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P27707

- DCK_HUMAN

UniProt

P27707 - DCK_HUMAN

Protein

Deoxycytidine kinase

Gene

DCK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    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

    1. ATP binding Source: UniProtKB-KW
    2. deoxycytidine kinase activity Source: UniProtKB
    3. drug binding Source: UniProtKB
    4. nucleoside kinase activity Source: Reactome
    5. phosphotransferase activity, alcohol group as acceptor Source: InterPro
    6. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. deoxyribonucleoside monophosphate biosynthetic process Source: GOC
    2. nucleobase-containing small molecule metabolic process Source: Reactome
    3. nucleotide biosynthetic process Source: GOC
    4. purine-containing compound salvage Source: Reactome
    5. purine nucleobase metabolic process Source: Reactome
    6. pyrimidine nucleobase metabolic process Source: Reactome
    7. pyrimidine nucleoside salvage Source: Reactome
    8. pyrimidine nucleotide metabolic process Source: UniProtKB
    9. small molecule metabolic process Source: Reactome

    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: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:2704. DCK.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell

    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.

    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/CK1.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP27707.
    PaxDbiP27707.
    PeptideAtlasiP27707.
    PRIDEiP27707.

    PTM databases

    PhosphoSiteiP27707.

    Expressioni

    Gene expression databases

    ArrayExpressiP27707.
    BgeeiP27707.
    CleanExiHS_DCK.
    GenevestigatoriP27707.

    Interactioni

    Subunit structurei

    Homodimer.5 Publications

    Protein-protein interaction databases

    BioGridi108001. 21 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 – 276
    Helixi34 – 385
    Turni39 – 413
    Helixi42 – 443
    Beta strandi48 – 514
    Helixi55 – 584
    Beta strandi61 – 633
    Helixi69 – 724
    Helixi81 – 877
    Helixi89 – 11224
    Helixi115 – 1184
    Beta strandi119 – 1213
    Beta strandi123 – 1286
    Helixi130 – 1356
    Helixi137 – 1437
    Helixi149 – 17022
    Beta strandi173 – 1797
    Helixi182 – 19211
    Helixi195 – 1973
    Helixi202 – 21615
    Helixi226 – 2305
    Beta strandi233 – 2375
    Helixi242 – 25817

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliP27707.
    SMRiP27707. Positions 19-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27707.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DCK/DGK family.Curated

    Phylogenomic databases

    eggNOGiCOG1428.
    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

    MATPPKRSCP SFSASSEGTR IKKISIEGNI AAGKSTFVNI LKQLCEDWEV    50
    VPEPVARWCN VQSTQDEFEE LTMSQKNGGN VLQMMYEKPE RWSFTFQTYA 100
    CLSRIRAQLA SLNGKLKDAE KPVLFFERSV YSDRYIFASN LYESECMNET 150
    EWTIYQDWHD WMNNQFGQSL ELDGIIYLQA TPETCLHRIY LRGRNEEQGI 200
    PLEYLEKLHY KHESWLLHRT LKTNFDYLQE VPILTLDVNE DFKDKYESLV 250
    EKVKEFLSTL 260
    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. 1 PublicationCurated
    Sequence conflicti122 – 1221P → S in AAV38745. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi118447.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3548.1.
    PIRi A38585.
    RefSeqi NP_000779.1. NM_000788.2.
    UniGenei Hs.709.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P5Z X-ray 1.60 B 1-260 [» ]
    1P60 X-ray 1.96 A/B 1-260 [» ]
    1P61 X-ray 2.21 B 1-260 [» ]
    1P62 X-ray 1.90 B 1-260 [» ]
    2A2Z X-ray 3.02 A/B/C/D 1-260 [» ]
    2A30 X-ray 3.02 A/B/C/D 1-260 [» ]
    2A7Q X-ray 2.55 A 1-260 [» ]
    2NO0 X-ray 1.80 A/B 1-260 [» ]
    2NO1 X-ray 1.91 A/B 1-260 [» ]
    2NO6 X-ray 1.90 A/B 1-260 [» ]
    2NO7 X-ray 1.70 A/B 1-260 [» ]
    2NO9 X-ray 2.15 A/B 1-260 [» ]
    2NOA X-ray 1.80 A/B 1-260 [» ]
    2QRN X-ray 3.40 A/B/C/D 1-260 [» ]
    2QRO X-ray 3.45 A/B/C/D 1-260 [» ]
    2ZI3 X-ray 2.30 A/B 1-260 [» ]
    2ZI4 X-ray 2.10 A 1-260 [» ]
    2ZI5 X-ray 1.77 A/B/C/D 1-260 [» ]
    2ZI6 X-ray 1.77 A/B/C/D 1-260 [» ]
    2ZI7 X-ray 1.97 A/B 1-260 [» ]
    2ZI9 X-ray 2.51 A/B 1-260 [» ]
    2ZIA X-ray 1.80 A/B 1-260 [» ]
    3HP1 X-ray 2.31 A 1-260 [» ]
    3IPX X-ray 2.00 A 20-260 [» ]
    3IPY X-ray 2.54 A/B 20-260 [» ]
    3KFX X-ray 1.96 A/B 1-260 [» ]
    3MJR X-ray 2.10 A/B/C/D 1-260 [» ]
    3QEJ X-ray 2.49 A/B 1-260 [» ]
    3QEN X-ray 2.00 A/B 1-260 [» ]
    3QEO X-ray 1.90 A/B 1-260 [» ]
    4JLJ X-ray 2.00 A/B 1-260 [» ]
    4JLK X-ray 1.89 A/B 1-260 [» ]
    4JLM X-ray 2.18 A/B 1-260 [» ]
    4JLN X-ray 2.15 A/B 1-260 [» ]
    4KCG X-ray 2.09 A/B 1-260 [» ]
    4L5B X-ray 1.94 A/B 1-260 [» ]
    ProteinModelPortali P27707.
    SMRi P27707. Positions 19-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108001. 21 interactions.
    IntActi P27707. 5 interactions.
    MINTi MINT-1387532.
    STRINGi 9606.ENSP00000286648.

    Chemistry

    BindingDBi P27707.
    ChEMBLi CHEMBL2447.
    DrugBanki DB00242. Cladribine.
    DB00631. Clofarabine.
    DB01262. Decitabine.
    DB01073. Fludarabine.
    DB00441. Gemcitabine.
    DB00642. Pemetrexed.
    DB00943. Zalcitabine.

    PTM databases

    PhosphoSitei P27707.

    Polymorphism databases

    DMDMi 118447.

    Proteomic databases

    MaxQBi P27707.
    PaxDbi P27707.
    PeptideAtlasi P27707.
    PRIDEi P27707.

    Protocols and materials databases

    DNASUi 1633.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286648 ; ENSP00000286648 ; ENSG00000156136 .
    GeneIDi 1633.
    KEGGi hsa:1633.
    UCSCi uc003hfx.3. human.

    Organism-specific databases

    CTDi 1633.
    GeneCardsi GC04P071816.
    HGNCi HGNC:2704. DCK.
    MIMi 125450. gene.
    neXtProti NX_P27707.
    PharmGKBi PA137.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1428.
    HOGENOMi HOG000290165.
    HOVERGENi HBG006216.
    InParanoidi P27707.
    KOi K00893.
    PhylomeDBi P27707.
    TreeFami TF324413.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08100-MONOMER.
    BRENDAi 2.7.1.74. 2681.
    Reactomei REACT_1923. Purine salvage.
    REACT_655. Pyrimidine salvage reactions.
    SABIO-RK P27707.

    Miscellaneous databases

    EvolutionaryTracei P27707.
    GeneWikii Deoxycytidine_kinase.
    GenomeRNAii 1633.
    NextBioi 6698.
    PROi P27707.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27707.
    Bgeei P27707.
    CleanExi HS_DCK.
    Genevestigatori P27707.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR002624. DNK.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10513. PTHR10513. 1 hit.
    Pfami PF01712. dNK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000705. DNK. 1 hit.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 138 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