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Q12882 (DPYD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydropyrimidine dehydrogenase [NADP(+)]

Short name=DHPDHase
Short name=DPD
EC=1.3.1.2
Alternative name(s):
Dihydrothymine dehydrogenase
Dihydrouracil dehydrogenase
Gene names
Name:DPYD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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

Binds 2 FAD.

Binds 2 FMN.

Binds 4 4Fe-4S clusters. Contains approximately 16 iron atoms per subunit By similarity.

Pathway

Amino-acid biosynthesis; beta-alanine biosynthesis.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

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

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6 Ref.14 Ref.15

Sequence similarities

Belongs to the dihydropyrimidine dehydrogenase family.

Contains 3 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
   Ligand4Fe-4S
FAD
Flavoprotein
FMN
Iron
Iron-sulfur
Metal-binding
NADP
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processUMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

beta-alanine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

purine nucleobase catabolic process

Inferred from mutant phenotype PubMed 11988088. Source: UniProtKB

pyrimidine nucleobase catabolic process

Inferred from mutant phenotype PubMed 11988088. Source: UniProtKB

pyrimidine nucleobase metabolic process

Traceable author statement. Source: Reactome

pyrimidine nucleoside catabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

thymidine catabolic process

Inferred from direct assay Ref.11. Source: UniProtKB

thymine catabolic process

Inferred from direct assay PubMed 10410956. Source: UniProtKB

uracil catabolic process

Inferred from direct assay Ref.11PubMed 18075467. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 9348115. Source: UniProtKB

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NADP binding

Inferred from sequence or structural similarity. Source: UniProtKB

dihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

dihydropyrimidine dehydrogenase (NADP+) activity

Inferred from direct assay PubMed 10410956Ref.11PubMed 18075467. Source: UniProtKB

flavin adenine dinucleotide binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12882-1)

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.
Isoform 2 (identifier: Q12882-2)

The sequence of this isoform differs from the canonical sequence as follows:
     162-173: VFKAMSIPQIRN → TLILAFSLMNHL
     174-1025: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 33
PRO_0000021114
Chain4 – 10251022Dihydropyrimidine dehydrogenase [NADP(+)]
PRO_0000021115

Regions

Domain69 – 100324Fe-4S ferredoxin-type 1
Domain944 – 976334Fe-4S ferredoxin-type 2
Domain978 – 1007304Fe-4S ferredoxin-type 3
Nucleotide binding194 – 1985FAD By similarity
Nucleotide binding218 – 2269FAD By similarity
Nucleotide binding340 – 3434NADP By similarity
Nucleotide binding364 – 3652NADP By similarity
Nucleotide binding437 – 4393NADP By similarity
Nucleotide binding480 – 48910FAD By similarity
Nucleotide binding481 – 4877NADP By similarity
Nucleotide binding574 – 5752FMN By similarity
Nucleotide binding793 – 7953FMN By similarity
Nucleotide binding816 – 8172FMN By similarity
Region668 – 6703Substrate binding By similarity
Region736 – 7372Substrate binding By similarity

Sites

Active site6711Proton acceptor By similarity
Metal binding791Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding821Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding871Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding911Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1301Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1401Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1561Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding9531Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding9561Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding9591Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding9631Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding9861Iron-sulfur 4 (4Fe-4S) By similarity
Metal binding9891Iron-sulfur 4 (4Fe-4S) By similarity
Metal binding9921Iron-sulfur 4 (4Fe-4S) By similarity
Metal binding9961Iron-sulfur 4 (4Fe-4S) By similarity
Binding site1291FAD; via carbonyl oxygen By similarity
Binding site2351FAD By similarity
Binding site2611FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3711NADP By similarity
Binding site5501FMN By similarity
Binding site6091Substrate By similarity
Binding site7091FMN By similarity
Binding site7671FMN; via amide nitrogen By similarity

Amino acid modifications

Modified residue3841N6-acetyllysine Ref.12
Modified residue9051Phosphoserine By similarity

Natural variations

Alternative sequence162 – 17312VFKAM…PQIRN → TLILAFSLMNHL in isoform 2.
VSP_044929
Alternative sequence174 – 1025852Missing in isoform 2.
VSP_044930
Natural variant291C → R in DPYDD; allele DPYD*9A and allele DPYD*9B; loss of activity. Ref.5 Ref.6 Ref.14 Ref.15 Ref.16
Corresponds to variant rs1801265 [ dbSNP | Ensembl ].
VAR_005173
Natural variant1661M → V.
Corresponds to variant rs2297595 [ dbSNP | Ensembl ].
VAR_054034
Natural variant2351R → W in DPYDD; allele DPYD*8; loss of activity. Ref.14 Ref.15
Corresponds to variant rs1801266 [ dbSNP | Ensembl ].
VAR_005174
Natural variant5341S → N in allele DPYD*4; low activity.
Corresponds to variant rs1801158 [ dbSNP | Ensembl ].
VAR_005175
Natural variant5431I → V in allele DPYD*5. Ref.8
Corresponds to variant rs1801159 [ dbSNP | Ensembl ].
VAR_005176
Natural variant7321V → I. Ref.8
Corresponds to variant rs1801160 [ dbSNP | Ensembl ].
VAR_014760
Natural variant8861R → H in DPYDD; allele DPYD*9B; 25% of activity. Ref.14 Ref.15
Corresponds to variant rs1801267 [ dbSNP | Ensembl ].
VAR_005177
Natural variant9951V → F in allele DPYD*10; low activity.
Corresponds to variant rs1801268 [ dbSNP | Ensembl ].
VAR_005178

