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Protein

Deoxycytidine kinase

Gene

DCK

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

Functioni

Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents.2 Publications

Catalytic activityi

NTP + deoxycytidine = NDP + dCMP.4 Publications

Kineticsi

  1. KM=6.2 µM for deoxycytidine (dC)1 Publication
  2. KM=15.5 µM for cytarabine (araC)1 Publication
  3. KM=22 µM for gemcitabine (dC)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531Substrate
    Binding sitei86 – 861Substrate
    Binding sitei97 – 971Substrate
    Active sitei127 – 1271Proton acceptorSequence Analysis
    Binding sitei128 – 1281Substrate
    Binding sitei133 – 1331Substrate
    Binding sitei197 – 1971Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi28 – 369ATP
    Nucleotide bindingi188 – 1925ATP
    Nucleotide bindingi240 – 2423ATP

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • deoxycytidine kinase activity Source: UniProtKB
    • drug binding Source: UniProtKB
    • nucleoside kinase activity Source: Reactome
    • protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08100-MONOMER.
    BRENDAi2.7.1.74. 2681.
    ReactomeiREACT_1923. Purine salvage.
    REACT_655. Pyrimidine salvage reactions.
    SABIO-RKP27707.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxycytidine kinase (EC:2.7.1.74)
    Short name:
    dCK
    Gene namesi
    Name:DCK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:2704. DCK.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi100 – 1001A → V: Strongly increased catalytic efficiency towards deoxycytidine; when associated with M-104 and A-133. 1 Publication
    Mutagenesisi104 – 1041R → L: Strongly increased catalytic efficiency towards deoxythymidine; when associated with A-133. 3 Publications
    Mutagenesisi104 – 1041R → M: Strongly increased catalytic efficiency towards deoxycytidine; when associated with V-100 and A-133. 3 Publications
    Mutagenesisi133 – 1331D → A: Strongly increased catalytic efficiency towards deoxycytidine; when associated with V-100 and M-104. Strongly increased catalytic efficiency towards deoxythymidine; when associated with L-104. 3 Publications

    Organism-specific databases

    PharmGKBiPA137.

    Chemistry

    DrugBankiDB00242. Cladribine.
    DB00631. Clofarabine.
    DB00987. Cytarabine.
    DB01262. Decitabine.
    DB00879. Emtricitabine.
    DB01073. Fludarabine.
    DB00441. Gemcitabine.
    DB00709. Lamivudine.
    DB01280. Nelarabine.
    DB00642. Pemetrexed.
    DB00943. Zalcitabine.

    Polymorphism and mutation databases

    BioMutaiDCK.
    DMDMi118447.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 260260Deoxycytidine kinasePRO_0000175090Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine; by CK11 Publication
    Modified residuei15 – 151Phosphoserine; by CK11 Publication
    Modified residuei72 – 721Phosphothreonine; by CK11 Publication
    Modified residuei74 – 741Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated and activated in vitro upon phosphorylation at Ser-74 by CSNK1D/CK1.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP27707.
    PaxDbiP27707.
    PeptideAtlasiP27707.
    PRIDEiP27707.

    PTM databases

    PhosphoSiteiP27707.

    Expressioni

    Gene expression databases

    BgeeiP27707.
    CleanExiHS_DCK.
    ExpressionAtlasiP27707. baseline and differential.
    GenevisibleiP27707. HS.

    Organism-specific databases

    HPAiHPA059609.
    HPA062773.

