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Q9EQF5

- DPYS_MOUSE

UniProt

Q9EQF5 - DPYS_MOUSE

Protein

Dihydropyrimidinase

Gene

Dpys

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate By similarity.By similarity

    Catalytic activityi

    5,6-dihydrouracil + H2O = 3-ureidopropanoate.

    Cofactori

    Binds 2 zinc ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi67 – 671Zinc 1By similarity
    Metal bindingi69 – 691Zinc 1By similarity
    Metal bindingi159 – 1591Zinc 1; via carbamate groupBy similarity
    Metal bindingi159 – 1591Zinc 2; via carbamate groupBy similarity
    Binding sitei164 – 1641SubstrateBy similarity
    Metal bindingi192 – 1921Zinc 2By similarity
    Metal bindingi248 – 2481Zinc 2By similarity
    Metal bindingi326 – 3261Zinc 1By similarity
    Binding sitei347 – 3471Substrate; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. amino acid binding Source: BHF-UCL
    2. dihydropyrimidinase activity Source: BHF-UCL
    3. phosphoprotein binding Source: BHF-UCL
    4. thymine binding Source: BHF-UCL
    5. uracil binding Source: BHF-UCL
    6. zinc ion binding Source: BHF-UCL

    GO - Biological processi

    1. beta-alanine metabolic process Source: BHF-UCL
    2. protein homooligomerization Source: BHF-UCL
    3. protein homotetramerization Source: BHF-UCL
    4. thymine catabolic process Source: BHF-UCL
    5. uracil catabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.5.2.2. 3474.

    Protein family/group databases

    MEROPSiM38.973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropyrimidinase (EC:3.5.2.2)
    Short name:
    DHP
    Short name:
    DHPase
    Alternative name(s):
    Dihydropyrimidine amidohydrolase
    Hydantoinase
    Gene namesi
    Name:Dpys
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1928679. Dpys.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: BHF-UCL

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 519519DihydropyrimidinasePRO_0000165907Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei159 – 1591N6-carboxylysineBy similarity
    Modified residuei256 – 2561N6-succinyllysine1 Publication

    Post-translational modificationi

    Carbamylation allows a single lysine to coordinate two zinc ions.By similarity

    Proteomic databases

    MaxQBiQ9EQF5.
    PaxDbiQ9EQF5.
    PRIDEiQ9EQF5.

    PTM databases

    PhosphoSiteiQ9EQF5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9EQF5.
    BgeeiQ9EQF5.
    CleanExiMM_DPYS.
    GenevestigatoriQ9EQF5.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi211101. 1 interaction.
    IntActiQ9EQF5. 1 interaction.
    MINTiMINT-1869933.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EQF5.
    SMRiQ9EQF5. Positions 6-493.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0044.
    GeneTreeiENSGT00740000115468.
    HOGENOMiHOG000219145.
    HOVERGENiHBG000806.
    InParanoidiQ9EQF5.
    KOiK01464.
    OMAiAVDYNIF.
    OrthoDBiEOG7SJD48.
    PhylomeDBiQ9EQF5.
    TreeFamiTF314706.

    Family and domain databases

    Gene3Di2.30.40.10. 2 hits.
    InterProiIPR006680. Amidohydro_1.
    IPR011778. Hydantoinase/dihydroPyrase.
    IPR011059. Metal-dep_hydrolase_composite.
    [Graphical view]
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51338. SSF51338. 2 hits.
    TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9EQF5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPQGRLLIR GGRIVNDDFS QVADVLVEDG VVRALGRDLL PPEDASRGLR    50
    ILDAAGKLVL PGGIDTHTHM QFPFMGSQSV DDFYQGTKAA LAGGTTMIID 100
    FAIPQKGSSL IEAFETWRNW ADPKVCCDYS LHVAVTWWSD KVKEEMKTLA 150
    RDKGVNSFKM FMAYKGLYMV QDEQLYAAFS QCKEIGAIAQ VHAENGDLIA 200
    EGAKKMLALG ITGPEGHELC RPEAVEAEAT LRAITIASAV NCPLYVVHVM 250
    SKSAAKVVAD ARRAGNVVYG EPIAAGLGTD GRQYWSEEWS HAAHHVMGPP 300
    LRPDPLTPGF LMDLLANGDL TTTGSDNCTF NTCQKALGKD DFTKIPNGVN 350
    GVEDRMSVIW EKGVHSGKMD ENRFVAVTST NAAKIFNLYP KKGRIAVGSD 400
    ADIVIWDPEA TRRISAKTHH QAVNFNIFEG MVCHGVPLVT ISRGRVVYEA 450
    GVFNVTAGHG KFIPRQPFAE YIYKRIKQRD QTCTPVPVKR APYKGEVTTL 500
    KARETKEDDT AGTRMQGHS 519
    Length:519
    Mass (Da):56,725
    Last modified:June 6, 2002 - v2
    Checksum:iF2C53D40EC120ABD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131R → L in AAG37999. (PubMed:10956643)Curated
    Sequence conflicti13 – 131R → L in AAH37086. (PubMed:15489334)Curated
    Sequence conflicti37 – 371R → P in AAK00644. 1 PublicationCurated
    Sequence conflicti43 – 431E → G in AAK00644. 1 PublicationCurated
    Sequence conflicti206 – 2061M → T in BAB23654. (PubMed:16141072)Curated
    Sequence conflicti299 – 2991P → L in AAK00644. 1 PublicationCurated
    Sequence conflicti366 – 3661S → N in AAK00644. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF249296 mRNA. Translation: AAG37999.1.
    AF227731 mRNA. Translation: AAK00644.1.
    AK004822 mRNA. Translation: BAB23593.1.
    AK004899 mRNA. Translation: BAB23654.1.
    BC037086 mRNA. Translation: AAH37086.1.
    CCDSiCCDS27445.1.
    RefSeqiNP_001157938.1. NM_001164466.1.
    NP_073559.3. NM_022722.3.
    UniGeneiMm.275974.

