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Protein

dCTP pyrophosphatase 1

Gene

Dctpp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for modified dCTP. Activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). Does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. May protect DNA or RNA against the incorporation of non-canonical nucleotide triphosphates. May protect cells against inappropriate methylation of CpG islands by DNA methyltransferases.2 Publications

Catalytic activityi

dCTP + H2O = dCMP + diphosphate.2 Publications

Cofactori

Mg2+1 PublicationNote: Probably binds two or three Mg2+ ions per subunit.1 Publication

Enzyme regulationi

Inhibited by divalent calcium or cadmium ions.

Kineticsi

  1. KM=0.16 mM for 5-methyl-dCTP (at pH 9.0)2 Publications
  2. KM=44 µM for dCTP (at pH 8.0)2 Publications
  3. KM=118 µM for dATP (at pH 8.0)2 Publications
  4. KM=407 µM for dTTP (at pH 8.0)2 Publications
  5. KM=529 µM for CTP (at pH 8.0)2 Publications
  6. KM=3.9 µM for 5-iodo-dCTP (at pH 8.0)2 Publications
  7. KM=21.7 µM for 5-bromo-dCTP (at pH 8.0)2 Publications
  8. KM=48.5 µM for 5-methyl-dCTP (at pH 8.0)2 Publications
  9. KM=50 µM for 5-chloro-dCTP (at pH 8.0)2 Publications

    pH dependencei

    Optimum pH is 9-9.5.2 Publications

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei38 – 381Substrate
    Metal bindingi63 – 631MagnesiumCurated
    Metal bindingi66 – 661MagnesiumCurated
    Binding sitei73 – 731Substrate
    Metal bindingi95 – 951MagnesiumCurated
    Metal bindingi98 – 981MagnesiumCurated
    Binding sitei102 – 1021Substrate

    GO - Molecular functioni

    • dCTP diphosphatase activity Source: Reactome
    • identical protein binding Source: MGI
    • magnesium ion binding Source: UniProtKB
    • nucleoside-triphosphate diphosphatase activity Source: UniProtKB
    • pyrimidine deoxyribonucleotide binding Source: MGI
    • pyrophosphatase activity Source: MGI

    GO - Biological processi

    • nucleoside triphosphate catabolic process Source: UniProtKB
    • protein homotetramerization Source: MGI
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17900.
    BRENDAi3.6.1.12. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    dCTP pyrophosphatase 1 (EC:3.6.1.12)
    Alternative name(s):
    Deoxycytidine-triphosphatase 1
    Short name:
    dCTPase 1
    RS21-C6
    XTP3-transactivated gene A protein homolog
    Gene namesi
    Name:Dctpp1
    Synonyms:Tdrg-TL1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 7

    Organism-specific databases

    MGIiMGI:1913672. Dctpp1.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi38 – 381H → A: Reduces affinity for substrate and catalytic activity by about 50%. 1 Publication
    Mutagenesisi47 – 471W → I: Reduces affinity for substrate and catalytic activity by about 50%. 1 Publication
    Mutagenesisi63 – 631E → Q: Loss of activity. 1 Publication
    Mutagenesisi66 – 661E → Q: Loss of activity. 1 Publication
    Mutagenesisi73 – 731W → I: Reduces affinity for substrate and catalytic activity by about 50%. 1 Publication
    Mutagenesisi95 – 951E → Q: Loss of activity. 1 Publication
    Mutagenesisi98 – 981D → N: Loss of activity. 1 Publication
    Mutagenesisi102 – 1021Y → I: Reduces affinity for substrate and catalytic activity by about 50%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedBy similarity
    Chaini2 – 170169dCTP pyrophosphatase 1PRO_0000291770Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei2 – 21PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ9QY93.
    MaxQBiQ9QY93.
    PaxDbiQ9QY93.
    PRIDEiQ9QY93.

    PTM databases

    PhosphoSiteiQ9QY93.
    SwissPalmiQ9QY93.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in heart, liver, skeletal muscle, cerebellum, brain, and salivary gland.1 Publication

    Gene expression databases

    BgeeiQ9QY93.
    CleanExiMM_2410015N17RIK.
    GenevisibleiQ9QY93. MM.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000047845.

    Structurei

    Secondary structure

    1
    170
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 4313Combined sources
    Turni44 – 463Combined sources
    Helixi48 – 503Combined sources
    Helixi53 – 7220Combined sources
    Beta strandi76 – 783Combined sources
    Helixi81 – 833Combined sources
    Helixi86 – 10924Combined sources
    Helixi114 – 1196Combined sources
    Turni120 – 1223Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A3QX-ray2.32A/B1-170[»]
    2OIEX-ray2.20A/B/C/D21-126[»]
    2OIGX-ray3.30A/B/C/D21-126[»]
    2Q4PX-ray2.32A/B1-170[»]
    ProteinModelPortaliQ9QY93.
    SMRiQ9QY93. Positions 21-122.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QY93.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati29 – 7547EARAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 515Substrate binding

    Sequence similaritiesi

    Contains 1 EAR repeat.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG410IXWQ. Eukaryota.
    ENOG4111PYX. LUCA.
    GeneTreeiENSGT00390000017709.
    HOGENOMiHOG000056700.
    InParanoidiQ9QY93.
    KOiK16904.
    OMAiEQFHQPR.
    OrthoDBiEOG70S774.
    PhylomeDBiQ9QY93.
    TreeFamiTF300237.

