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P33316

- DUT_HUMAN

UniProt

P33316 - DUT_HUMAN

Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial

Gene

DUT

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 4 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.1 Publication

    Catalytic activityi

    dUTP + H2O = dUMP + diphosphate.1 Publication

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Phosphorylation is necessary for activity.

    Kineticsi

    for both isoform 2 and isoform 3.

    1. KM=2.5 µM for dUTP1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei198 – 1981Substrate; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei241 – 2411SubstrateBy similarity

    GO - Molecular functioni

    1. dUTP diphosphatase activity Source: Reactome
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. DNA replication Source: ProtInc
    2. dUMP biosynthetic process Source: UniProtKB-UniPathway
    3. dUTP metabolic process Source: InterPro
    4. nucleobase-containing compound metabolic process Source: ProtInc
    5. nucleobase-containing small molecule metabolic process Source: Reactome
    6. pyrimidine nucleobase metabolic process Source: Reactome
    7. pyrimidine nucleoside biosynthetic process Source: Reactome
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05235-MONOMER.
    BRENDAi3.6.1.23. 2681.
    ReactomeiREACT_21376. Pyrimidine biosynthesis.
    SABIO-RKP33316.
    UniPathwayiUPA00610; UER00666.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (EC:3.6.1.23)
    Short name:
    dUTPase
    Alternative name(s):
    dUTP pyrophosphatase
    Gene namesi
    Name:DUT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:3078. DUT.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrion Source: ProtInc
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi99 – 991S → A: Loss of phosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA151.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6969Mitochondrion2 PublicationsAdd
    BLAST
    Chaini70 – 252183Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrialPRO_0000007392Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei88 – 881Phosphoserine2 Publications

    Post-translational modificationi

    Nuclear isoform 2 is phosphorylated in vivo on Ser-11, a reaction that can be catalyzed in vitro by CDC2. Phosphorylation in mature T-cells occurs in a cell cycle-dependent manner. Isoform 3 is not phosphorylated.2 Publications
    The initiator methionine is cleaved in isoform 2.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP33316.
    PaxDbiP33316.
    PeptideAtlasiP33316.
    PRIDEiP33316.

    PTM databases

    PhosphoSiteiP33316.

    Expressioni

    Tissue specificityi

    Found in a variety of tissues. Isoform 3 expression is constitutive, while isoform 2 expression correlates with the onset of DNA replication (at protein level). Isoform 2 degradation coincides with the cessation of nuclear DNA replication (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP33316.
    BgeeiP33316.
    CleanExiHS_DUT.
    GenevestigatoriP33316.

    Organism-specific databases

    HPAiHPA054422.

    Interactioni

    Subunit structurei

    Homotrimer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NUDT18Q6ZVK83EBI-353224,EBI-740486

    Protein-protein interaction databases

    BioGridi108187. 14 interactions.
    IntActiP33316. 21 interactions.
    MINTiMINT-1436411.

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi113 – 1208
    Beta strandi127 – 1304
    Beta strandi134 – 1396
    Beta strandi144 – 1463
    Beta strandi150 – 1556
    Beta strandi158 – 1614
    Beta strandi166 – 1716
    Helixi174 – 1807
    Beta strandi182 – 1854
    Beta strandi198 – 2036
    Beta strandi205 – 2073
    Beta strandi209 – 2113
    Beta strandi216 – 22611
    Beta strandi229 – 2324
    Beta strandi240 – 2423
    Turni246 – 2494

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q5HX-ray2.00A/B/C112-252[»]
    1Q5UX-ray2.00X/Y/Z112-252[»]
    2HQUX-ray2.20A/B/C94-252[»]
    3ARAX-ray1.70A/B/C94-252[»]
    3ARNX-ray1.80A/B/C94-252[»]
    3EHWX-ray1.80A/B/C/X/Y/Z94-252[»]
    4MZ5X-ray2.10A/C97-109[»]
    4MZ6X-ray1.88A/C97-109[»]
    ProteinModelPortaliP33316.
    SMRiP33316. Positions 112-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33316.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni173 – 1753Substrate binding
    Regioni187 – 1904Substrate binding
    Regioni246 – 2472Substrate binding

    Sequence similaritiesi

    Belongs to the dUTPase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0756.
    KOiK01520.
    OMAiMIEDENE.
    PhylomeDBiP33316.
    TreeFamiTF105416.

