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Dihydropyrimidine dehydrogenase [NADP( )] (DHPDHase) (DPD) (EC 1.3.1.2) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase)

 DPYD_HUMAN              Reviewed;        1025 AA.
Q12882; A2RRQ2; A2RRQ3; A8K5A2; A8MWG9; B1AN21; E9PFN1; Q16694;
Q16761; Q32NB0; Q96HL6; Q96TH1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
10-OCT-2018, entry version 186.
RecName: Full=Dihydropyrimidine dehydrogenase [NADP(+)];
Short=DHPDHase;
Short=DPD;
EC=1.3.1.2;
AltName: Full=Dihydrothymine dehydrogenase;
AltName: Full=Dihydrouracil dehydrogenase;
Flags: Precursor;
Name=DPYD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8083224;
Yokota H., Fernandez-Salguero P., Furuya H., Lin K., McBride O.W.,
Podschun B., Schnackerz K.D., Gonzalez F.J.;
"cDNA cloning and chromosome mapping of human dihydropyrimidine
dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and
congenital thymine uraciluria.";
J. Biol. Chem. 269:23192-23196(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9135003;
Johnson M.R., Wang K., Tillmanns S., Albin N., Diasio R.B.;
"Structural organization of the human dihydropyrimidine dehydrogenase
gene.";
Cancer Res. 57:1660-1663(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9464498; DOI=10.1016/S0304-3835(97)00377-7;
Ogura K., Nishiyama T., Takubo H., Kato A., Okuda H., Arakawa K.,
Fukushima M., Nagayama S., Kawaguchi Y., Watabe T.;
"Suicidal inactivation of human dihydropyrimidine dehydrogenase by
(E)-5-(2-bromovinyl)uracil derived from the antiviral, sorivudine.";
Cancer Lett. 122:107-113(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT DPYDD
ARG-29.
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT DPYDD
ARG-29.
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS VAL-543 AND ILE-732.
TISSUE=Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 581-635.
TISSUE=Liver;
PubMed=8892022; DOI=10.1007/BF01799841;
Vreken P., van Kuilenburg A.B.P., Meinsma R., Smit G.P.A.,
Bakker H.D., de Abreu R.A., van Gennip A.H.;
"A point mutation in an invariant splice donor site leads to exon
skipping in two unrelated Dutch patients with dihydropyrimidine
dehydrogenase deficiency.";
J. Inherit. Metab. Dis. 19:645-654(1996).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 581-635.
PubMed=9170156;
Fernandez-Salguero P.M., Sapone A., Wei X., Holt J.R., Jones S.,
Idle J.R., Gonzalez F.J.;
"Lack of correlation between phenotype and genotype for the
polymorphically expressed dihydropyrimidine dehydrogenase in a family
of Pakistani origin.";
Pharmacogenetics 7:161-163(1997).
[11]
CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=1512248;
Lu Z.-H., Zhang R., Diasio R.B.;
"Purification and characterization of dihydropyrimidine dehydrogenase
from human liver.";
J. Biol. Chem. 267:17102-17109(1992).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
VARIANTS DPYDD ARG-29; TRP-235 AND HIS-886.
PubMed=9439663; DOI=10.1007/s004390050637;
Vreken P., van Kuilenburg A.B.P., Meinsma R., van Gennip A.H.;
"Dihydropyrimidine dehydrogenase (DPD) deficiency: identification and
expression of missense mutations C29R, R886H and R235W.";
Hum. Genet. 101:333-338(1997).
[17]
VARIANTS DPYDD ARG-29; TRP-235 AND HIS-886.
PubMed=9266349; DOI=10.1023/A:1005357307122;
Vreken P., van Kuilenburg A.B.P., Meinsma R., van Gennip A.H.;
"Identification of novel point mutations in the dihydropyrimidine
dehydrogenase gene.";
J. Inherit. Metab. Dis. 20:335-338(1997).
[18]
VARIANTS ASN-534 AND VAL-543.
PubMed=9472650; DOI=10.1038/bjc.1998.79;
Ridge S.A., Sludden J., Wei X., Sapone A., Brown O., Hardy S.,
Canney P., Fernandez-Salguero P., Gonzalez F.J., Cassidy J.,
McLeod H.L.;
"Dihydropyrimidine dehydrogenase pharmacogenetics in patients with
colorectal cancer.";
Br. J. Cancer 77:497-500(1998).
[19]
VARIANTS ASN-534; VAL-543 AND ILE-732.