    Family and domain databases

    InterProiIPR009039. EAR.
    IPR025984. MazG-like.
    [Graphical view]
    PfamiPF12643. MazG-like. 1 hit.
    [Graphical view]
    PROSITEiPS50912. EAR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9QY93-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTAGDGERG TVGQEDSAAA RPFRFSPEPT LEDIRRLHAE FAAERDWEQF
    60 70 80 90 100
    HQPRNLLLAL VGEVGELAEL FQWKSDTEPG PQAWPPKERA ALQEELSDVL
    110 120 130 140 150
    IYLVALAARC HVDLPQAVIS KMDTNRQRYP VHLSRGSACK YTDLPRGTIS
    160 170
    ENQAVGAGDP ASELRDQAST
    Length:170
    Mass (Da):18,795
    Last modified:May 1, 2000 - v1
    Checksum:iA20ECDA7857446A3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF110764 mRNA. Translation: AAF15970.1.
    AK003643 mRNA. Translation: BAB22909.1.
    AK010508 mRNA. Translation: BAB26992.1.
    AK010606 mRNA. Translation: BAB27056.1.
    BC004623 mRNA. Translation: AAH04623.1.
    CCDSiCCDS21862.1.
    RefSeqiNP_075692.1. NM_023203.1.
    UniGeneiMm.29898.

    Genome annotation databases

    EnsembliENSMUST00000035276; ENSMUSP00000047845; ENSMUSG00000042462.
    GeneIDi66422.
    KEGGimmu:66422.
    UCSCiuc009juw.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF110764 mRNA. Translation: AAF15970.1.
    AK003643 mRNA. Translation: BAB22909.1.
    AK010508 mRNA. Translation: BAB26992.1.
    AK010606 mRNA. Translation: BAB27056.1.
    BC004623 mRNA. Translation: AAH04623.1.
    CCDSiCCDS21862.1.
    RefSeqiNP_075692.1. NM_023203.1.
    UniGeneiMm.29898.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A3QX-ray2.32A/B1-170[»]
    2OIEX-ray2.20A/B/C/D21-126[»]
    2OIGX-ray3.30A/B/C/D21-126[»]
    2Q4PX-ray2.32A/B1-170[»]
    ProteinModelPortaliQ9QY93.
    SMRiQ9QY93. Positions 21-122.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000047845.

    PTM databases

    PhosphoSiteiQ9QY93.
    SwissPalmiQ9QY93.

    Proteomic databases

    EPDiQ9QY93.
    MaxQBiQ9QY93.
    PaxDbiQ9QY93.
    PRIDEiQ9QY93.

    Protocols and materials databases

    DNASUi66422.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000035276; ENSMUSP00000047845; ENSMUSG00000042462.
    GeneIDi66422.
    KEGGimmu:66422.
    UCSCiuc009juw.2. mouse.

    Organism-specific databases

    CTDi79077.
    MGIiMGI:1913672. Dctpp1.

    Phylogenomic databases

    eggNOGiENOG410IXWQ. Eukaryota.
    ENOG4111PYX. LUCA.
    GeneTreeiENSGT00390000017709.
    HOGENOMiHOG000056700.
    InParanoidiQ9QY93.
    KOiK16904.
    OMAiEQFHQPR.
    OrthoDBiEOG70S774.
    PhylomeDBiQ9QY93.
    TreeFamiTF300237.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17900.
    BRENDAi3.6.1.12. 3474.

    Miscellaneous databases

    EvolutionaryTraceiQ9QY93.
    NextBioi321647.
    PROiQ9QY93.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9QY93.
    CleanExiMM_2410015N17RIK.
    GenevisibleiQ9QY93. MM.

    Family and domain databases

    InterProiIPR009039. EAR.
    IPR025984. MazG-like.
    [Graphical view]
    PfamiPF12643. MazG-like. 1 hit.
    [Graphical view]
    PROSITEiPS50912. EAR. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "RS21-C6: a novel gene encoding a molecule relavent to TCR and CD3 expression of pre-T cells."
      Wang H., Chen W.F., Li Y., Jin C.G., Wang Y., Yu Q., Qian X.P.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/cJ.
    2. "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.
    3. "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: Mammary tumor.
    4. "Mouse RS21-C6 is a mammalian 2'-deoxycytidine 5'-triphosphate pyrophosphohydrolase that prefers 5-iodocytosine."
      Nonaka M., Tsuchimoto D., Sakumi K., Nakabeppu Y.
      FEBS J. 276:1654-1666(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
    6. "X-ray structure of protein from Mus musculus mm.29898."
      Center for eukaryotic structural genomics (CESG)
      Submitted (JUL-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS), SUBUNIT.
    7. "Crystal structure of RS21-C6, involved in nucleoside triphosphate pyrophosphohydrolysis."
      Wu B., Liu Y., Zhao Q., Liao S., Zhang J., Bartlam M., Chen W., Rao Z.
      J. Mol. Biol. 367:1405-1412(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-126 IN COMPLEX WITH 5-METHYL DCTP, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-38; TRP-47; GLU-63; GLU-66; TRP-73; GLU-95; ASP-98 AND TYR-102.
    8. "Ensemble refinement of protein crystal structures: validation and application."
      Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.
      Structure 15:1040-1052(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS).

    Entry informationi

    Entry nameiDCTP1_MOUSE
    AccessioniPrimary (citable) accession number: Q9QY93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: May 1, 2000
    Last modified: May 11, 2016
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.