P27707 (DCK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Deoxycytidine kinase
Short name=dCK
EC=2.7.1.74

Gene names

Name:

DCK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.19 Ref.22
Catalytic activity	NTP + deoxycytidine = NDP + dCMP. Ref.16 Ref.19 Ref.20 Ref.22
Subunit structure	Homodimer. Ref.16 Ref.17
Subcellular location	Nucleus Ref.8.
Post-translational modification	Phosphorylated and activated in vitro upon phosphorylation at Ser-74 by CSNK1D/CK1. Ref.13
Sequence similarities	Belongs to the DCK/DGK family.
Caution	Was shown to be phosphorylated and activated by CSNK1D/CK1 in vitro but probably not in vivo (Ref.13).
Biophysicochemical properties	Kinetic parameters: KM=6.2 µM for deoxycytidine (dC) Ref.16 KM=15.5 µM for cytarabine (araC) KM=22 µM for gemcitabine (dC)

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	purine nucleobase metabolic process Traceable author statement. Source: Reactome purine-containing compound salvage Traceable author statement. Source: Reactome pyrimidine nucleobase metabolic process Traceable author statement. Source: Reactome pyrimidine nucleoside salvage Traceable author statement. Source: Reactome pyrimidine nucleotide metabolic process Inferred from direct assay Ref.16. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW deoxycytidine kinase activity Inferred from direct assay Ref.16. Source: UniProtKB drug binding Inferred from direct assay Ref.16. Source: UniProtKB phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 260

260

Deoxycytidine kinase

PRO_0000175090

Regions

Nucleotide binding

28 – 36

9

ATP

Nucleotide binding

188 – 192

5

ATP

Nucleotide binding

240 – 242

3

ATP

Sites

Active site

127

1

Proton acceptor Potential

Binding site

53

1

Substrate

Binding site

86

1

Substrate

Binding site

97

1

Substrate

Binding site

128

1

Substrate

Binding site

133

1

Substrate

Binding site

197

1

Substrate

Amino acid modifications

Modified residue

11

1

Phosphoserine; by CK1 Probable

Modified residue

15

1

Phosphoserine; by CK1 Probable

Modified residue

72

1

Phosphothreonine; by CK1 Probable

Modified residue

74

1

Phosphoserine Ref.11 Ref.13 Ref.14

Experimental info

Mutagenesis

100

1

A → V: Strongly increased catalytic efficiency towards deoxycytidine; when associated with M-104 and A-133. Ref.16

Mutagenesis

104

1

R → L: Strongly increased catalytic efficiency towards deoxythymidine; when associated with A-133. Ref.16 Ref.20 Ref.22

Mutagenesis

104

1

R → M: Strongly increased catalytic efficiency towards deoxycytidine; when associated with V-100 and A-133. Ref.16 Ref.20 Ref.22

Mutagenesis

133

1

D → 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. Ref.16 Ref.20 Ref.22

Sequence conflict

122

1

P → S in AAV38744. Ref.4

Sequence conflict

122

1

P → S in AAV38745. Ref.4

Secondary structure

1

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260

Helix Strand Turn

Details...

Beta strand

22 – 27

6

Helix

34 – 38

5

Turn

39 – 41

3

Helix

42 – 44

3

Beta strand

48 – 51

4

Helix

55 – 58

4

Beta strand

61 – 63

3

Helix

69 – 72

4

Helix

81 – 87

7

Helix

89 – 112

24

Helix

115 – 118

4

Beta strand

119 – 121

3

Beta strand

123 – 128

6

Helix

130 – 135

6

Helix

137 – 143

7

Helix

149 – 170

22

Beta strand

173 – 179

7

Helix

182 – 192

11

Helix

195 – 197

3

Helix

202 – 216

15

Helix

226 – 230

5

Beta strand

233 – 237

5

Helix

242 – 258

17

Sequences

	Sequence		Length	Mass (Da)
	P27707 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 626B9D2D6BED8DBC	FASTA	260	30,519
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of human deoxycytidine kinase cDNA." Chottiner E.G., Shewach D.S., Datta N.S., Ashcraft E., Gribbin D., Ginsburg D., Fox I.H., Mitchell B.S. Proc. Natl. Acad. Sci. U.S.A. 88:1531-1535(1991) [PubMed] [Europe PMC] [Abstract] 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]	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 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]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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]	"Lead optimization and structure-based design of potent and bioavailable deoxycytidine kinase inhibitors." Jessop T.C., Tarver J.E., Carlsen M., Xu A., Healy J.P., Heim-Riether A., Fu Q., Taylor J.A., Augeri D.J., Shen M., Stouch T.R., Swanson R.V., Tari L.W., Hunter M., Hoffman I., Keyes P.E., Yu X.C., Miranda M. , Liu Q., Swaffield J.C., David Kimball S., Nouraldeen A., Wilson A.G., Foushee A.M., Jhaver K., Finch R., Anderson S., Oravecz T., Carson K.G. Bioorg. Med. Chem. Lett. 19:6784-6787(2009) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00020454.

PIR

A38585.

RefSeq

NP_000779.1. NM_000788.2.

UniGene

Hs.709.

3D structure databases

PDBe
RCSB PDB
PDBj

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	4-260	[»]
2A30	X-ray	3.02	A/B/C/D	4-260	[»]
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	[»]

ProteinModelPortal

P27707.

ModBase

Search...

Protein-protein interaction databases

IntAct

P27707. 4 interactions.

MINT

MINT-1387532.

STRING

9606.ENSP00000286648.

PTM databases

PhosphoSite

P27707.

Polymorphism databases

DMDM

118447.

Proteomic databases

PaxDb

P27707.

PeptideAtlas

P27707.

PRIDE

P27707.

Protocols and materials databases

DNASU

1633.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000286648; ENSP00000286648; ENSG00000156136.

GeneID

1633.

KEGG

hsa:1633.

UCSC

uc003hfx.3. human.

Organism-specific databases

CTD

1633.

GeneCards

GC04P071816.

HGNC

HGNC:2704. DCK.

MIM

125450. gene.

neXtProt

NX_P27707.

PharmGKB

PA137.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1428.

HOGENOM

HOG000290165.

HOVERGEN

HBG006216.

InParanoid

P27707.

KO

K00893.

PhylomeDB

P27707.

Enzyme and pathway databases

BRENDA

2.7.1.74. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P27707.

Gene expression databases

ArrayExpress

P27707.

Bgee

P27707.

CleanEx

HS_DCK.

Genevestigator

P27707.

GermOnline

ENSG00000156136. Homo sapiens.

Family and domain databases

InterPro

IPR002624. Deoxynucleoside_kinase.
[Graphical view]

PANTHER

PTHR10513. PTHR10513. 1 hit.

Pfam

PF01712. dNK. 1 hit.
[Graphical view]

PIRSF

PIRSF000705. DNK. 1 hit.

ProtoNet

Search...

Other

BindingDB

P27707.

ChEMBL

CHEMBL2447.

DrugBank

DB00242. Cladribine.
DB00631. Clofarabine.
DB01262. Decitabine.
DB01073. Fludarabine.
DB00441. Gemcitabine.
DB00642. Pemetrexed.
DB00943. Zalcitabine.

EvolutionaryTrace

P27707.

GenomeRNAi

1633.

NextBio

6698.

SOURCE

Search...

Entry information

Entry name

DCK_HUMAN

Accession

Primary (citable) accession number: P27707
Secondary accession number(s): B2R8V6, Q5TZY7, Q6FI11

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.