    Genome annotation databases

    EnsembliENSMUST00000022915; ENSMUSP00000022915; ENSMUSG00000022304.
    ENSMUST00000110306; ENSMUSP00000105935; ENSMUSG00000022304.
    GeneIDi64705.
    KEGGimmu:64705.
    UCSCiuc007vok.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF249296 mRNA. Translation: AAG37999.1 .
    AF227731 mRNA. Translation: AAK00644.1 .
    AK004822 mRNA. Translation: BAB23593.1 .
    AK004899 mRNA. Translation: BAB23654.1 .
    BC037086 mRNA. Translation: AAH37086.1 .
    CCDSi CCDS27445.1.
    RefSeqi NP_001157938.1. NM_001164466.1.
    NP_073559.3. NM_022722.3.
    UniGenei Mm.275974.

    3D structure databases

    ProteinModelPortali Q9EQF5.
    SMRi Q9EQF5. Positions 6-493.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211101. 1 interaction.
    IntActi Q9EQF5. 1 interaction.
    MINTi MINT-1869933.

    Protein family/group databases

    MEROPSi M38.973.

    PTM databases

    PhosphoSitei Q9EQF5.

    Proteomic databases

    MaxQBi Q9EQF5.
    PaxDbi Q9EQF5.
    PRIDEi Q9EQF5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022915 ; ENSMUSP00000022915 ; ENSMUSG00000022304 .
    ENSMUST00000110306 ; ENSMUSP00000105935 ; ENSMUSG00000022304 .
    GeneIDi 64705.
    KEGGi mmu:64705.
    UCSCi uc007vok.2. mouse.

    Organism-specific databases

    CTDi 1807.
    MGIi MGI:1928679. Dpys.

    Phylogenomic databases

    eggNOGi COG0044.
    GeneTreei ENSGT00740000115468.
    HOGENOMi HOG000219145.
    HOVERGENi HBG000806.
    InParanoidi Q9EQF5.
    KOi K01464.
    OMAi AVDYNIF.
    OrthoDBi EOG7SJD48.
    PhylomeDBi Q9EQF5.
    TreeFami TF314706.

    Enzyme and pathway databases

    BRENDAi 3.5.2.2. 3474.

    Miscellaneous databases

    NextBioi 320175.
    PROi Q9EQF5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9EQF5.
    Bgeei Q9EQF5.
    CleanExi MM_DPYS.
    Genevestigatori Q9EQF5.

    Family and domain databases

    Gene3Di 2.30.40.10. 2 hits.
    InterProi IPR006680. Amidohydro_1.
    IPR011778. Hydantoinase/dihydroPyrase.
    IPR011059. Metal-dep_hydrolase_composite.
    [Graphical view ]
    Pfami PF01979. Amidohydro_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51338. SSF51338. 2 hits.
    TIGRFAMsi TIGR02033. D-hydantoinase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of CRMP5, a novel member of the collapsin response mediator protein family."
      Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A., Matsuda Y., Noda M.
      J. Biol. Chem. 275:37957-37965(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Swiss Webster / NIH.
      Tissue: Embryo.
    2. "Molecular cloning, nucleotide sequencing, characterization and overexpression of dihydropyrimidinase from mouse liver."
      Chang C.J., Huang C.J., Yang Y.S., Wu T.K.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Liver and Lung.
    4. "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].
      Strain: FVB/N.
      Tissue: Liver.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiDPYS_MOUSE
    AccessioniPrimary (citable) accession number: Q9EQF5
    Secondary accession number(s): Q99PP1, Q9DBK3, Q9DBP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3