    Interactioni

    Subunit structurei

    Homodimer.5 Publications

    Protein-protein interaction databases

    BioGridi108001. 22 interactions.
    IntActiP27707. 5 interactions.
    MINTiMINT-1387532.
    STRINGi9606.ENSP00000286648.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 276Combined sources
    Helixi34 – 385Combined sources
    Turni39 – 413Combined sources
    Helixi42 – 443Combined sources
    Beta strandi48 – 514Combined sources
    Helixi55 – 584Combined sources
    Beta strandi61 – 633Combined sources
    Helixi69 – 724Combined sources
    Helixi73 – 775Combined sources
    Helixi81 – 877Combined sources
    Helixi89 – 11224Combined sources
    Helixi115 – 1184Combined sources
    Beta strandi119 – 1213Combined sources
    Beta strandi123 – 1286Combined sources
    Helixi130 – 1356Combined sources
    Helixi137 – 1437Combined sources
    Helixi149 – 17022Combined sources
    Beta strandi173 – 1797Combined sources
    Helixi182 – 19211Combined sources
    Helixi195 – 1973Combined sources
    Helixi202 – 21615Combined sources
    Helixi226 – 2305Combined sources
    Beta strandi233 – 2375Combined sources
    Helixi242 – 25817Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P5ZX-ray1.60B1-260[»]
    1P60X-ray1.96A/B1-260[»]
    1P61X-ray2.21B1-260[»]
    1P62X-ray1.90B1-260[»]
    2A2ZX-ray3.02A/B/C/D1-260[»]
    2A30X-ray3.02A/B/C/D1-260[»]
    2A7QX-ray2.55A1-260[»]
    2NO0X-ray1.80A/B1-260[»]
    2NO1X-ray1.91A/B1-260[»]
    2NO6X-ray1.90A/B1-260[»]
    2NO7X-ray1.70A/B1-260[»]
    2NO9X-ray2.15A/B1-260[»]
    2NOAX-ray1.80A/B1-260[»]
    2QRNX-ray3.40A/B/C/D1-260[»]
    2QROX-ray3.45A/B/C/D1-260[»]
    2ZI3X-ray2.30A/B1-260[»]
    2ZI4X-ray2.10A1-260[»]
    2ZI5X-ray1.77A/B/C/D1-260[»]
    2ZI6X-ray1.77A/B/C/D1-260[»]
    2ZI7X-ray1.97A/B1-260[»]
    2ZI9X-ray2.51A/B1-260[»]
    2ZIAX-ray1.80A/B1-260[»]
    3HP1X-ray2.31A1-260[»]
    3IPXX-ray2.00A20-260[»]
    3IPYX-ray2.54A/B20-260[»]
    3KFXX-ray1.96A/B1-260[»]
    3MJRX-ray2.10A/B/C/D1-260[»]
    3QEJX-ray2.49A/B1-260[»]
    3QENX-ray2.00A/B1-260[»]
    3QEOX-ray1.90A/B1-260[»]
    4JLJX-ray2.00A/B1-260[»]
    4JLKX-ray1.89A/B1-260[»]
    4JLMX-ray2.18A/B1-260[»]
    4JLNX-ray2.15A/B1-260[»]
    4KCGX-ray2.09A/B1-260[»]
    4L5BX-ray1.94A/B1-260[»]
    4Q18X-ray2.00A/B1-260[»]
    4Q19X-ray2.09A/B1-260[»]
    4Q1AX-ray1.90A/B1-260[»]
    4Q1BX-ray2.15A/B1-260[»]
    4Q1CX-ray2.00A/B1-260[»]
    4Q1DX-ray2.00A/B1-260[»]
    4Q1EX-ray1.85A/B1-260[»]
    4Q1FX-ray2.10A/B1-260[»]
    ProteinModelPortaliP27707.
    SMRiP27707. Positions 19-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27707.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DCK/DGK family.Curated

    Phylogenomic databases

    eggNOGiCOG1428.
    GeneTreeiENSGT00510000046588.
    HOGENOMiHOG000290165.
    HOVERGENiHBG006216.
    InParanoidiP27707.
    KOiK00893.
    PhylomeDBiP27707.
    TreeFamiTF324413.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR002624. DNK.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10513. PTHR10513. 1 hit.
    PfamiPF01712. dNK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000705. DNK. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P27707-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATPPKRSCP SFSASSEGTR IKKISIEGNI AAGKSTFVNI LKQLCEDWEV
    60 70 80 90 100
    VPEPVARWCN VQSTQDEFEE LTMSQKNGGN VLQMMYEKPE RWSFTFQTYA
    110 120 130 140 150
    CLSRIRAQLA SLNGKLKDAE KPVLFFERSV YSDRYIFASN LYESECMNET
    160 170 180 190 200
    EWTIYQDWHD WMNNQFGQSL ELDGIIYLQA TPETCLHRIY LRGRNEEQGI
    210 220 230 240 250
    PLEYLEKLHY KHESWLLHRT LKTNFDYLQE VPILTLDVNE DFKDKYESLV
    260
    EKVKEFLSTL
    Length:260
    Mass (Da):30,519
    Last modified:August 1, 1992 - v1
    Checksum:i626B9D2D6BED8DBC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti122 – 1221P → S in AAV38744 (Ref. 4) Curated
    Sequence conflicti122 – 1221P → S in AAV38745 (Ref. 4) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M60527 mRNA. Translation: AAA35752.1.
    AK313523 mRNA. Translation: BAG36303.1.
    CR536527 mRNA. Translation: CAG38764.1.
    CR541876 mRNA. Translation: CAG46674.1.
    BT019941 mRNA. Translation: AAV38744.1.
    BT019942 mRNA. Translation: AAV38745.1.
    CH471057 Genomic DNA. Translation: EAX05637.1.
    BC103764 mRNA. Translation: AAI03765.1.
    BC114617 mRNA. Translation: AAI14618.1.
    CCDSiCCDS3548.1.
    PIRiA38585.
    RefSeqiNP_000779.1. NM_000788.2.
    UniGeneiHs.709.