Experimental info

Sequence conflict1311P → S in AAI08743. Ref.6
Sequence conflict8451E → G in BAF83906. Ref.5
Sequence conflict9101N → S in AAA57474. Ref.1
Sequence conflict10241V → G in AAI31779. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 0201943955AB2C21

FASTA1,025111,401
        10         20         30         40         50         60 
MAPVLSKDSA DIESILALNP RTQTHATLCS TSAKKLDKKH WKRNPDKNCF NCEKLENNFD 

        70         80         90        100        110        120 
DIKHTTLGER GALREAMRCL KCADAPCQKS CPTNLDIKSF ITSIANKNYY GAAKMIFSDN 

       130        140        150        160        170        180 
PLGLTCGMVC PTSDLCVGGC NLYATEEGPI NIGGLQQFAT EVFKAMSIPQ IRNPSLPPPE 

       190        200        210        220        230        240 
KMSEAYSAKI ALFGAGPASI SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV 

       250        260        270        280        290        300 
VNFEIELMKD LGVKIICGKS LSVNEMTLST LKEKGYKAAF IGIGLPEPNK DAIFQGLTQD 

       310        320        330        340        350        360 
QGFYTSKDFL PLVAKGSKAG MCACHSPLPS IRGVVIVLGA GDTAFDCATS ALRCGARRVF 

       370        380        390        400        410        420 
IVFRKGFVNI RAVPEEMELA KEEKCEFLPF LSPRKVIVKG GRIVAMQFVR TEQDETGKWN 

       430        440        450        460        470        480 
EDEDQMVHLK ADVVISAFGS VLSDPKVKEA LSPIKFNRWG LPEVDPETMQ TSEAWVFAGG 

       490        500        510        520        530        540 
DVVGLANTTV ESVNDGKQAS WYIHKYVQSQ YGASVSAKPE LPLFYTPIDL VDISVEMAGL 

       550        560        570        580        590        600 
KFINPFGLAS ATPATSTSMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI IRGTTSGPMY 

       610        620        630        640        650        660 
GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNKNDW TELAKKSEDS 

       670        680        690        700        710        720 
GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ AVQIPFFAKL TPNVTDIVSI 

       730        740        750        760        770        780 
ARAAKEGGAN GVTATNTVSG LMGLKSDGTP WPAVGIAKRT TYGGVSGTAI RPIALRAVTS 

       790        800        810        820        830        840 
IARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAIQ NQDFTVIEDY CTGLKALLYL 

       850        860        870        880        890        900 
KSIEELQDWD GQSPATVSHQ KGKPVPRIAE LMDKKLPSFG PYLEQRKKII AENKIRLKEQ 

       910        920        930        940        950        960 
NVAFSPLKRN CFIPKRPIPT IKDVIGKALQ YLGTFGELSN VEQVVAMIDE EMCINCGKCY 

       970        980        990       1000       1010       1020 
MTCNDSGYQA IQFDPETHLP TITDTCTGCT LCLSVCPIVD CIKMVSRTTP YEPKRGVPLS 


VNPVC 

« Hide

Isoform 2 [UniParc].

Checksum: 94D241E912F29B6B
Show »

FASTA17318,936

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
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. expand/collapse author list , 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.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-29.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , AC091608, AC093576, AC099787, AC114878, AC138135, BX908805 Genomic DNA. Translation: CAH70570.1.
BX908805 expand/collapse EMBL AC list , 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.
CCDSCCDS30777.1. [Q12882-1]
CCDS53346.1. [Q12882-2]
PIRA54718.
RefSeqNP_000101.2. NM_000110.3. [Q12882-1]
NP_001153773.1. NM_001160301.1. [Q12882-2]
UniGeneHs.335034.

3D structure databases

ProteinModelPortalQ12882.
SMRQ12882. Positions 2-1019.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108140. 2 interactions.
IntActQ12882. 18 interactions.
STRING9606.ENSP00000359211.

Chemistry

BindingDBQ12882.
ChEMBLCHEMBL3172.
DrugBankDB01101. Capecitabine.
DB00109. Enfuvirtide.

PTM databases

PhosphoSiteQ12882.

Polymorphism databases

DMDM160332325.

Proteomic databases

MaxQBQ12882.
PaxDbQ12882.
PRIDEQ12882.

Protocols and materials databases

DNASU1806.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370192; ENSP00000359211; ENSG00000188641.
GeneID1806.
KEGGhsa:1806.
UCSCuc001drv.3. human. [Q12882-1]
uc001drw.3. human.

Organism-specific databases

CTD1806.
GeneCardsGC01M097543.
H-InvDBHIX0000804.
HGNCHGNC:3012. DPYD.
HPACAB033241.
MIM274270. phenotype.
612779. gene.
neXtProtNX_Q12882.
Orphanet293948. 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.
PharmGKBPA145.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0167.
HOVERGENHBG004351.
InParanoidQ12882.
KOK00207.
OrthoDBEOG7MH0X9.
PhylomeDBQ12882.
TreeFamTF105791.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00131.

Gene expression databases

ArrayExpressQ12882.
BgeeQ12882.
CleanExHS_DPYD.
GenevestigatorQ12882.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR017896. 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]
PfamPF01180. DHO_dh. 1 hit.
PF14691. Fer4_20. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
TIGRFAMsTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDPYD. human.
GeneWikiDPYD.
GenomeRNAi1806.
NextBio35501869.
PROQ12882.
SOURCESearch...

Entry information

Entry nameDPYD_HUMAN
AccessionPrimary (citable) accession number: Q12882
Secondary accession number(s): A2RRQ2 expand/collapse secondary AC list , A2RRQ3, A8K5A2, A8MWG9, B1AN21, E9PFN1, Q16694, Q16761, Q32NB0, Q96HL6, Q96TH1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM