Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

  1. ATP binding Source: UniProtKB-KW
  2. deoxycytidine kinase activity Source: UniProtKB
  3. drug binding Source: UniProtKB
  4. nucleoside kinase activity Source: Reactome
  5. 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
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

Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: HPA
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.

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.
GenevestigatoriP27707.

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
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[»]
4Q1CX-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.

Polymorphism databases

DMDMi118447.

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[»]
4Q1CX-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 databases

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.
GenevestigatoriP27707.

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(2003) [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 (MAY-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 (SEP-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(2003) [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(1990) [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(1996) [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(2007) [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(2009) [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(2009) [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(2002) [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(2005) [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(2006) [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(2007) [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(2008) [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(2009) [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(2009) [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: March 4, 2015
This is version 143 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.