy similarity
Metal bindingi953 – 9531Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi956 – 9561Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi959 – 9591Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi963 – 9631Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi986 – 9861Iron-sulfur 4 (4Fe-4S)By similarity
Metal bindingi989 – 9891Iron-sulfur 4 (4Fe-4S)By similarity
Metal bindingi992 – 9921Iron-sulfur 4 (4Fe-4S)By similarity
Metal bindingi996 – 9961Iron-sulfur 4 (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi194 – 1985FADBy similarity
Nucleotide bindingi218 – 2269FADBy similarity
Nucleotide bindingi340 – 3434NADPBy similarity
Nucleotide bindingi364 – 3652NADPBy similarity
Nucleotide bindingi437 – 4393NADPBy similarity
Nucleotide bindingi480 – 48910FADBy similarity
Nucleotide bindingi481 – 4877NADPBy similarity
Nucleotide bindingi574 – 5752FMNBy similarity
Nucleotide bindingi793 – 7953FMNBy similarity
Nucleotide bindingi816 – 8172FMNBy similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. dihydroorotate dehydrogenase activity Source: InterPro
  3. dihydropyrimidine dehydrogenase (NADP+) activity Source: UniProtKB
  4. flavin adenine dinucleotide binding Source: UniProtKB
  5. metal ion binding Source: UniProtKB-KW
  6. NADP binding Source: UniProtKB
  7. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. beta-alanine biosynthetic process Source: UniProtKB-UniPathway
  2. nucleobase-containing small molecule metabolic process Source: Reactome
  3. purine nucleobase catabolic process Source: UniProtKB
  4. pyrimidine nucleobase catabolic process Source: UniProtKB
  5. pyrimidine nucleobase metabolic process Source: Reactome
  6. pyrimidine nucleoside catabolic process Source: Reactome
  7. small molecule metabolic process Source: Reactome
  8. thymidine catabolic process Source: UniProtKB
  9. thymine catabolic process Source: UniProtKB
  10. UMP biosynthetic process Source: InterPro
  11. uracil catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1023. Pyrimidine catabolism.
UniPathwayiUPA00131.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropyrimidine dehydrogenase [NADP(+)] (EC:1.3.1.2)
Short name:
DHPDHase
Short name:
DPD
Alternative name(s):
Dihydrothymine dehydrogenase
Dihydrouracil dehydrogenase
Gene namesi
Name:DPYD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3012. DPYD.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Dihydropyrimidine dehydrogenase deficiency4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA metabolic disorder with large phenotypic variability, ranging from no symptoms to a convulsive disorder with motor and mental retardation. It is characterized by persistent urinary excretion of excessive amounts of uracil, thymine and 5-hydroxymethyluracil. Patients suffering from this disease show a severe reaction to the anticancer drug 5-fluorouracil.

See also OMIM:274270
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291C → R in DPYDD; allele DPYD*9A and allele DPYD*9B; loss of activity. 5 Publications
Corresponds to variant rs1801265 [ dbSNP | Ensembl ].
VAR_005173
Natural varianti235 – 2351R → W in DPYDD; allele DPYD*8; loss of activity. 2 Publications
Corresponds to variant rs1801266 [ dbSNP | Ensembl ].
VAR_005174
Natural varianti886 – 8861R → H in DPYDD; allele DPYD*9B; 25% of activity. 2 Publications
Corresponds to variant rs1801267 [ dbSNP | Ensembl ].
VAR_005177

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi274270. phenotype.
Orphaneti293948. 1p21.3 microdeletion syndrome.
240839. 5-fluorouracil toxicity.
240855. Capecitabine toxicity.
1675. Dihydropyrimidine dehydrogenase deficiency.
240955. Susceptibility to adverse reaction due to 5-fluorouracil treatment.
240963. Susceptibility to adverse reaction due to capecitabine treatment.
PharmGKBiPA145.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 33PRO_0000021114
Chaini4 – 10251022Dihydropyrimidine dehydrogenase [NADP(+)]PRO_0000021115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei384 – 3841N6-acetyllysine1 Publication
Modified residuei905 – 9051PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ12882.
PaxDbiQ12882.
PRIDEiQ12882.

PTM databases

PhosphoSiteiQ12882.

Expressioni

Tissue specificityi

Found in most tissues with greatest activity found in liver and peripheral blood mononuclear cells.

Gene expression databases

BgeeiQ12882.
CleanExiHS_DPYD.
GenevestigatoriQ12882.

Organism-specific databases

HPAiCAB033241.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi108140. 4 interactions.
IntActiQ12882. 18 interactions.
STRINGi9606.ENSP00000359211.

