Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Deoxycytidine kinase  

UniProtKB / Swiss-Prot ID :  DCK_HUMAN

Gene Name (Synonyms) : 
DCK  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein 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. 

Protein Sequence MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCNVQSTQDEFEE...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCEEEEEEECCCCCCHHHHHHHHHHHCCCCCEEECCCCCCCCCCCCCCCHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
3Phosphothreonine--MATPPKR
--CCCCCCC
38.53HPRD
Link-
3Phosphothreonine--MATPPKR
--CCCCCCC
38.53Phosphositeplus
Link-
3Phosphothreonine--MATPPKR
--CCCCCCC
38.53SysPTM
Link-
3Phosphothreonine.--MATPPKR
--CCCCCCC
38.53UniProtKB
Link-
8PhosphoserinePPKRSCPSF
CCCCCCCCC
36.18HPRD
Link-
8PhosphoserinePPKRSCPSF
CCCCCCCCC
36.18Phosphositeplus
Link-
8PhosphoserinePPKRSCPSF
CCCCCCCCC
36.18SysPTM
Link-
8Phosphoserine.PPKRSCPSF
CCCCCCCCC
36.18UniProtKB
Link-
11PhosphoserineRSCPSFSAS
CCCCCCCCC
35.84HPRD
Link-
11PhosphoserineRSCPSFSAS
CCCCCCCCC
35.84Phosphositeplus
Link-
11PhosphoserineRSCPSFSAS
CCCCCCCCC
35.84SysPTM
Link-
13PhosphoserineCPSFSASSE
CCCCCCCCC
31.42HPRD
Link-
13PhosphoserineCPSFSASSE
CCCCCCCCC
31.42Phosphositeplus
Link-
13Phosphoserine.CPSFSASSE
CCCCCCCCC
31.42UniProtKB
Link-
15PhosphoserineSFSASSEGT
CCCCCCCCC
27.94HPRD
Link-
15PhosphoserineSFSASSEGT
CCCCCCCCC
27.94Phosphositeplus
Link-
15PhosphoserineSFSASSEGT
CCCCCCCCC
27.94SysPTM
Link-
16Phosphoserine.FSASSEGTR
CCCCCCCCC
39.50UniProtKB
Link-
19PhosphothreonineSSEGTRIKK
CCCCCCEEE
25.77HPRD
Link
34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IAAGKSTFV
CCCCHHHHH
41.41Phosphositeplus
Link
35PhosphoserineAAGKSTFVN
CCCHHHHHH
26.59Phosphositeplus
Link
35Phosphoserine.AAGKSTFVN
CCCHHHHHH
26.59UniProtKB
Link
63PhosphoserineCNVQSTQDE
CCCCCCCCC
24.61Phosphositeplus
Link
63Phosphoserine.CNVQSTQDE
CCCCCCCCC
24.61UniProtKB
Link
64PhosphothreonineNVQSTQDEF
CCCCCCCCH
23.97HPRD
Link-
64PhosphothreonineNVQSTQDEF
CCCCCCCCH
23.97Phosphositeplus
Link-
72PhosphothreonineFEELTMSQK
HHHHCCHHC
20.32HPRD
Link-
72PhosphothreonineFEELTMSQK
HHHHCCHHC
20.32Phosphositeplus
Link-
74PhosphoserineELTMSQKNG
HHCCHHCCC
32.54HPRD
Link-
74PhosphoserineELTMSQKNG
HHCCHHCCC
32.54PhosphoELM
Link-
74PhosphoserineELTMSQKNG
HHCCHHCCC
32.54Phosphositeplus
Link-
74PhosphoserineELTMSQKNG
HHCCHHCCC
32.54SysPTM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MED19_HUMANphysical interactionMINT-64896MINT16169070
GOLM1_HUMANphysical interactionMINT-64962MINT16169070
DD19B_HUMANyeast 2-hybridHPRD:00507HPRD16169070
GOLM1_HUMANyeast 2-hybridHPRD:00507HPRD16169070
PUR8_HUMANENSP00000286648STRING
PUR8_HUMANENSP00000286648STRING
PUR8_HUMANENSP00000286648STRING
AICDA_HUMANENSP00000286648STRING
AICDA_HUMANENSP00000286648STRING
AICDA_HUMANENSP00000286648STRING
AMPD3_HUMANENSP00000286648STRING
AMPD3_HUMANENSP00000286648STRING
AMPD3_HUMANENSP00000286648STRING
AMPD2_HUMANENSP00000286648STRING
AMPD2_HUMANENSP00000286648STRING
AMPD2_HUMANENSP00000286648STRING
KAD7_HUMANENSP00000286648STRING
KAD7_HUMANENSP00000286648STRING
KAD7_HUMANENSP00000286648STRING
ENTP3_HUMANENSP00000286648STRING
ENTP3_HUMANENSP00000286648STRING
ENTP3_HUMANENSP00000286648STRING
CANT1_HUMANENSP00000286648STRING
CANT1_HUMANENSP00000286648STRING
CANT1_HUMANENSP00000286648STRING
DCTD_HUMANENSP00000286648STRING
DCTD_HUMANENSP00000286648STRING
DCTD_HUMANENSP00000286648STRING
ENTP8_HUMANENSP00000286648STRING
ENTP8_HUMANENSP00000286648STRING
ENTP8_HUMANENSP00000286648STRING
ENTP8_HUMANENSP00000286648STRING
ENTP8_HUMANENSP00000286648STRING
ENTP8_HUMANENSP00000286648STRING
KAD5_HUMANENSP00000286648STRING
KAD5_HUMANENSP00000286648STRING
KAD5_HUMANENSP00000286648STRING
PNPH_HUMANENSP00000286648STRING
PNPH_HUMANENSP00000286648STRING
PNPH_HUMANENSP00000286648STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00242Cladribine
DB00631Clofarabine
DB00987Cytarabine
DB01262Decitabine
DB00879Emtricitabine
DB01073Fludarabine
DB00441Gemcitabine
DB00709Lamivudine
DB01280Nelarabine
DB00642Pemetrexed
DB00943Zalcitabine
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-11; SER-13;SER-15; SER-16; SER-35; SER-63; THR-72 AND SER-74, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-8; SER-11; SER-15AND SER-74, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures