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Q12882

- DPYD_HUMAN

UniProt

Q12882 - DPYD_HUMAN

Protein

Dihydropyrimidine dehydrogenase [NADP(+)]

Gene

DPYD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    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.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 oxidase 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

    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

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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

    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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 154 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