    Genome annotation databases

    EnsembliENST00000286648; ENSP00000286648; ENSG00000156136.
    GeneIDi1633.
    KEGGihsa:1633.
    UCSCiuc003hfx.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M60527 mRNA. Translation: AAA35752.1.
    AK313523 mRNA. Translation: BAG36303.1.
    CR536527 mRNA. Translation: CAG38764.1.
    CR541876 mRNA. Translation: CAG46674.1.
    BT019941 mRNA. Translation: AAV38744.1.
    BT019942 mRNA. Translation: AAV38745.1.
    CH471057 Genomic DNA. Translation: EAX05637.1.
    BC103764 mRNA. Translation: AAI03765.1.
    BC114617 mRNA. Translation: AAI14618.1.
    CCDSiCCDS3548.1.
    PIRiA38585.
    RefSeqiNP_000779.1. NM_000788.2.
    UniGeneiHs.709.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P5ZX-ray1.60B1-260[»]
    1P60X-ray1.96A/B1-260[»]
    1P61X-ray2.21B1-260[»]
    1P62X-ray1.90B1-260[»]
    2A2ZX-ray3.02A/B/C/D1-260[»]
    2A30X-ray3.02A/B/C/D1-260[»]
    2A7QX-ray2.55A1-260[»]
    2NO0X-ray1.80A/B1-260[»]
    2NO1X-ray1.91A/B1-260[»]
    2NO6X-ray1.90A/B1-260[»]
    2NO7X-ray1.70A/B1-260[»]
    2NO9X-ray2.15A/B1-260[»]
    2NOAX-ray1.80A/B1-260[»]
    2QRNX-ray3.40A/B/C/D1-260[»]
    2QROX-ray3.45A/B/C/D1-260[»]
    2ZI3X-ray2.30A/B1-260[»]
    2ZI4X-ray2.10A1-260[»]
    2ZI5X-ray1.77A/B/C/D1-260[»]
    2ZI6X-ray1.77A/B/C/D1-260[»]
    2ZI7X-ray1.97A/B1-260[»]
    2ZI9X-ray2.51A/B1-260[»]
    2ZIAX-ray1.80A/B1-260[»]
    3HP1X-ray2.31A1-260[»]
    3IPXX-ray2.00A20-260[»]
    3IPYX-ray2.54A/B20-260[»]
    3KFXX-ray1.96A/B1-260[»]
    3MJRX-ray2.10A/B/C/D1-260[»]
    3QEJX-ray2.49A/B1-260[»]
    3QENX-ray2.00A/B1-260[»]
    3QEOX-ray1.90A/B1-260[»]
    4JLJX-ray2.00A/B1-260[»]
    4JLKX-ray1.89A/B1-260[»]
    4JLMX-ray2.18A/B1-260[»]
    4JLNX-ray2.15A/B1-260[»]
    4KCGX-ray2.09A/B1-260[»]
    4L5BX-ray1.94A/B1-260[»]
    4Q18X-ray2.00A/B1-260[»]
    4Q19X-ray2.09A/B1-260[»]
    4Q1AX-ray1.90A/B1-260[»]
    4Q1BX-ray2.15A/B1-260[»]
    4Q1CX-ray2.00A/B1-260[»]
    4Q1DX-ray2.00A/B1-260[»]
    4Q1EX-ray1.85A/B1-260[»]
    4Q1FX-ray2.10A/B1-260[»]
    ProteinModelPortaliP27707.
    SMRiP27707. Positions 19-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108001. 22 interactions.
    IntActiP27707. 5 interactions.
    MINTiMINT-1387532.
    STRINGi9606.ENSP00000286648.

    Chemistry

    BindingDBiP27707.
    ChEMBLiCHEMBL2447.
    DrugBankiDB00242. Cladribine.
    DB00631. Clofarabine.
    DB00987. Cytarabine.
    DB01262. Decitabine.
    DB00879. Emtricitabine.
    DB01073. Fludarabine.
    DB00441. Gemcitabine.
    DB00709. Lamivudine.
    DB01280. Nelarabine.
    DB00642. Pemetrexed.
    DB00943. Zalcitabine.

    PTM databases

    PhosphoSiteiP27707.

    Polymorphism and mutation databases

    BioMutaiDCK.
    DMDMi118447.

    Proteomic databases

    MaxQBiP27707.
    PaxDbiP27707.
    PeptideAtlasiP27707.
    PRIDEiP27707.

    Protocols and materials databases

    DNASUi1633.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000286648; ENSP00000286648; ENSG00000156136.
    GeneIDi1633.
    KEGGihsa:1633.
    UCSCiuc003hfx.3. human.