Structurei

3D structure databases

ProteinModelPortaliQ12882.
SMRiQ12882. Positions 2-1019.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 100324Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini944 – 976334Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini978 – 1007304Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni668 – 6703Substrate bindingBy similarity
Regioni736 – 7372Substrate bindingBy similarity

Sequence similaritiesi

Contains 3 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0167.
GeneTreeiENSGT00500000044896.
HOVERGENiHBG004351.
InParanoidiQ12882.
KOiK00207.
OrthoDBiEOG7MH0X9.
PhylomeDBiQ12882.
TreeFamiTF105791.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR012135. Dihydroorotate_DH_1_2.
IPR028261. DPD_II.
IPR009051. Helical_ferredxn.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
PF14691. Fer4_20. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
TIGRFAMsiTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q12882-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPVLSKDSA DIESILALNP RTQTHATLCS TSAKKLDKKH WKRNPDKNCF
60 70 80 90 100
NCEKLENNFD DIKHTTLGER GALREAMRCL KCADAPCQKS CPTNLDIKSF
110 120 130 140 150
ITSIANKNYY GAAKMIFSDN PLGLTCGMVC PTSDLCVGGC NLYATEEGPI
160 170 180 190 200
NIGGLQQFAT EVFKAMSIPQ IRNPSLPPPE KMSEAYSAKI ALFGAGPASI
210 220 230 240 250
SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV VNFEIELMKD
260 270 280 290 300
LGVKIICGKS LSVNEMTLST LKEKGYKAAF IGIGLPEPNK DAIFQGLTQD
310 320 330 340 350
QGFYTSKDFL PLVAKGSKAG MCACHSPLPS IRGVVIVLGA GDTAFDCATS
360 370 380 390 400
ALRCGARRVF IVFRKGFVNI RAVPEEMELA KEEKCEFLPF LSPRKVIVKG
410 420 430 440 450
GRIVAMQFVR TEQDETGKWN EDEDQMVHLK ADVVISAFGS VLSDPKVKEA
460 470 480 490 500
LSPIKFNRWG LPEVDPETMQ TSEAWVFAGG DVVGLANTTV ESVNDGKQAS
510 520 530 540 550
WYIHKYVQSQ YGASVSAKPE LPLFYTPIDL VDISVEMAGL KFINPFGLAS
560 570 580 590 600
ATPATSTSMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI IRGTTSGPMY
610 620 630 640 650
GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNKNDW
660 670 680 690 700
TELAKKSEDS GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ
710 720 730 740 750
AVQIPFFAKL TPNVTDIVSI ARAAKEGGAN GVTATNTVSG LMGLKSDGTP
760 770 780 790 800
WPAVGIAKRT TYGGVSGTAI RPIALRAVTS IARALPGFPI LATGGIDSAE
810 820 830 840 850
SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL KSIEELQDWD
860 870 880 890 900
GQSPATVSHQ KGKPVPRIAE LMDKKLPSFG PYLEQRKKII AENKIRLKEQ
910 920 930 940 950
NVAFSPLKRN CFIPKRPIPT IKDVIGKALQ YLGTFGELSN VEQVVAMIDE
960 970 980 990 1000
EMCINCGKCY MTCNDSGYQA IQFDPETHLP TITDTCTGCT LCLSVCPIVD
1010 1020
CIKMVSRTTP YEPKRGVPLS VNPVC
Length:1,025
Mass (Da):111,401
Last modified:November 13, 2007 - v2
Checksum:i0201943955AB2C21
GO
Isoform 2 (identifier: Q12882-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-173: VFKAMSIPQIRN → TLILAFSLMNHL
     174-1025: Missing.

Note: No experimental confirmation available.

Show »
Length:173
Mass (Da):18,936
Checksum:i94D241E912F29B6B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311P → S in AAI08743. (PubMed:16710414)Curated
Sequence conflicti845 – 8451E → G in BAF83906. (PubMed:14702039)Curated
Sequence conflicti910 – 9101N → S in AAA57474. (PubMed:8083224)Curated
Sequence conflicti1024 – 10241V → G in AAI31779. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291C → R in DPYDD; allele DPYD*9A and allele DPYD*9B; loss of activity. 5 Publications
Corresponds to variant rs1801265 [ dbSNP | Ensembl ].
VAR_005173
Natural varianti166 – 1661M → V.
Corresponds to variant rs2297595 [ dbSNP | Ensembl ].
VAR_054034
Natural varianti235 – 2351R → W in DPYDD; allele DPYD*8; loss of activity. 2 Publications
Corresponds to variant rs1801266 [ dbSNP | Ensembl ].
VAR_005174
Natural varianti534 – 5341S → N in allele DPYD*4; low activity.
Corresponds to variant rs1801158 [ dbSNP | Ensembl ].
VAR_005175
Natural varianti543 – 5431I → V in allele DPYD*5. 1 Publication
Corresponds to variant rs1801159 [ dbSNP | Ensembl ].
VAR_005176
Natural varianti732 – 7321V → I.1 Publication
Corresponds to variant rs1801160 [ dbSNP | Ensembl ].
VAR_014760
Natural varianti886 – 8861R → H in DPYDD; allele DPYD*9B; 25% of activity. 2 Publications
Corresponds to variant rs1801267 [ dbSNP | Ensembl ].
VAR_005177
Natural varianti995 – 9951V → F in allele DPYD*10; low activity.
Corresponds to variant rs1801268 [ dbSNP | Ensembl ].
VAR_005178

