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UniProtKB/Swiss-Prot entry P27707


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DCK_HUMAN
Primary accession number P27707
Secondary accession numbers Q5TZY7 Q6FI11
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 75)
Name and origin of the protein
Protein name Deoxycytidine kinase
Synonyms dCK
EC 2.7.1.74
Gene name
Name: DCK
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 58-70; 119-127 AND 189-192.
PubMed=1996353 [NCBI, ExPASy, EBI, Israel, Japan]
Chottiner E.G., Shewach D.S., Datta N.S., Ashcraft E., Gribbin D., Ginsburg D., Fox I.H., Mitchell B.S.;
"Cloning and expression of human deoxycytidine kinase cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 88:1531-1535(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
DOI=10.1016/0014-5793(91)80332-W; PubMed=2013338 [NCBI, ExPASy, EBI, Israel, Japan]
Eriksson S., Cederlund E., Bergman T., Joernvall H., Bohman C.;
"Characterization of human deoxycytidine kinase. Correlation with cDNA sequences.";
FEBS Lett. 280:363-366(1991).
[7]
SUBCELLULAR LOCATION.
DOI=10.1073/pnas.94.22.11941; PubMed=9342341 [NCBI, ExPASy, EBI, Israel, Japan]
Johansson M., Brismar S., Karlsson A.;
"Human deoxycytidine kinase is located in the cell nucleus.";
Proc. Natl. Acad. Sci. U.S.A. 94:11941-11945(1997).
[8]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
DOI=10.1038/nsb942; PubMed=12808445 [NCBI, ExPASy, EBI, Israel, Japan]
Sabini E., Ort S., Monnerjahn C., Konrad M., Lavie A.;
"Structure of human dCK suggests strategies to improve anticancer and antiviral therapy.";
Nat. Struct. Biol. 10:513-519(2003).
Comments
  • FUNCTION: Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents.
  • CATALYTIC ACTIVITY: NTP + deoxycytidine = NDP + dCMP.
  • SUBUNIT: Homodimer.
  • SUBCELLULAR LOCATION: Nucleus.
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity).
  • SIMILARITY: Belongs to the DCK/DGK family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M60527; AAA35752.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536527; CAG38764.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541876; CAG46674.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019941; AAV38744.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019942; AAV38745.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471057; EAX05637.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC103764; AAI03765.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC114617; AAI14618.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38585; A38585.
RefSeq NP_000779.1; -.
UniGene Hs.709
3D structure databases
PDB
1P5Z; X-ray; 1.60 A; B=1-260.[ExPASy / RCSB / EBI]
1P60; X-ray; 1.96 A; A/B=1-260.[ExPASy / RCSB / EBI]
1P61; X-ray; 2.21 A; B=1-260.[ExPASy / RCSB / EBI]
1P62; X-ray; 1.90 A; B=1-260.[ExPASy / RCSB / EBI]
2A2Z; X-ray; 3.02 A; A/B/C/D=1-260.[ExPASy / RCSB / EBI]
2A30; X-ray; 3.02 A; A/B/C/D=1-260.[ExPASy / RCSB / EBI]
2A7Q; X-ray; 2.55 A; A=1-260.[ExPASy / RCSB / EBI]
2NO0; X-ray; 1.80 A; A/B=1-260.[ExPASy / RCSB / EBI]
2NO1; X-ray; 1.91 A; A/B=1-260.[ExPASy / RCSB / EBI]
2NO6; X-ray; 1.90 A; A/B=1-260.[ExPASy / RCSB / EBI]
2NO7; X-ray; 1.70 A; A/B=1-260.[ExPASy / RCSB / EBI]
2NO9; X-ray; 2.15 A; A/B=1-260.[ExPASy / RCSB / EBI]
2NOA; X-ray; 1.80 A; A/B=1-260.[ExPASy / RCSB / EBI]
2QRN; X-ray; 3.40 A; A/B/C/D=1-260.[ExPASy / RCSB / EBI]
2QRO; X-ray; 3.45 A; A/B/C/D=1-260.[ExPASy / RCSB / EBI]
2ZI3; X-ray; 2.30 A; A/B=1-260.[ExPASy / RCSB / EBI]
2ZI4; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
2ZI5; X-ray; 1.77 A; A/B/C/D=1-260.[ExPASy / RCSB / EBI]
