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Q12882

- DPYD_HUMAN

UniProt

Q12882 - DPYD_HUMAN

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Protein
Dihydropyrimidine dehydrogenase [NADP(+)]
Gene
DPYD
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 2 FAD.
Binds 2 FMN.
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 oxygen By 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 – 2351FAD By similarity
Binding sitei261 – 2611FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei371 – 3711NADP By similarity
Binding sitei550 – 5501FMN By similarity
Binding sitei609 – 6091Substrate By similarity
Active sitei671 – 6711Proton acceptor By similarity
Binding sitei709 – 7091FMN By similarity
Binding sitei767 – 7671FMN; via amide nitrogen By 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 – 1985FAD By similarity
Nucleotide bindingi218 – 2269FAD By similarity
Nucleotide bindingi340 – 3434NADP By similarity
Nucleotide bindingi364 – 3652NADP By similarity
Nucleotide bindingi437 – 4393NADP By similarity
Nucleotide bindingi480 – 48910FAD By similarity
Nucleotide bindingi481 – 4877NADP By similarity
Nucleotide bindingi574 – 5752FMN By similarity
Nucleotide bindingi793 – 7953FMN By similarity
Nucleotide bindingi816 – 8172FMN By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. UMP biosynthetic process Source: InterPro
  2. beta-alanine biosynthetic process Source: UniProtKB-UniPathway
  3. nucleobase-containing small molecule metabolic process Source: Reactome
  4. purine nucleobase catabolic process Source: UniProtKB
  5. pyrimidine nucleobase catabolic process Source: UniProtKB
  6. pyrimidine nucleobase metabolic process Source: Reactome
  7. pyrimidine nucleoside catabolic process Source: Reactome
  8. small molecule metabolic process Source: Reactome
  9. thymidine catabolic process Source: UniProtKB
  10. thymine catabolic process Source: UniProtKB
  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 deficiency (DPYDD) [MIM:274270]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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 – 33
PRO_0000021114
Chaini4 – 10251022Dihydropyrimidine dehydrogenase [NADP(+)]
PRO_0000021115Add
BLAST

Amino acid modifications

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

ArrayExpressiQ12882.
BgeeiQ12882.
CleanExiHS_DPYD.
GenevestigatoriQ12882.

Organism-specific databases

HPAiCAB033241.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi108140. 2 interactions.
IntActiQ12882. 18 interactions.
STRINGi9606.ENSP00000359211.

Structurei

3D structure databases

ProteinModelPortaliQ12882.
SMRiQ12882. Positions 2-1019.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0167.
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

MAPVLSKDSA DIESILALNP RTQTHATLCS TSAKKLDKKH WKRNPDKNCF     50
NCEKLENNFD DIKHTTLGER GALREAMRCL KCADAPCQKS CPTNLDIKSF 100
ITSIANKNYY GAAKMIFSDN PLGLTCGMVC PTSDLCVGGC NLYATEEGPI 150
NIGGLQQFAT EVFKAMSIPQ IRNPSLPPPE KMSEAYSAKI ALFGAGPASI 200
SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV VNFEIELMKD 250
LGVKIICGKS LSVNEMTLST LKEKGYKAAF IGIGLPEPNK DAIFQGLTQD 300
QGFYTSKDFL PLVAKGSKAG MCACHSPLPS IRGVVIVLGA GDTAFDCATS 350
ALRCGARRVF IVFRKGFVNI RAVPEEMELA KEEKCEFLPF LSPRKVIVKG 400
GRIVAMQFVR TEQDETGKWN EDEDQMVHLK ADVVISAFGS VLSDPKVKEA 450
LSPIKFNRWG LPEVDPETMQ TSEAWVFAGG DVVGLANTTV ESVNDGKQAS 500
WYIHKYVQSQ YGASVSAKPE LPLFYTPIDL VDISVEMAGL KFINPFGLAS 550
ATPATSTSMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI IRGTTSGPMY 600
GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNKNDW 650
TELAKKSEDS GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ 700
AVQIPFFAKL TPNVTDIVSI ARAAKEGGAN GVTATNTVSG LMGLKSDGTP 750
WPAVGIAKRT TYGGVSGTAI RPIALRAVTS IARALPGFPI LATGGIDSAE 800
SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL KSIEELQDWD 850
GQSPATVSHQ KGKPVPRIAE LMDKKLPSFG PYLEQRKKII AENKIRLKEQ 900
NVAFSPLKRN CFIPKRPIPT IKDVIGKALQ YLGTFGELSN VEQVVAMIDE 950
EMCINCGKCY MTCNDSGYQA IQFDPETHLP TITDTCTGCT LCLSVCPIVD 1000
CIKMVSRTTP YEPKRGVPLS VNPVC 1025
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

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.
VSP_044929Add
BLAST
Alternative sequencei174 – 1025852Missing in isoform 2.
VSP_044930Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311P → S in AAI08743. 1 Publication
Sequence conflicti845 – 8451E → G in BAF83906. 1 Publication
Sequence conflicti910 – 9101N → S in AAA57474. 1 Publication
Sequence conflicti1024 – 10241V → G in AAI31779. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000370192; ENSP00000359211; ENSG00000188641.
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS30777.1. [Q12882-1 ]
CCDS53346.1. [Q12882-2 ]
PIRi A54718.
RefSeqi NP_000101.2. NM_000110.3. [Q12882-1 ]
NP_001153773.1. NM_001160301.1. [Q12882-2 ]
UniGenei Hs.335034.

3D structure databases

ProteinModelPortali Q12882.
SMRi Q12882. Positions 2-1019.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108140. 2 interactions.
IntActi Q12882. 18 interactions.
STRINGi 9606.ENSP00000359211.

Chemistry

BindingDBi Q12882.
ChEMBLi CHEMBL3172.
DrugBanki DB01101. Capecitabine.
DB00109. Enfuvirtide.

PTM databases

PhosphoSitei Q12882.

Polymorphism databases

DMDMi 160332325.

Proteomic databases

MaxQBi Q12882.
PaxDbi Q12882.
PRIDEi Q12882.

Protocols and materials databases

DNASUi 1806.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370192 ; ENSP00000359211 ; ENSG00000188641 .
GeneIDi 1806.
KEGGi hsa:1806.
UCSCi uc001drv.3. human. [Q12882-1 ]
uc001drw.3. human.

Organism-specific databases

CTDi 1806.
GeneCardsi GC01M097543.
H-InvDB HIX0000804.
HGNCi HGNC:3012. DPYD.
HPAi CAB033241.
MIMi 274270. phenotype.
612779. gene.
neXtProti NX_Q12882.
Orphaneti 293948. 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.
PharmGKBi PA145.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0167.
HOVERGENi HBG004351.
InParanoidi Q12882.
KOi K00207.
OrthoDBi EOG7MH0X9.
PhylomeDBi Q12882.
TreeFami TF105791.

Enzyme and pathway databases

UniPathwayi UPA00131 .
Reactomei REACT_1023. Pyrimidine catabolism.

Miscellaneous databases

ChiTaRSi DPYD. human.
GeneWikii DPYD.
GenomeRNAii 1806.
NextBioi 35501869.
PROi Q12882.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q12882.
Bgeei Q12882.
CleanExi HS_DPYD.
Genevestigatori Q12882.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR017896. 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 ]
Pfami PF01180. DHO_dh. 1 hit.
PF14691. Fer4_20. 1 hit.
[Graphical view ]
SUPFAMi SSF46548. SSF46548. 1 hit.
TIGRFAMsi TIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEi PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 153 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

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