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei162 – 17312VFKAM…PQIRN → TLILAFSLMNHL in isoform 2. 2 PublicationsVSP_044929Add
BLAST
Alternative sequencei174 – 1025852Missing in isoform 2. 2 PublicationsVSP_044930Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09178 mRNA. Translation: AAA57474.1.
U20938 mRNA. Translation: AAB51366.1.
AB003063 mRNA. Translation: BAA89789.1.
BT006740 mRNA. Translation: AAP35386.1.
AK291217 mRNA. Translation: BAF83906.1.
AL356457
, AC091608, AC093576, AC099787, AC114878, AC138135, BX908805 Genomic DNA. Translation: CAH70570.1.
BX908805
, AC091608, AC093576, AC099787, AC114878, AC138135, AL356457 Genomic DNA. Translation: CAI15125.1.
CH471097 Genomic DNA. Translation: EAW73002.1.
BC008379 mRNA. Translation: AAH08379.1.
BC064027 mRNA. Translation: AAH64027.1.
BC108742 mRNA. Translation: AAI08743.1.
BC131777 mRNA. Translation: AAI31778.1.
BC131778 mRNA. Translation: AAI31779.1.
X95670 Genomic DNA. Translation: CAA64973.1.
U57655 Genomic DNA. Translation: AAB07049.1.
CCDSiCCDS30777.1. [Q12882-1]
CCDS53346.1. [Q12882-2]
PIRiA54718.
RefSeqiNP_000101.2. NM_000110.3. [Q12882-1]
NP_001153773.1. NM_001160301.1. [Q12882-2]
UniGeneiHs.335034.

Genome annotation databases

EnsembliENST00000306031; ENSP00000307107; ENSG00000188641. [Q12882-2]
ENST00000370192; ENSP00000359211; ENSG00000188641. [Q12882-1]
GeneIDi1806.
KEGGihsa:1806.
UCSCiuc001drv.3. human. [Q12882-1]
uc001drw.3. human.

Polymorphism databases

DMDMi160332325.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09178 mRNA. Translation: AAA57474.1.
U20938 mRNA. Translation: AAB51366.1.
AB003063 mRNA. Translation: BAA89789.1.
BT006740 mRNA. Translation: AAP35386.1.
AK291217 mRNA. Translation: BAF83906.1.
AL356457
, AC091608, AC093576, AC099787, AC114878, AC138135, BX908805 Genomic DNA. Translation: CAH70570.1.
BX908805
, AC091608, AC093576, AC099787, AC114878, AC138135, AL356457 Genomic DNA. Translation: CAI15125.1.
CH471097 Genomic DNA. Translation: EAW73002.1.
BC008379 mRNA. Translation: AAH08379.1.
BC064027 mRNA. Translation: AAH64027.1.
BC108742 mRNA. Translation: AAI08743.1.
BC131777 mRNA. Translation: AAI31778.1.
BC131778 mRNA. Translation: AAI31779.1.
X95670 Genomic DNA. Translation: CAA64973.1.
U57655 Genomic DNA. Translation: AAB07049.1.
CCDSiCCDS30777.1. [Q12882-1]
CCDS53346.1. [Q12882-2]
PIRiA54718.
RefSeqiNP_000101.2. NM_000110.3. [Q12882-1]
NP_001153773.1. NM_001160301.1. [Q12882-2]
UniGeneiHs.335034.

3D structure databases

ProteinModelPortaliQ12882.
SMRiQ12882. Positions 2-1019.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108140. 4 interactions.
IntActiQ12882. 18 interactions.
STRINGi9606.ENSP00000359211.

Chemistry

BindingDBiQ12882.
ChEMBLiCHEMBL3172.
DrugBankiDB01101. Capecitabine.
DB03147. Flavin adenine dinucleotide.
DB00544. Fluorouracil.

PTM databases

PhosphoSiteiQ12882.

Polymorphism databases

DMDMi160332325.

Proteomic databases

MaxQBiQ12882.
PaxDbiQ12882.
PRIDEiQ12882.

