dbPTM

DCTP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DCTP1_HUMAN
UniProt AC	Q9H773
Protein Name	dCTP pyrophosphatase 1 {ECO:0000305}
Gene Name	DCTPP1 {ECO:0000312\|HGNC:HGNC:28777}
Organism	Homo sapiens (Human).
Sequence Length	170
Subcellular Localization	Mitochondrion . Nucleus . Cytoplasm, cytosol .
Protein Description	Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which it may even have a higher efficiency. May protect DNA or RNA against the incorporation of these genotoxic nucleotide analogs through their catabolism..
Protein Sequence	MSVAGGEIRGDTGGEDTAAPGRFSFSPEPTLEDIRRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGPQGWSPRERAALQEELSDVLIYLVALAARCRVDLPLAVLSKMDINRRRYPAHLARSSSRKYTELPHGAISEDQAVGPADIPCDSTGQTST

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSVAGGEIR ------CCCCCCCCC	22.22	23401153
2	Acetylation	------MSVAGGEIR ------CCCCCCCCC	22.22	18691976
9	Methylation	SVAGGEIRGDTGGED CCCCCCCCCCCCCCC	32.41	115920149
12	Phosphorylation	GGEIRGDTGGEDTAA CCCCCCCCCCCCCCC	50.32	22115753
17	Phosphorylation	GDTGGEDTAAPGRFS CCCCCCCCCCCCCCC	22.03	22115753
24	Phosphorylation	TAAPGRFSFSPEPTL CCCCCCCCCCCCCCH	24.37	27050516
26	Phosphorylation	APGRFSFSPEPTLED CCCCCCCCCCCCHHH	27.44	27690223
30	Phosphorylation	FSFSPEPTLEDIRRL CCCCCCCCHHHHHHH	40.91	27690223
35	Methylation	EPTLEDIRRLHAEFA CCCHHHHHHHHHHHH	47.64	115920141
45	Methylation	HAEFAAERDWEQFHQ HHHHHHHCCHHHHHC	50.01	115920145
75	Phosphorylation	AELFQWKTDGEPGPQ HHHHCCCCCCCCCCC	46.40	23927012
85	Phosphorylation	EPGPQGWSPRERAAL CCCCCCCCHHHHHHH	22.39	23401153
110	Glutathionylation	LVALAARCRVDLPLA HHHHHHHCCCCCCHH	4.22	22555962
121	Ubiquitination	LPLAVLSKMDINRRR CCHHHHHHCCCCCCC	36.11	21963094
129	Phosphorylation	MDINRRRYPAHLARS CCCCCCCCCHHHHHH	11.71	28152594
136	Phosphorylation	YPAHLARSSSRKYTE CCHHHHHHCCCCCCC	27.36	26074081
137	Phosphorylation	PAHLARSSSRKYTEL CHHHHHHCCCCCCCC	28.71	26074081
138	Phosphorylation	AHLARSSSRKYTELP HHHHHHCCCCCCCCC	33.76	25394399
140	Ubiquitination	LARSSSRKYTELPHG HHHHCCCCCCCCCCC	59.48	29967540
141	Phosphorylation	ARSSSRKYTELPHGA HHHCCCCCCCCCCCC	12.34	28796482
142	Phosphorylation	RSSSRKYTELPHGAI HHCCCCCCCCCCCCC	33.80	28796482
150	Phosphorylation	ELPHGAISEDQAVGP CCCCCCCCCCCCCCC	34.29	23401153
162	Glutathionylation	VGPADIPCDSTGQTS CCCCCCCCCCCCCCC	7.06	22555962
164	Phosphorylation	PADIPCDSTGQTST- CCCCCCCCCCCCCC-	40.95	23401153
165	Phosphorylation	ADIPCDSTGQTST-- CCCCCCCCCCCCC--	21.76	23663014
168	Phosphorylation	PCDSTGQTST----- CCCCCCCCCC-----	35.36	25159151
169	Phosphorylation	CDSTGQTST------ CCCCCCCCC------	25.00	23401153
170	Phosphorylation	DSTGQTST------- CCCCCCCC-------	46.12	25159151

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
Oops, there are no upstream regulatory protein records of DCTP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DCTP1_HUMAN !!

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 DCTP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DCTP1_HUMAN	DCTPP1	physical	16189514
DCTP1_HUMAN	DCTPP1	physical	16169070
A4_HUMAN	APP	physical	21832049
CAPZB_HUMAN	CAPZB	physical	22863883
GNPI1_HUMAN	GNPDA1	physical	22863883
HERC4_HUMAN	HERC4	physical	22863883
PDE12_HUMAN	PDE12	physical	22863883
RD23A_HUMAN	RAD23A	physical	22863883
WDR4_HUMAN	WDR4	physical	22863883
DCTP1_HUMAN	DCTPP1	physical	25416956
CF161_HUMAN	C15orf26	physical	27173435

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
There are no disease associations of PTM sites.

Regulatory Network of DCTP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-2; THR-12 AND SER-85,AND MASS SPECTROMETRY.	18691976 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.	17287340 [Abstract]