    Family and domain databases

    Gene3Di2.70.40.10. 1 hit.
    InterProiIPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    [Graphical view]
    PfamiPF00692. dUTPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51283. SSF51283. 1 hit.
    TIGRFAMsiTIGR00576. dut. 1 hit.

    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 3 (identifier: P33316-3) [UniParc]FASTAAdd to Basket

    Also known as: DUT-M

    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

    MTPLCPRPAL CYHFLTSLLR SAMQNARGAR QRAEAAVLSG PGPPLGRAAQ    50
    HGIPRPLSSA GRLSQGCRGA STVGAAGWKG ELPKAGGSPA PGPETPAISP 100
    SKRARPAEVG GMQLRFARLS EHATAPTRGS ARAAGYDLYS AYDYTIPPME 150
    KAVVKTDIQI ALPSGCYGRV APRSGLAAKH FIDVGAGVID EDYRGNVGVV 200
    LFNFGKEKFE VKKGDRIAQL ICERIFYPEI EEVQALDDTE RGSGGFGSTG 250
    KN 252
    Length:252
    Mass (Da):26,563
    Last modified:September 21, 2011 - v4
    Checksum:i8E2EBC9ED5B0FAD2
    GO
    Isoform 2 (identifier: P33316-2) [UniParc]FASTAAdd to Basket

    Also known as: DUT-N

    The sequence of this isoform differs from the canonical sequence as follows:
         1-93: MTPLCPRPAL...KAGGSPAPGP → MPCSE

    Note: Major isoform. Phosphorylated in Ser-11. Contains a phosphoserine at position 11.

    Show »
    Length:164
    Mass (Da):17,748
    Checksum:iE75BC583BF8C7245
    GO

    Sequence cautioni

    The sequence AAB71393.1 differs from that shown. Reason: Frameshift at positions 29 and 47.
    The sequence AAB93866.1 differs from that shown. Reason: Frameshift at positions 29 and 47.
    The sequence AAB94642.1 differs from that shown. Reason: Frameshift at positions 29 and 47.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti175 – 1751G → S in BAF84204. (PubMed:14702039)Curated
    Sequence conflicti182 – 1821I → T in BAG60677. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti100 – 1001P → S.1 Publication
    Corresponds to variant rs28381104 [ dbSNP | Ensembl ].
    VAR_022314

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9393MTPLC…PAPGP → MPCSE in isoform 2. 6 PublicationsVSP_001324Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31930 mRNA. Translation: AAC50418.1.
    U62891 mRNA. Translation: AAC51123.1.
    AF018432
    , AF018429, AF018430, AF018431 Genomic DNA. Translation: AAB71393.1. Frameshift.
    AF018432
    , AF018429, AF018430, AF018431 Genomic DNA. Translation: AAB71394.1.
    U90223 mRNA. Translation: AAB94642.1. Frameshift.
    U90224 Genomic DNA. Translation: AAB93866.1. Frameshift.
    U90224 Genomic DNA. Translation: AAB93867.1.
    AB049113 mRNA. Translation: BAB13724.1.
    AY935242 Genomic DNA. Translation: AAX14045.1.
    AK291515 mRNA. Translation: BAF84204.1.
    AK312122 mRNA. Translation: BAG35058.1.
    CR541720 mRNA. Translation: CAG46521.1.
    CR541781 mRNA. Translation: CAG46580.1.
    CH471082 Genomic DNA. Translation: EAW77350.1.
    AK298464 mRNA. Translation: BAG60677.1.
    BC033645 mRNA. Translation: AAH33645.1.
    BC070339 mRNA. Translation: AAH70339.1.
    BC110377 mRNA. Translation: AAI10378.1.
    M89913 mRNA. Translation: AAA58444.1.
    L11877 mRNA. Translation: AAA36801.1.
    CCDSiCCDS32231.1. [P33316-3]
    CCDS45255.1. [P33316-2]
    PIRiA46256.
    G02777.
    RefSeqiNP_001020419.1. NM_001025248.1. [P33316-3]
    NP_001020420.1. NM_001025249.1.
    NP_001939.1. NM_001948.3. [P33316-2]
    UniGeneiHs.527980.

    Genome annotation databases

    EnsembliENST00000331200; ENSP00000370376; ENSG00000128951. [P33316-3]
    ENST00000455976; ENSP00000405160; ENSG00000128951. [P33316-2]
    ENST00000558813; ENSP00000453717; ENSG00000128951.
    GeneIDi1854.
    KEGGihsa:1854.
    UCSCiuc001zws.3. human. [P33316-3]
    uc001zww.3. human. [P33316-2]

    Polymorphism databases

    DMDMi347595814.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31930 mRNA. Translation: AAC50418.1 .
    U62891 mRNA. Translation: AAC51123.1 .
    AF018432
    , AF018429 , AF018430 , AF018431 Genomic DNA. Translation: AAB71393.1 . Frameshift.
    AF018432
    , AF018429 , AF018430 , AF018431 Genomic DNA. Translation: AAB71394.1 .
    U90223 mRNA. Translation: AAB94642.1 . Frameshift.
    U90224 Genomic DNA. Translation: AAB93866.1 . Frameshift.
    U90224 Genomic DNA. Translation: AAB93867.1 .
    AB049113 mRNA. Translation: BAB13724.1 .
    AY935242 Genomic DNA. Translation: AAX14045.1 .
    AK291515 mRNA. Translation: BAF84204.1 .
    AK312122 mRNA. Translation: BAG35058.1 .
    CR541720 mRNA. Translation: CAG46521.1 .
    CR541781 mRNA. Translation: CAG46580.1 .
    CH471082 Genomic DNA. Translation: EAW77350.1 .
    AK298464 mRNA. Translation: BAG60677.1 .
    BC033645 mRNA. Translation: AAH33645.1 .
    BC070339 mRNA. Translation: AAH70339.1 .
    BC110377 mRNA. Translation: AAI10378.1 .
    M89913 mRNA. Translation: AAA58444.1 .
    L11877 mRNA. Translation: AAA36801.1 .
    CCDSi CCDS32231.1. [P33316-3 ]
    CCDS45255.1. [P33316-2 ]
    PIRi A46256.
    G02777.
    RefSeqi NP_001020419.1. NM_001025248.1. [P33316-3 ]
    NP_001020420.1. NM_001025249.1.
    NP_001939.1. NM_001948.3. [P33316-2 ]
    UniGenei Hs.527980.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q5H X-ray 2.00 A/B/C 112-252 [» ]
    1Q5U X-ray 2.00 X/Y/Z 112-252 [» ]
    2HQU X-ray 2.20 A/B/C 94-252 [» ]
    3ARA X-ray 1.70 A/B/C 94-252 [» ]
    3ARN X-ray 1.80 A/B/C 94-252 [» ]
    3EHW X-ray 1.80 A/B/C/X/Y/Z 94-252 [» ]
    4MZ5 X-ray 2.10 A/C 97-109 [» ]
    4MZ6 X-ray 1.88 A/C 97-109 [» ]
    ProteinModelPortali P33316.
    SMRi P33316. Positions 112-236.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108187. 14 interactions.
    IntActi P33316. 21 interactions.
    MINTi MINT-1436411.

    Chemistry

    BindingDBi P33316.
    ChEMBLi CHEMBL5203.

    PTM databases

    PhosphoSitei P33316.

    Polymorphism databases

    DMDMi 347595814.

    Proteomic databases

    MaxQBi P33316.
    PaxDbi P33316.
    PeptideAtlasi P33316.
    PRIDEi P33316.

    Protocols and materials databases

    DNASUi 1854.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331200 ; ENSP00000370376 ; ENSG00000128951 . [P33316-3 ]
    ENST00000455976 ; ENSP00000405160 ; ENSG00000128951 . [P33316-2 ]
    ENST00000558813 ; ENSP00000453717 ; ENSG00000128951 .
    GeneIDi 1854.
    KEGGi hsa:1854.
    UCSCi uc001zws.3. human. [P33316-3 ]
    uc001zww.3. human. [P33316-2 ]

    Organism-specific databases

    CTDi 1854.
    GeneCardsi GC15P048623.
    HGNCi HGNC:3078. DUT.
    HPAi HPA054422.
    MIMi 601266. gene.
    neXtProti NX_P33316.
    PharmGKBi PA151.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0756.
    KOi K01520.
    OMAi MIEDENE.
    PhylomeDBi P33316.
    TreeFami TF105416.

    Enzyme and pathway databases

    UniPathwayi UPA00610 ; UER00666 .
    BioCyci MetaCyc:HS05235-MONOMER.
    BRENDAi 3.6.1.23. 2681.
    Reactomei REACT_21376. Pyrimidine biosynthesis.
    SABIO-RK P33316.

    Miscellaneous databases

    EvolutionaryTracei P33316.
    GeneWikii DUT_(gene).
    GenomeRNAii 1854.
    NextBioi 7591.
    PROi P33316.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P33316.
    Bgeei P33316.
    CleanExi HS_DUT.
    Genevestigatori P33316.

    Family and domain databases

    Gene3Di 2.70.40.10. 1 hit.
    InterProi IPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    [Graphical view ]
    Pfami PF00692. dUTPase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51283. SSF51283. 1 hit.
    TIGRFAMsi TIGR00576. dut. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of distinct nuclear and mitochondrial forms of human deoxyuridine triphosphate nucleotidohydrolase."
      Ladner R.D., McNulty D.E., Carr S.A., Roberts G.D., Caradonna S.J.
      J. Biol. Chem. 271:7745-7751(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 70-93 (ISOFORM 3), PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN SEQUENCE OF 94-115; 119-128; 133-151; 156-169; 180-206 AND 217-241 (ISOFORMS 2/3), CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 2), SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    2. "Assignment of the human dUTPase gene (DUT) to chromosome 15q15-q21. 1 by fluorescence in situ hybridization."
      Cohen D., Heng H.H.Q., Shi X.-M., McIntosh E.M., Tsui L.-C., Pearlman R.E.
      Genomics 40:213-215(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Human genomic nuclear and mitochondria dUTPase gene."
      Pearlman R.E.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 3).
    4. "The human dUTPase gene encodes both nuclear and mitochondrial isoforms. Differential expression of the isoforms and characterization of a cDNA encoding the mitochondrial species."
      Ladner R.D., Caradonna S.J.
      J. Biol. Chem. 272:19072-19080(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139 (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Lung fibroblast.
    5. "Unknown transcriptional variant of nuclear dUTPase in human osteosarcoma."
      Chano T., Okabe H., Baldini N., Lapucci C., Scotlandi K., Serra M., Saeki Y.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    6. "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] (ISOFORMS 2 AND 3).
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    8. NIEHS SNPs program
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-100.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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 2 AND 3).
      Tissue: Brain, Eye and Urinary bladder.
    11. "Human dUTP pyrophosphatase: cDNA sequence and potential biological importance of the enzyme."
      McIntosh E.M., Ager D.D., Gadsden M.H., Haynes R.H.
      Proc. Natl. Acad. Sci. U.S.A. 89:8020-8024(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 112-252.
    12. Erratum
      McIntosh E.M., Ager D.D., Gadsden M.H., Haynes R.H.
      Proc. Natl. Acad. Sci. U.S.A. 90:4328-4328(1993)
    13. "Maturation stage and proliferation-dependent expression of dUTPase in human T cells."
      Strahler J.R., Zhu X.-X., Wang Y.K., Hora N., Andrews P.C., Roseman N.A., Neel J.V., Turka L., Hanash S.M.
      Proc. Natl. Acad. Sci. U.S.A. 90:4991-4995(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 112-252, PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION.
      Tissue: Lymphocyte.
    14. "Identification of a consensus cyclin-dependent kinase phosphorylation site unique to the nuclear form of human deoxyuridine triphosphate nucleotidohydrolase."
      Ladner R.D., Carr S.A., Huddleston M.J., McNulty D.E., Caradonna S.J.
      J. Biol. Chem. 271:7752-7757(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PHOSPHORYLATION AT SER-11 (ISOFORM 2), MUTAGENESIS OF SER-99, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits."
      Mol C.D., Harris J.M., McIntosh E.M., Tainer J.A.
      Structure 4:1077-1092(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 112-252 IN COMPLEX WITH SUBSTRATE AND MAGNESIUM IONS, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    22. "Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase."
      Varga B., Barabas O., Kovari J., Toth J., Hunyadi-Gulyas E., Klement E., Medzihradszky K.F., Toelgyesi F., Fidy J., Vertessy B.G.
      FEBS Lett. 581:4783-4788(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 89-252 (ISOFORM 2) IN COMPLEX WITH SUBSTRATE ANALOG AND MAGNESIUM IONS, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.

    Entry informationi

    Entry nameiDUT_HUMAN
    AccessioniPrimary (citable) accession number: P33316
    Secondary accession number(s): A8K650
    , B4DPR5, O14785, Q16708, Q16860, Q6FHN1, Q6NSA3, Q96Q81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 154 of the entry and version 4 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

    Miscellaneous

    Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3