PubMed=9723824; DOI=10.1046/j.1365-2125.1998.00751.x;
Ridge S.A., Sludden J., Brown O., Robertson L., Wei X., Sapone A.,
Fernandez-Salguero P.M., Gonzalez F.J., Vreken P.,
van Kuilenburg A.B., van Gennip A.H., McLeod H.L.;
"Dihydropyrimidine dehydrogenase pharmacogenetics in Caucasian
subjects.";
Br. J. Clin. Pharmacol. 46:151-156(1998).
[20]
VARIANT [LARGE SCALE ANALYSIS] ARG-29.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: Involved in pyrimidine base degradation. Catalyzes the
reduction of uracil and thymine. Also involved the degradation of
the chemotherapeutic drug 5-fluorouracil.
-!- CATALYTIC ACTIVITY: 5,6-dihydrouracil + NADP(+) = uracil + NADPH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 2 FAD.;
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Note=Binds 2 FMN.;
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron
atoms per subunit. {ECO:0000250};
-!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis.
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
Q9HD26:GOPC; NbExp=3; IntAct=EBI-2839838, EBI-349832;
Q9BS40:LXN; NbExp=3; IntAct=EBI-2839838, EBI-1044504;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q12882-1; Sequence=Displayed;
Name=2;
IsoId=Q12882-2; Sequence=VSP_044929, VSP_044930;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Found in most tissues with greatest activity
found in liver and peripheral blood mononuclear cells.
-!- DISEASE: 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. {ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:16710414, ECO:0000269|PubMed:9266349,
ECO:0000269|PubMed:9439663}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
{ECO:0000305}.
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EMBL; U09178; AAA57474.1; -; mRNA.
EMBL; U20938; AAB51366.1; -; mRNA.
EMBL; AB003063; BAA89789.1; -; mRNA.
EMBL; BT006740; AAP35386.1; -; mRNA.
EMBL; AK291217; BAF83906.1; -; mRNA.
EMBL; AC091608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC099787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC114878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX908805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471097; EAW73002.1; -; Genomic_DNA.
EMBL; BC008379; AAH08379.1; -; mRNA.
EMBL; BC064027; AAH64027.1; -; mRNA.
EMBL; BC108742; AAI08743.1; -; mRNA.
EMBL; BC131777; AAI31778.1; -; mRNA.
EMBL; BC131778; AAI31779.1; -; mRNA.
EMBL; X95670; CAA64973.1; -; Genomic_DNA.
EMBL; U57655; AAB07049.1; -; Genomic_DNA.
CCDS; CCDS30777.1; -. [Q12882-1]
CCDS; CCDS53346.1; -. [Q12882-2]
PIR; A54718; A54718.
RefSeq; NP_000101.2; NM_000110.3. [Q12882-1]
RefSeq; NP_001153773.1; NM_001160301.1. [Q12882-2]
UniGene; Hs.335034; -.
ProteinModelPortal; Q12882; -.
SMR; Q12882; -.
BioGrid; 108140; 9.
IntAct; Q12882; 20.
STRING; 9606.ENSP00000359211; -.
BindingDB; Q12882; -.
ChEMBL; CHEMBL3172; -.
DrugBank; DB03554; 5-Iodouracil.
DrugBank; DB03048; 6-Carboxymethyluracil.
DrugBank; DB01101; Capecitabine.
DrugBank; DB03516; Eniluracil.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB00544; Fluorouracil.
DrugBank; DB02338; Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate.
DrugBank; DB03247; Riboflavin Monophosphate.
DrugBank; DB03419; Uracil.
CarbonylDB; Q12882; -.
iPTMnet; Q12882; -.
PhosphoSitePlus; Q12882; -.
BioMuta; DPYD; -.
DMDM; 160332325; -.
EPD; Q12882; -.
MaxQB; Q12882; -.
PaxDb; Q12882; -.
PeptideAtlas; Q12882; -.
PRIDE; Q12882; -.
ProteomicsDB; 58999; -.
DNASU; 1806; -.
Ensembl; ENST00000306031; ENSP00000307107; ENSG00000188641. [Q12882-2]
Ensembl; ENST00000370192; ENSP00000359211; ENSG00000188641. [Q12882-1]
GeneID; 1806; -.
KEGG; hsa:1806; -.
UCSC; uc001drv.4; human. [Q12882-1]
CTD; 1806; -.
DisGeNET; 1806; -.
EuPathDB; HostDB:ENSG00000188641.12; -.
GeneCards; DPYD; -.
H-InvDB; HIX0000804; -.
HGNC; HGNC:3012; DPYD.
HPA; CAB033241; -.
HPA; HPA045210; -.
MalaCards; DPYD; -.
MIM; 274270; phenotype.
MIM; 612779; gene.
neXtProt; NX_Q12882; -.
OpenTargets; ENSG00000188641; -.
Orphanet; 293948; 1p21.3 microdeletion syndrome.
Orphanet; 240839; 5-fluorouracil toxicity.
Orphanet; 1675; Dihydropyrimidine dehydrogenase deficiency.
PharmGKB; PA145; -.
eggNOG; KOG0399; Eukaryota.
eggNOG; COG0167; LUCA.
eggNOG; COG0493; LUCA.
eggNOG; COG1146; LUCA.
GeneTree; ENSGT00500000044896; -.
HOGENOM; HOG000169491; -.
HOVERGEN; HBG074715; -.
InParanoid; Q12882; -.
KO; K00207; -.
OMA; EQGWGFV; -.
OrthoDB; EOG091G00YL; -.
PhylomeDB; Q12882; -.
TreeFam; TF105791; -.
BioCyc; MetaCyc:HS06975-MONOMER; -.
BRENDA; 1.3.1.2; 2681.
Reactome; R-HSA-73621; Pyrimidine catabolism.
SIGNOR; Q12882; -.
UniPathway; UPA00131; -.
ChiTaRS; DPYD; human.
GeneWiki; DPYD; -.
GenomeRNAi; 1806; -.
PRO; PR:Q12882; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000188641; Expressed in 219 organ(s), highest expression level in germinal epithelium of ovary.
CleanEx; HS_DPYD; -.
Genevisible; Q12882; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006145; P:purine nucleobase catabolic process; IMP:UniProtKB.
GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IMP:UniProtKB.
GO; GO:0046135; P:pyrimidine nucleoside catabolic process; TAS:Reactome.
GO; GO:0006214; P:thymidine catabolic process; IDA:UniProtKB.
GO; GO:0006210; P:thymine catabolic process; IDA:UniProtKB.
GO; GO:0006212; P:uracil catabolic process; IDA:UniProtKB.
Gene3D; 1.10.1060.10; -; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.50.50.60; -; 3.
InterPro; IPR017896; 4Fe4S_Fe-S-bd.
InterPro; IPR017900; 4Fe4S_Fe_S_CS.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR005720; Dihydroorotate_DH.
InterPro; IPR028261; DPD_II.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR009051; Helical_ferredxn.
Pfam; PF01180; DHO_dh; 1.
Pfam; PF14691; Fer4_20; 1.
Pfam; PF07992; Pyr_redox_2; 1.
SUPFAM; SSF46548; SSF46548; 1.
TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
PROSITE; PS00198; 4FE4S_FER_1; 1.
PROSITE; PS51379; 4FE4S_FER_2; 3.
1: Evidence at protein level;
4Fe-4S; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; FAD;
Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NADP;
Nucleotide-binding; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome; Repeat.
PROPEP 1 3
/FTId=PRO_0000021114.
CHAIN 4 1025 Dihydropyrimidine dehydrogenase
[NADP(+)].
/FTId=PRO_0000021115.
DOMAIN 69 100 4Fe-4S ferredoxin-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
DOMAIN 944 976 4Fe-4S ferredoxin-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
DOMAIN 978 1007 4Fe-4S ferredoxin-type 3.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
NP_BIND 194 198 FAD. {ECO:0000250}.
NP_BIND 218 226 FAD. {ECO:0000250}.
NP_BIND 340 343 NADP. {ECO:0000250}.
NP_BIND 364 365 NADP. {ECO:0000250}.
NP_BIND 437 439 NADP. {ECO:0000250}.
NP_BIND 480 489 FAD. {ECO:0000250}.
NP_BIND 481 487 NADP. {ECO:0000250}.
NP_BIND 574 575 FMN. {ECO:0000250}.
NP_BIND 793 795 FMN. {ECO:0000250}.
NP_BIND 816 817 FMN. {ECO:0000250}.
REGION 668 670 Substrate binding. {ECO:0000250}.
REGION 736 737 Substrate binding. {ECO:0000250}.
ACT_SITE 671 671 Proton acceptor. {ECO:0000250}.
METAL 79 79 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
METAL 82 82 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
METAL 87 87 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
METAL 91 91 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
METAL 130 130 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
METAL 136 136 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
METAL 140 140 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
METAL 156 156 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
METAL 953 953 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 956 956 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 959 959 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 963 963 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 986 986 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
METAL 989 989 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
METAL 992 992 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
METAL 996 996 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}.
BINDING 129 129 FAD; via carbonyl oxygen. {ECO:0000250}.
BINDING 235 235 FAD. {ECO:0000250}.
BINDING 261 261 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 371 371 NADP. {ECO:0000250}.
BINDING 550 550 FMN. {ECO:0000250}.