Protocols and materials databases

DNASUi1806.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306031; ENSP00000307107; ENSG00000188641. [Q12882-2]
ENST00000370192; ENSP00000359211; ENSG00000188641. [Q12882-1]
GeneIDi1806.
KEGGihsa:1806.
UCSCiuc001drv.3. human. [Q12882-1]
uc001drw.3. human.

Organism-specific databases

CTDi1806.
GeneCardsiGC01M097543.
H-InvDBHIX0000804.
HGNCiHGNC:3012. DPYD.
HPAiCAB033241.
MIMi274270. phenotype.
612779. gene.
neXtProtiNX_Q12882.
Orphaneti293948. 1p21.3 microdeletion syndrome.
240839. 5-fluorouracil toxicity.
240855. Capecitabine toxicity.
1675. Dihydropyrimidine dehydrogenase deficiency.
240955. Susceptibility to adverse reaction due to 5-fluorouracil treatment.
240963. Susceptibility to adverse reaction due to capecitabine treatment.
PharmGKBiPA145.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0167.
GeneTreeiENSGT00500000044896.
HOVERGENiHBG004351.
InParanoidiQ12882.
KOiK00207.
OrthoDBiEOG7MH0X9.
PhylomeDBiQ12882.
TreeFamiTF105791.

Enzyme and pathway databases

UniPathwayiUPA00131.
ReactomeiREACT_1023. Pyrimidine catabolism.

Miscellaneous databases

ChiTaRSiDPYD. human.
GeneWikiiDPYD.
GenomeRNAii1806.
NextBioi35501869.
PROiQ12882.
SOURCEiSearch...

Gene expression databases

BgeeiQ12882.
CleanExiHS_DPYD.
GenevestigatoriQ12882.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR012135. Dihydroorotate_DH_1_2.
IPR028261. DPD_II.
IPR009051. Helical_ferredxn.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
PF14691. Fer4_20. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
TIGRFAMsiTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria."
    Yokota H., Fernandez-Salguero P., Furuya H., Lin K., McBride O.W., Podschun B., Schnackerz K.D., Gonzalez F.J.
    J. Biol. Chem. 269:23192-23196(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Structural organization of the human dihydropyrimidine dehydrogenase gene."
    Johnson M.R., Wang K., Tillmanns S., Albin N., Diasio R.B.
    Cancer Res. 57:1660-1663(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Suicidal inactivation of human dihydropyrimidine dehydrogenase by (E)-5-(2-bromovinyl)uracil derived from the antiviral, sorivudine."
    Ogura K., Nishiyama T., Takubo H., Kato A., Okuda H., Arakawa K., Fukushima M., Nagayama S., Kawaguchi Y., Watabe T.
    Cancer Lett. 122:107-113(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT DPYDD ARG-29.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT DPYDD ARG-29.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS VAL-543 AND ILE-732.
    Tissue: Skin and Uterus.
  9. "A point mutation in an invariant splice donor site leads to exon skipping in two unrelated Dutch patients with dihydropyrimidine dehydrogenase deficiency."
    Vreken P., van Kuilenburg A.B.P., Meinsma R., Smit G.P.A., Bakker H.D., de Abreu R.A., van Gennip A.H.
    J. Inherit. Metab. Dis. 19:645-654(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 581-635.
    Tissue: Liver.
  10. "Lack of correlation between phenotype and genotype for the polymorphically expressed dihydropyrimidine dehydrogenase in a family of Pakistani origin."
    Fernandez-Salguero P.M., Sapone A., Wei X., Holt J.R., Jones S., Idle J.R., Gonzalez F.J.
    Pharmacogenetics 7:161-163(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 581-635.
  11. "Purification and characterization of dihydropyrimidine dehydrogenase from human liver."
    Lu Z.-H., Zhang R., Diasio R.B.
    J. Biol. Chem. 267:17102-17109(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Dihydropyrimidine dehydrogenase (DPD) deficiency: identification and expression of missense mutations C29R, R886H and R235W."
    Vreken P., van Kuilenburg A.B.P., Meinsma R., van Gennip A.H.
    Hum. Genet. 101:333-338(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DPYDD ARG-29; TRP-235 AND HIS-886.
  15. "Identification of novel point mutations in the dihydropyrimidine dehydrogenase gene."
    Vreken P., van Kuilenburg A.B.P., Meinsma R., van Gennip A.H.
    J. Inherit. Metab. Dis. 20:335-338(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DPYDD ARG-29; TRP-235 AND HIS-886.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-29.

Entry informationi

Entry nameiDPYD_HUMAN
AccessioniPrimary (citable) accession number: Q12882
Secondary accession number(s): A2RRQ2
, A2RRQ3, A8K5A2, A8MWG9, B1AN21, E9PFN1, Q16694, Q16761, Q32NB0, Q96HL6, Q96TH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 13, 2007
Last modified: February 4, 2015
This is version 158 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.