    Organism-specific databases

    CTDi1633.
    GeneCardsiGC04P071816.
    HGNCiHGNC:2704. DCK.
    HPAiHPA059609.
    HPA062773.
    MIMi125450. gene.
    neXtProtiNX_P27707.
    PharmGKBiPA137.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1428.
    GeneTreeiENSGT00510000046588.
    HOGENOMiHOG000290165.
    HOVERGENiHBG006216.
    InParanoidiP27707.
    KOiK00893.
    PhylomeDBiP27707.
    TreeFamiTF324413.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08100-MONOMER.
    BRENDAi2.7.1.74. 2681.
    ReactomeiREACT_1923. Purine salvage.
    REACT_655. Pyrimidine salvage reactions.
    SABIO-RKP27707.

    Miscellaneous databases

    ChiTaRSiDCK. human.
    EvolutionaryTraceiP27707.
    GeneWikiiDeoxycytidine_kinase.
    GenomeRNAii1633.
    NextBioi6698.
    PROiP27707.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP27707.
    CleanExiHS_DCK.
    ExpressionAtlasiP27707. baseline and differential.
    GenevisibleiP27707. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR002624. DNK.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10513. PTHR10513. 1 hit.
    PfamiPF01712. dNK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000705. DNK. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 58-70; 119-127 AND 189-192.
    2. "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].
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Uterus.
    7. "Characterization of human deoxycytidine kinase. Correlation with cDNA sequences."
      Eriksson S., Cederlund E., Bergman T., Joernvall H., Bohman C.
      FEBS Lett. 280:363-366(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
    8. "Human deoxycytidine kinase is located in the cell nucleus."
      Johansson M., Brismar S., Karlsson A.
      Proc. Natl. Acad. Sci. U.S.A. 94:11941-11945(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Casein kinase 1delta activates human recombinant deoxycytidine kinase by Ser-74 phosphorylation, but is not involved in the in vivo regulation of its activity."
      Smal C., Vertommen D., Amsailale R., Arts A., Degand H., Morsomme P., Rider M.H., Neste E.V., Bontemps F.
      Arch. Biochem. Biophys. 502:44-52(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11; SER-15; THR-72 AND SER-74 BY CSNK1D/CK1.
    14. "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-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Structure of human dCK suggests strategies to improve anticancer and antiviral therapy."
      Sabini E., Ort S., Monnerjahn C., Konrad M., Lavie A.
      Nat. Struct. Biol. 10:513-519(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH ADP; DEOXYCYTIDINE; ARAC AND GEMCITABINE, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-100; ARG-104 AND ASP-133.
    17. "The structure of human deoxycytidine kinase in complex with clofarabine reveals key interactions for prodrug activation."
      Zhang Y., Secrist J.A. III, Ealick S.E.
      Acta Crystallogr. D 62:133-139(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH ADP AND CLOFARABINE, SUBUNIT.
    18. "Nonenantioselectivity property of human deoxycytidine kinase explained by structures of the enzyme in complex with L- and D-nucleosides."
      Sabini E., Hazra S., Konrad M., Lavie A.
      J. Med. Chem. 50:3004-3014(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH ADP; D-DEOXYCYTIDINE; L-DEOXYCYTIDINE AND EMTRICITABINE.
    19. "Structural basis for substrate promiscuity of dCK."
      Sabini E., Hazra S., Ort S., Konrad M., Lavie A.
      J. Mol. Biol. 378:607-621(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEXES WITH D-DEOXYADENOSINE; L-DEOXYADENOSINE; ADP AND UDP, CATALYTIC ACTIVITY, FUNCTION.
    20. "Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase."
      Hazra S., Sabini E., Ort S., Konrad M., Lavie A.
      Biochemistry 48:1256-1263(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-104 AND ASP-133.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-260 IN COMPLEX WITH SYNTHETIC INHIBITOR.
    22. "Structural and kinetic characterization of human deoxycytidine kinase variants able to phosphorylate 5-substituted deoxycytidine and thymidine analogues."
      Hazra S., Ort S., Konrad M., Lavie A.
      Biochemistry 49:6784-6790(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH ADP AND 5-METHYL-DEOXYCYTIDINE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-104 AND ASP-133.
    23. "The sugar ring of the nucleoside is required for productive substrate positioning in the active site of human deoxycytidine kinase (dCK): implications for the development of dCK-activated acyclic guanine analogues."
      Hazra S., Konrad M., Lavie A.
      J. Med. Chem. 53:5792-5800(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ACYCLOVIR AND UDP.

    Entry informationi

    Entry nameiDCK_HUMAN
    AccessioniPrimary (citable) accession number: P27707
    Secondary accession number(s): B2R8V6, Q5TZY7, Q6FI11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: June 24, 2015
    This is version 145 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

    Caution

    Was shown to be phosphorylated and activated by CSNK1D/CK1 in vitro but probably not in vivo.1 Publication

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.