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P27707 (DCK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxycytidine kinase

Short name=dCK
EC=2.7.1.74
Gene names
Name:DCK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdeoxyribonucleoside monophosphate biosynthetic process

Inferred from direct assay Ref.16. Source: GOC

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

nucleotide biosynthetic process

Inferred from experiment. Source: GOC

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

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP 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

nucleoside kinase activity

Inferred from experiment. Source: Reactome

phosphotransferase activity, alcohol group as acceptor

Inferred from electronic annotation. Source: InterPro

protein homodimerization activity

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Deoxycytidine kinase
PRO_0000175090

Regions

Nucleotide binding28 – 369ATP
Nucleotide binding188 – 1925ATP
Nucleotide binding240 – 2423ATP

Sites

Active site1271Proton acceptor Potential
Binding site531Substrate
Binding site861Substrate
Binding site971Substrate
Binding site1281Substrate
Binding site1331Substrate
Binding site1971Substrate

Amino acid modifications

Modified residue111Phosphoserine; by CK1 Probable
Modified residue151Phosphoserine; by CK1 Probable
Modified residue721Phosphothreonine; by CK1 Probable
Modified residue741Phosphoserine Ref.11 Ref.13 Ref.14

Experimental info

Mutagenesis1001A → V: Strongly increased catalytic efficiency towards deoxycytidine; when associated with M-104 and A-133. Ref.16
Mutagenesis1041R → L: Strongly increased catalytic efficiency towards deoxythymidine; when associated with A-133. Ref.16 Ref.20 Ref.22
Mutagenesis1041R → M: Strongly increased catalytic efficiency towards deoxycytidine; when associated with V-100 and A-133. Ref.16 Ref.20 Ref.22
Mutagenesis1331D → 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 conflict1221P → S in AAV38744. Ref.4
Sequence conflict1221P → S in AAV38745. Ref.4

Secondary structure

............................................ 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27707 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 626B9D2D6BED8DBC

FASTA26030,519
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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. expand/collapse author list , 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.
CCDSCCDS3548.1.
PIRA38585.
RefSeqNP_000779.1. NM_000788.2.
UniGeneHs.709.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP27707.
SMRP27707. Positions 19-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108001. 21 interactions.
IntActP27707. 5 interactions.
MINTMINT-1387532.
STRING9606.ENSP00000286648.

Chemistry

BindingDBP27707.
ChEMBLCHEMBL2447.
DrugBankDB00242. Cladribine.
DB00631. Clofarabine.
DB01262. Decitabine.
DB01073. Fludarabine.
DB00441. Gemcitabine.
DB00642. Pemetrexed.
DB00943. Zalcitabine.

PTM databases

PhosphoSiteP27707.

Polymorphism databases

DMDM118447.

Proteomic databases

MaxQBP27707.
PaxDbP27707.
PeptideAtlasP27707.
PRIDEP27707.

Protocols and materials databases

DNASU1633.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286648; ENSP00000286648; ENSG00000156136.
GeneID1633.
KEGGhsa:1633.
UCSCuc003hfx.3. human.

Organism-specific databases

CTD1633.
GeneCardsGC04P071816.
HGNCHGNC:2704. DCK.
MIM125450. gene.
neXtProtNX_P27707.
PharmGKBPA137.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1428.
HOGENOMHOG000290165.
HOVERGENHBG006216.
InParanoidP27707.
KOK00893.
PhylomeDBP27707.
TreeFamTF324413.

Enzyme and pathway databases

BioCycMetaCyc:HS08100-MONOMER.
BRENDA2.7.1.74. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP27707.

Gene expression databases

ArrayExpressP27707.
BgeeP27707.
CleanExHS_DCK.
GenevestigatorP27707.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR002624. Deoxynucleoside_kinase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10513. PTHR10513. 1 hit.
PfamPF01712. dNK. 1 hit.
[Graphical view]
PIRSFPIRSF000705. DNK. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP27707.
GeneWikiDeoxycytidine_kinase.
GenomeRNAi1633.
NextBio6698.
PROP27707.
SOURCESearch...

Entry information

Entry nameDCK_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM