UniProt Accession

 DCTP1_HUMAN; Q9H773 

Genbank Protein ID

 AY453409; AF212242; AF210430; CR457335; AK024843; BC001344 

Genbank Nucleotide ID

 AAR26724.1; AAK14927.1; AAK48422.1; CAG33616.1; BAB15025.1; AAH01344.1 

Protein Name

 dCTP pyrophosphatase 1 

Protein Synonyms/Alias

 Deoxycytidine-triphosphatase 1; dCTPase 1; RS21C6; XTP3-transactivated gene A protein 

Gene Name

 DCTPP1 

Gene Synonyms/Alias

 XTP3TPA; CDA03 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
121	LPLAVLSKMDINRRR	ubiquitination	[1, 2, 3, 4]
140	LARSSSRKYTELPHG	ubiquitination	[3]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for modified dCTP. Activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). Does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. May protect DNA or RNA against the incorporation of non- canonical nucleotide triphosphates. May protect cells against inappropriate methylation of CpG islands by DNA methyltransferases (By similarity). 

Sequence Annotation

 REPEAT 29 75 EAR.
 REGION 47 51 Substrate binding (By similarity).
 METAL 63 63 Magnesium (By similarity).
 METAL 66 66 Magnesium (By similarity).
 METAL 95 95 Magnesium (By similarity).
 METAL 98 98 Magnesium (By similarity).
 BINDING 38 38 Substrate (By similarity).
 BINDING 73 73 Substrate (By similarity).
 BINDING 102 102 Substrate (By similarity).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 12 12 Phosphothreonine.
 MOD_RES 85 85 Phosphoserine.  

Keyword

 Acetylation; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 170 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0047840; F:dCTP diphosphatase activity; IEA:EC.
 GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
 GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:UniProtKB.
 GO:0032556; F:pyrimidine deoxyribonucleotide binding; IEA:Compara.
 GO:0009143; P:nucleoside triphosphate catabolic process; ISS:UniProtKB.
 GO:0051289; P:protein homotetramerization; IEA:Compara. 

Interpro

 IPR009039; EAR.
 IPR004518; MazG_cat. 

Pfam

 PF03819; MazG 

SMART

  

PROSITE

 PS50912; EAR 

PRINTS