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Q9H773

- DCTP1_HUMAN

UniProt

Q9H773 - DCTP1_HUMAN

Protein

dCTP pyrophosphatase 1

Gene

DCTPP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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 By similarity.By similarity

    Catalytic activityi

    dCTP + H2O = dCMP + diphosphate.

    Cofactori

    Magnesium. Probably binds two or three magnesium ions per subunit By similarity.By similarity

    Sites

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

    GO - Molecular functioni

    1. dCTP diphosphatase activity Source: UniProtKB-EC
    2. magnesium ion binding Source: UniProtKB
    3. nucleoside-triphosphate diphosphatase activity Source: UniProtKB
    4. pyrimidine deoxyribonucleotide binding Source: Ensembl

    GO - Biological processi

    1. nucleoside triphosphate catabolic process Source: UniProtKB
    2. protein homotetramerization Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    dCTP pyrophosphatase 1 (EC:3.6.1.12)
    Alternative name(s):
    Deoxycytidine-triphosphatase 1
    Short name:
    dCTPase 1
    RS21C6
    XTP3-transactivated gene A protein
    Gene namesi
    Name:DCTPP1
    Synonyms:XTP3TPA
    ORF Names:CDA03
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:28777. DCTPP1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164718733.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 170169dCTP pyrophosphatase 1PRO_0000291769Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei12 – 121Phosphothreonine1 Publication
    Modified residuei85 – 851Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H773.
    PaxDbiQ9H773.
    PeptideAtlasiQ9H773.
    PRIDEiQ9H773.

    PTM databases

    PhosphoSiteiQ9H773.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H773.
    BgeeiQ9H773.
    GenevestigatoriQ9H773.

    Organism-specific databases

    HPAiHPA002832.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi122527. 21 interactions.
    IntActiQ9H773. 4 interactions.
    STRINGi9606.ENSP00000322524.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H773.
    SMRiQ9H773. Positions 23-123.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

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

    Sequence similaritiesi

    Contains 1 EAR repeat.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG131091.
    HOGENOMiHOG000056700.
    InParanoidiQ9H773.
    KOiK16904.
    OMAiGPQAWPP.
    OrthoDBiEOG70S774.
    PhylomeDBiQ9H773.
    TreeFamiTF300237.

    Family and domain databases

    InterProiIPR009039. EAR.
    IPR004518. MazG_cat.
    [Graphical view]
    PfamiPF03819. MazG. 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.

    Q9H773-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVAGGEIRG DTGGEDTAAP GRFSFSPEPT LEDIRRLHAE FAAERDWEQF    50
    HQPRNLLLAL VGEVGELAEL FQWKTDGEPG PQGWSPRERA ALQEELSDVL 100
    IYLVALAARC RVDLPLAVLS KMDINRRRYP AHLARSSSRK YTELPHGAIS 150
    EDQAVGPADI PCDSTGQTST 170
    Length:170
    Mass (Da):18,681
    Last modified:March 1, 2001 - v1
    Checksum:i23BC932D5461320B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY453409 mRNA. Translation: AAR26724.1.
    AF212242 mRNA. Translation: AAK14927.1.
    AF210430 mRNA. Translation: AAK48422.1.
    CR457335 mRNA. Translation: CAG33616.1.
    AK024843 mRNA. Translation: BAB15025.1.
    BC001344 mRNA. Translation: AAH01344.1.
    CCDSiCCDS10680.1.
    RefSeqiNP_077001.1. NM_024096.1.
    UniGeneiHs.632191.

    Genome annotation databases

    EnsembliENST00000319285; ENSP00000322524; ENSG00000179958.
    GeneIDi79077.
    KEGGihsa:79077.
    UCSCiuc002dyf.3. human.

    Polymorphism databases

    DMDMi74733624.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY453409 mRNA. Translation: AAR26724.1 .
    AF212242 mRNA. Translation: AAK14927.1 .
    AF210430 mRNA. Translation: AAK48422.1 .
    CR457335 mRNA. Translation: CAG33616.1 .
    AK024843 mRNA. Translation: BAB15025.1 .
    BC001344 mRNA. Translation: AAH01344.1 .
    CCDSi CCDS10680.1.
    RefSeqi NP_077001.1. NM_024096.1.
    UniGenei Hs.632191.

    3D structure databases

    ProteinModelPortali Q9H773.
    SMRi Q9H773. Positions 23-123.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122527. 21 interactions.
    IntActi Q9H773. 4 interactions.
    STRINGi 9606.ENSP00000322524.

    Chemistry

    BindingDBi Q9H773.

    PTM databases

    PhosphoSitei Q9H773.

    Polymorphism databases

    DMDMi 74733624.

    Proteomic databases

    MaxQBi Q9H773.
    PaxDbi Q9H773.
    PeptideAtlasi Q9H773.
    PRIDEi Q9H773.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319285 ; ENSP00000322524 ; ENSG00000179958 .
    GeneIDi 79077.
    KEGGi hsa:79077.
    UCSCi uc002dyf.3. human.

    Organism-specific databases

    CTDi 79077.
    GeneCardsi GC16M030435.
    HGNCi HGNC:28777. DCTPP1.
    HPAi HPA002832.
    neXtProti NX_Q9H773.
    PharmGKBi PA164718733.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG131091.
    HOGENOMi HOG000056700.
    InParanoidi Q9H773.
    KOi K16904.
    OMAi GPQAWPP.
    OrthoDBi EOG70S774.
    PhylomeDBi Q9H773.
    TreeFami TF300237.

    Miscellaneous databases

    GeneWikii XTP3-transactivated_gene_A_protein.
    GenomeRNAii 79077.
    NextBioi 67876.
    PROi Q9H773.

    Gene expression databases

    ArrayExpressi Q9H773.
    Bgeei Q9H773.
    Genevestigatori Q9H773.

    Family and domain databases

    InterProi IPR009039. EAR.
    IPR004518. MazG_cat.
    [Graphical view ]
    Pfami PF03819. MazG. 1 hit.
    [Graphical view ]
    PROSITEi PS50912. EAR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Screening and cloning of the target genes transactivated by XTP3 using a suppression subtractive hybridization technique."
      Wang C., Cheng J., Lang Z., Wu Y., Yang Y., Zhang L., Ji D.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A novel gene expressed in human pheochromocytoma."
      Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pheochromocytoma.
    3. Zhang J., Chen W.F., Wang H.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
    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.
      , 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].
    6. "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].
      Tissue: Cervix.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-12 AND SER-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDCTP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H773
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3