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dCK (human)

Overview dCK 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. Belongs to the DCK/DGK family. Note: This description may include information from UniProtKB. Protein type: Nucleotide Metabolism - pyrimidine; Nucleotide Metabolism - purine; Kinase, other; EC 2.7.1.74 Cellular Component: cytosol; nucleus Molecular Function: protein homodimerization activity; nucleoside kinase activity; deoxycytidine kinase activity; magnesium ion binding; pyrimidine deoxyribonucleoside binding; drug binding; phosphotransferase activity, alcohol group as acceptor; ATP binding Biological Process: deoxycytidine metabolic process; pyrimidine base metabolic process; nucleobase, nucleoside and nucleotide metabolic process; pyrimidine nucleotide metabolic process; nucleotide biosynthetic process; pyrimidine nucleoside salvage; drug metabolic process; purine base metabolic process; purine salvage Reference #:  P27707 (UniProtKB) Alt. Names/Synonyms: DCK; Deoxycytidine kinase; MGC117410; MGC138632 Gene Symbols: DCK Molecular weight: 30,519 Da Basal Isoelectric point: 5.14  Predict pI for various phosphorylation states

Select Structure to View Below dCK 1P5Z - B=1-260 (human) 1P60 - A/B=1-260 (human) 1P61 - B=1-260 (human) 1P62 - B=1-260 (human) 2A2Z - A/B/C/D=1-260 (human) 2A30 - A/B/C/D=1-260 (human) 2A7Q - A=1-260 (human) 2NO0 - A/B=1-260 (human) 2NO1 - A/B=1-260 (human) 2NO6 - A/B=1-260 (human) 2NO7 - A/B=1-260 (human) 2NO9 - A/B=1-260 (human) 2NOA - A/B=1-260 (human) 2QRN - A/D/C/B=1-260 (human) 2QRO - A/D/C/B=1-260 (human) 2ZI3 - A/B=1-260 (human) 2ZI4 - A=1-260 (human) 2ZI5 - A/D/C/B=1-260 (human) 2ZI6 - A/D/C/B=1-260 (human) 2ZI7 - A/B=1-260 (human) 2ZI9 - A/B=1-260 (human) 2ZIA - A/B=1-260 (human) 3HP1 - A=1-260 (human) 3IPX - A=20-260 (human) 3IPY - A/B=20-260 (human) 3KFX - A/B=1-260 (human) 3MJR - A/D/C/B=1-260 (human) 3QEJ - A/B=1-260 (human) 3QEN - A/B=1-260 (human) 3QEO - A/B=1-260 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1P5Z 1P60 1P61 1P62 2A2Z 2A30 2A7Q 2NO0 2NO1 2NO6 2NO7 2NO9 2NOA 2QRN 2QRO 2ZI3 2ZI4 2ZI5 2ZI6 2ZI7 2ZI9 2ZIA 3HP1 3IPX 3IPY 3KFX 3MJR 3QEJ 3QEN 3QEO  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  InnateDB  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
enzymatic activity, induced: S74‑p phosphorylation: T3‑p, S11‑p, S15‑p protein conformation: S74‑p protein stabilization: T3‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
3	3		T3-p	_____MAtPPKRsCP
0	2		S8-p	MAtPPKRsCPsFsAs
4	15		S11-p	PPKRsCPsFsAssEG
0	13		S13-p	KRsCPsFsAssEGTR
0	2		A14	RsCPsFsAssEGTRI
4	11		S15-p	sCPsFsAssEGTRIK
0	4		S16-p	CPsFsAssEGTRIKk
0	1		K23-u	sEGTRIKkISIEGNI
0	2		K34-u	EGNIAAGksTFVNIL
0	1		S35-p	GNIAAGksTFVNILK
0	7		S63-p	ARWCNVQstQDEFEE
0	6		T64-p	RWCNVQstQDEFEEL
1	12		T72-p	QDEFEELtMsQKNGG
0	1		M73	DEFEELtMsQKNGGN
9	100		S74-p	EFEELtMsQKNGGNV
0	1		K88-a	VLQMMYEkPERWSFT
0	3		K115-u	QLASLNGkLkDAEkP
0	51		K117-u	ASLNGkLkDAEkPVL
0	5		K121-u	GkLkDAEkPVLFFER
0	1		Y190-p	ETCLHRIyLRGRNEE
0	1		Y204-p	EQGIPLEyLEKLHYK
0	1		K222-u	WLLHRTLkTNFDYLQ
0	17		K243-u	LDVNEDFkDKYESLV
0	1		K245	VNEDFkDKYESLVEk
0	1		K252-a	KYESLVEkVKEFLST
0	3		K252-u	KYESLVEkVKEFLST

	mouse
T3	_____MATPPKRFCP
F8	MATPPKRFCPsPsts
S11-p	PPKRFCPsPstssEG
S13-p	KRFCPsPstssEGTR
T14-p	RFCPsPstssEGTRI
S15-p	FCPsPstssEGTRIK
S16-p	CPsPstssEGTRIKK
K23	sEGTRIKKISIEGNI
K34	EGNIAAGKSTFVNIL
S35	GNIAAGKSTFVNILK
S63	ARWCNVQSTQEEFEE
T64	RWCNVQSTQEEFEEL
T72	QEEFEELTtsQKSGG
T73-p	EEFEELTtsQKSGGN
S74-p	EFEELTtsQKSGGNV
K88	VLQMMYEKPERWSFT
K115	QLASLNGKLkDAEkP
K117-u	ASLNGKLkDAEkPVL
K121-u	GKLkDAEkPVLFFER
Y190	EKCLNRIYLRGRNEE
Y204	EQGIPLEYLEKLHYK
K222	WLLHRTLKTSFDYLQ
K243-u	LDVNEDFkDkHESLV
K245-u	VNEDFkDkHESLVEK
K252	kHESLVEKVKEFLST
K252	kHESLVEKVKEFLST

	rat
T3	_____MATPPKRFCS
F8	MATPPKRFCSsPSTS
S11-p	PPKRFCSsPSTSSEG
S13	KRFCSsPSTSSEGTR
T14	RFCSsPSTSSEGTRI
S15	FCSsPSTSSEGTRIK
S16	CSsPSTSSEGTRIKK
K23	SEGTRIKKISIEGNI
K34	EGNIAAGKSTFVNIL
S35	GNIAAGKSTFVNILK
S63	ARWCNVQSTQDEFEE
T64	RWCNVQSTQDEFEEL
T72	QDEFEELTTSQKSGG
T73	DEFEELTTSQKSGGN
S74	EFEELTTSQKSGGNV
K88	VLQMMYEKPERWSFI
S115	QLASLNGSLRDAEKP
R117	ASLNGSLRDAEKPVL
K121	GSLRDAEKPVLFFER
Y190	EKCLNRIYIRGRDEE
Y204	EQGIPLEYLEKLHYK
K222	WLLHRTLKTNFEYLQ
K243	LDVNLDFKDKEESLV
K245	VNLDFKDKEESLVEK
K252	KEESLVEKVKEFLST
K252	KEESLVEKVKEFLST

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