2ZI6; X-ray; 1.77 A; A/B/C/D=1-260.[ExPASy / RCSB / EBI]
2ZI7; X-ray; 1.97 A; A/B=1-260.[ExPASy / RCSB / EBI]
2ZI9; X-ray; 2.51 A; A/B=1-260.[ExPASy / RCSB / EBI]
2ZIA; X-ray; 1.80 A; A/B=1-260.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1P5Z; -.
1P60; -.
1P61; -.
1P62; -.
2A2Z; -.
2A30; -.
2A7Q; -.
2NO0; -.
2NO1; -.
2NO6; -.
2NO7; -.
2NO9; -.
2NOA; -.
2QRN; -.
2QRO; -.
2ZI3; -.
2ZI4; -.
2ZI5; -.
2ZI6; -.
2ZI7; -.
2ZI9; -.
2ZIA; -.
ModBase P27707.
Protein-protein interaction databases
IntAct P27707; -.
PTM databases
PhosphoSite P27707; -.
Enzyme and pathway databases
Reactome REACT_1698; Nucleotide metabolism.
Organism-specific databases
H-InvDB HIX0031480; -.
HGNC HGNC:2704; DCK.
GenAtlas DCK.
MIM 125450; gene. [NCBI / EBI]
PharmGKB PA137; -.
GeneCards P27707.
Gene expression databases
ArrayExpress P27707; -.
CleanEx HS_DCK; -.
GermOnline ENSG00000156136; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004137; Molecular function: deoxycytidine kinase activity (traceable author statement from ProtInc).
GO:0016773; Molecular function: phosphotransferase activity, alcohol group as acceptor (inferred from electronic annotation from InterPro).
GO:0006220; Biological process: pyrimidine nucleotide metabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002624; Deoxynucleoside_kinase.
Graphical view of domain structure.
PANTHER PTHR10513; dNK; 1.
Pfam PF01712; dNK; 1.
Pfam graphical view of domain structure.
BLOCKS P27707.
ProtoNet P27707.
Proteomic databases
PeptideAtlas P27707; -.
Genome annotation databases
Ensembl ENSG00000156136; Homo sapiens. [Contig view]
GeneID 1633; -.
KEGG hsa:1633; -.
Phylogenomic databases
HOGENOM P27707; -.
HOVERGEN P27707; -.
Other
DrugBank DB00242; Cladribine.
DB00631; Clofarabine.
DB01262; Decitabine.
DB01073; Fludarabine.
DB00441; Gemcitabine.
DB00642; Pemetrexed.
DB00943; Zalcitabine.
NextBio 6698; -.
SOURCE DCK; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   260  260     Deoxycytidine kinase. PRO_0000175090
NP_BIND   28    35  8     ATP (Probable). 
MOD_RES   11    11        Phosphoserine (By similarity). 
MOD_RES   74    74        Phosphoserine (By similarity). 
CONFLICT   122   122        P -> S (in Ref. 3; AAV38744/AAV38745). 
STRAND   22    27  6      
HELIX   34    38  5      
TURN   39    41  3      
HELIX   42    44  3      
STRAND   48    51  4      
HELIX   55    58  4      
HELIX   81    87  7      
HELIX   89   112  24      
HELIX   115   118  4      
STRAND   119   121  3      
STRAND   123   128  6      
HELIX   130   135  6      
HELIX   137   143  7      
HELIX   149   170  22      
STRAND   173   179  7      
HELIX   182   192  11      
HELIX   195   197  3      
HELIX   202   216  15      
HELIX   226   230  5      
STRAND   233   237  5      
HELIX   242   258  17      
Sequence information
Length: 260 AA [This is the length of the unprocessed precursor] Molecular weight: 30519 Da [This is the MW of the unprocessed precursor] CRC64: 626B9D2D6BED8DBC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATPPKRSCP SFSASSEGTR IKKISIEGNI AAGKSTFVNI LKQLCEDWEV VPEPVARWCN 

        70         80         90        100        110        120 
VQSTQDEFEE LTMSQKNGGN VLQMMYEKPE RWSFTFQTYA CLSRIRAQLA SLNGKLKDAE 

       130        140        150        160        170        180 
KPVLFFERSV YSDRYIFASN LYESECMNET EWTIYQDWHD WMNNQFGQSL ELDGIIYLQA 

       190        200        210        220        230        240 
TPETCLHRIY LRGRNEEQGI PLEYLEKLHY KHESWLLHRT LKTNFDYLQE VPILTLDVNE 

       250        260 
DFKDKYESLV EKVKEFLSTL 

P27707 in FASTA format

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