dbPTM

DCK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DCK_HUMAN
UniProt AC	P27707
Protein Name	Deoxycytidine kinase
Gene Name	DCK
Organism	Homo sapiens (Human).
Sequence Length	260
Subcellular Localization	Nucleus .
Protein Description	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	MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCNVQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAEKPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQATPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNEDFKDKYESLVEKVKEFLSTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MATPPKRSCP -----CCCCCCCCCC	38.53	20544527
8	Phosphorylation	MATPPKRSCPSFSAS CCCCCCCCCCCCCCC	36.18	25159151
11	Phosphorylation	PPKRSCPSFSASSEG CCCCCCCCCCCCCCC	35.84	20544527
13	Phosphorylation	KRSCPSFSASSEGTR CCCCCCCCCCCCCCE	31.42	25159151
15	Phosphorylation	SCPSFSASSEGTRIK CCCCCCCCCCCCEEE	27.94	20544527
16	Phosphorylation	CPSFSASSEGTRIKK CCCCCCCCCCCEEEE	39.50	25159151
19	Phosphorylation	FSASSEGTRIKKISI CCCCCCCCEEEEEEE	25.77	21712546
23	Ubiquitination	SEGTRIKKISIEGNI CCCCEEEEEEEECCC	39.04	-
34	Ubiquitination	EGNIAAGKSTFVNIL ECCCCCCHHHHHHHH	41.41	21906983
35	Phosphorylation	GNIAAGKSTFVNILK CCCCCCHHHHHHHHH	26.59	22817900
42	Ubiquitination	STFVNILKQLCEDWE HHHHHHHHHHHCCCC	37.11	-
45	Glutathionylation	VNILKQLCEDWEVVP HHHHHHHHCCCCCCC	4.06	22555962
63	Phosphorylation	ARWCNVQSTQDEFEE HHHCCCCCCHHHHHH	24.61	21082442
64	Phosphorylation	RWCNVQSTQDEFEEL HHCCCCCCHHHHHHH	23.97	17525332
72	Phosphorylation	QDEFEELTMSQKNGG HHHHHHHHHHHHCCC	20.32	30266825
74	Phosphorylation	EFEELTMSQKNGGNV HHHHHHHHHHCCCCE	32.54	22167270
76	Ubiquitination	EELTMSQKNGGNVLQ HHHHHHHHCCCCEEH	50.70	-
88	Acetylation	VLQMMYEKPERWSFT EEHHHEECCCCEEEE	34.39	7825067
88	Ubiquitination	VLQMMYEKPERWSFT EEHHHEECCCCEEEE	34.39	-
115	Ubiquitination	QLASLNGKLKDAEKP HHHHHCCCCCCCCCC	51.82	-
115	Acetylation	QLASLNGKLKDAEKP HHHHHCCCCCCCCCC	51.82	25953088
117	Ubiquitination	ASLNGKLKDAEKPVL HHHCCCCCCCCCCEE	59.38	21906983
117	Acetylation	ASLNGKLKDAEKPVL HHHCCCCCCCCCCEE	59.38	25953088
121	Ubiquitination	GKLKDAEKPVLFFER CCCCCCCCCEEEEEC	41.99	-
121	Acetylation	GKLKDAEKPVLFFER CCCCCCCCCEEEEEC	41.99	26822725
190	Phosphorylation	ETCLHRIYLRGRNEE HHHHHHHHHCCCCHH	7.12	-
204	Phosphorylation	EQGIPLEYLEKLHYK HCCCCHHHHHHHCCC	28.04	-
207	Acetylation	IPLEYLEKLHYKHES CCHHHHHHHCCCCHH	37.66	26822725
211	Ubiquitination	YLEKLHYKHESWLLH HHHHHCCCCHHHHHH	30.10	-
214	Phosphorylation	KLHYKHESWLLHRTL HHCCCCHHHHHHHHH	23.81	27067055
222	Ubiquitination	WLLHRTLKTNFDYLQ HHHHHHHCCCCHHHC	40.59	-
243	Ubiquitination	LDVNEDFKDKYESLV EECCHHHHHHHHHHH	66.68	-
245	Ubiquitination	VNEDFKDKYESLVEK CCHHHHHHHHHHHHH	52.05	-
246	Phosphorylation	NEDFKDKYESLVEKV CHHHHHHHHHHHHHH	22.38	29083192
248	Phosphorylation	DFKDKYESLVEKVKE HHHHHHHHHHHHHHH	34.33	29083192
252	Ubiquitination	KYESLVEKVKEFLST HHHHHHHHHHHHHHC	51.64	-
252	Acetylation	KYESLVEKVKEFLST HHHHHHHHHHHHHHC	51.64	11688171
254	Ubiquitination	ESLVEKVKEFLSTL- HHHHHHHHHHHHCC-	54.54	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
11	S	Phosphorylation	Kinase	CSNK1D	P48730	GPS
11	S	Phosphorylation	Kinase	CK1	-	Uniprot
15	S	Phosphorylation	Kinase	CSNK1D	P48730	GPS
15	S	Phosphorylation	Kinase	CK1	-	Uniprot
72	T	Phosphorylation	Kinase	CSNK1D	P48730	GPS
72	T	Phosphorylation	Kinase	CK1	-	Uniprot
74	S	Phosphorylation	Kinase	ATM	Q13315	PSP
74	S	Phosphorylation	Kinase	ATR	Q13535	PSP
74	S	Phosphorylation	Kinase	CSNK1D	P48730	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
74	S	Phosphorylation		18669648
Phosphorylated and activated in vitro upon phosphorylation at Ser-74 by CSNK1D/CK1.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DCK_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RXRG_HUMAN	RXRG	physical	21900206
DCK_HUMAN	DCK	physical	21900206
TFEC_HUMAN	TFEC	physical	21988832
PURA2_HUMAN	ADSS	physical	22863883
CHM4A_HUMAN	CHMP4A	physical	22863883
CHRC1_HUMAN	CHRAC1	physical	22863883
EFHD2_HUMAN	EFHD2	physical	22863883
CH10_HUMAN	HSPE1	physical	22863883
IDHC_HUMAN	IDH1	physical	22863883
PTMS_HUMAN	PTMS	physical	22863883
RANG_HUMAN	RANBP1	physical	22863883
RBBP7_HUMAN	RBBP7	physical	22863883
TALDO_HUMAN	TALDO1	physical	22863883
THOP1_HUMAN	THOP1	physical	22863883
TYSY_HUMAN	TYMS	physical	22863883

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00242	Cladribine
DB00631	Clofarabine
DB00987	Cytarabine
DB01262	Decitabine
DB00879	Emtricitabine
DB01073	Fludarabine
DB00441	Gemcitabine
DB00709	Lamivudine
DB01280	Nelarabine
DB00642	Pemetrexed
DB00943	Zalcitabine

Regulatory Network of DCK_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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.	19369195 [Abstract]
"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.	18691976 [Abstract]

show