BINDING 609 609 Substrate. {ECO:0000250}.
BINDING 709 709 FMN. {ECO:0000250}.
BINDING 767 767 FMN; via amide nitrogen. {ECO:0000250}.
MOD_RES 384 384 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 905 905 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 162 173 VFKAMSIPQIRN -> TLILAFSLMNHL (in isoform
2). {ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_044929.
VAR_SEQ 174 1025 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_044930.
VARIANT 29 29 C -> R (in DPYDD; allele DPYD*9A and
allele DPYD*9B; loss of activity;
dbSNP:rs1801265).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:16710414,
ECO:0000269|PubMed:18987736,
ECO:0000269|PubMed:9266349,
ECO:0000269|PubMed:9439663}.
/FTId=VAR_005173.
VARIANT 166 166 M -> V (in dbSNP:rs2297595).
/FTId=VAR_054034.
VARIANT 235 235 R -> W (in DPYDD; allele DPYD*8; loss of
activity; dbSNP:rs1801266).
{ECO:0000269|PubMed:9266349,
ECO:0000269|PubMed:9439663}.
/FTId=VAR_005174.
VARIANT 534 534 S -> N (in allele DPYD*4;
dbSNP:rs1801158).
{ECO:0000269|PubMed:9472650,
ECO:0000269|PubMed:9723824}.
/FTId=VAR_005175.
VARIANT 543 543 I -> V (in allele DPYD*5;
dbSNP:rs1801159).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9472650,
ECO:0000269|PubMed:9723824}.
/FTId=VAR_005176.
VARIANT 732 732 V -> I (in dbSNP:rs1801160).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9723824}.
/FTId=VAR_014760.
VARIANT 886 886 R -> H (in DPYDD; allele DPYD*9B; 25% of
activity; dbSNP:rs1801267).
{ECO:0000269|PubMed:9266349,
ECO:0000269|PubMed:9439663}.
/FTId=VAR_005177.
VARIANT 995 995 V -> F (in allele DPYD*10; low activity;
dbSNP:rs1801268).
/FTId=VAR_005178.
CONFLICT 131 131 P -> S (in Ref. 6; AAI08743).
{ECO:0000305}.
CONFLICT 845 845 E -> G (in Ref. 5; BAF83906).
{ECO:0000305}.
CONFLICT 910 910 N -> S (in Ref. 1; AAA57474).
{ECO:0000305}.
CONFLICT 1024 1024 V -> G (in Ref. 8; AAI31779).
{ECO:0000305}.
SEQUENCE 1025 AA; 111401 MW; 0201943955AB2C21 CRC64;
MAPVLSKDSA DIESILALNP RTQTHATLCS TSAKKLDKKH WKRNPDKNCF NCEKLENNFD
DIKHTTLGER GALREAMRCL KCADAPCQKS CPTNLDIKSF ITSIANKNYY GAAKMIFSDN
PLGLTCGMVC PTSDLCVGGC NLYATEEGPI NIGGLQQFAT EVFKAMSIPQ IRNPSLPPPE
KMSEAYSAKI ALFGAGPASI SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV
VNFEIELMKD LGVKIICGKS LSVNEMTLST LKEKGYKAAF IGIGLPEPNK DAIFQGLTQD
QGFYTSKDFL PLVAKGSKAG MCACHSPLPS IRGVVIVLGA GDTAFDCATS ALRCGARRVF
IVFRKGFVNI RAVPEEMELA KEEKCEFLPF LSPRKVIVKG GRIVAMQFVR TEQDETGKWN
EDEDQMVHLK ADVVISAFGS VLSDPKVKEA LSPIKFNRWG LPEVDPETMQ TSEAWVFAGG
DVVGLANTTV ESVNDGKQAS WYIHKYVQSQ YGASVSAKPE LPLFYTPIDL VDISVEMAGL
KFINPFGLAS ATPATSTSMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI IRGTTSGPMY
GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNKNDW TELAKKSEDS
GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ AVQIPFFAKL TPNVTDIVSI
ARAAKEGGAN GVTATNTVSG LMGLKSDGTP WPAVGIAKRT TYGGVSGTAI RPIALRAVTS
IARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL
KSIEELQDWD GQSPATVSHQ KGKPVPRIAE LMDKKLPSFG PYLEQRKKII AENKIRLKEQ
NVAFSPLKRN CFIPKRPIPT IKDVIGKALQ YLGTFGELSN VEQVVAMIDE EMCINCGKCY
MTCNDSGYQA IQFDPETHLP TITDTCTGCT LCLSVCPIVD CIKMVSRTTP YEPKRGVPLS
VNPVC


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