CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022650
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 dCTP pyrophosphatase 1 
Protein Synonyms/Alias
 Deoxycytidine-triphosphatase 1; dCTPase 1; RS21-C6; XTP3-transactivated gene A protein homolog 
Gene Name
 Dctpp1 
Gene Synonyms/Alias
 Tdrg-TL1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
140LSRGSACKYTDLPRGacetylation[1, 2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
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. 
Sequence Annotation
 REPEAT 29 75 EAR.
 REGION 47 51 Substrate binding.
 METAL 63 63 Magnesium (Probable).
 METAL 66 66 Magnesium (Probable).
 METAL 95 95 Magnesium (Probable).
 METAL 98 98 Magnesium (Probable).
 BINDING 38 38 Substrate.
 BINDING 73 73 Substrate.
 BINDING 102 102 Substrate.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 2 2 Phosphoserine (By similarity).  
Keyword
 3D-structure; 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
MSTAGDGERG TVGQEDSAAA RPFRFSPEPT LEDIRRLHAE FAAERDWEQF HQPRNLLLAL 60
VGEVGELAEL FQWKSDTEPG PQAWPPKERA ALQEELSDVL IYLVALAARC HVDLPQAVIS 120
KMDTNRQRYP VHLSRGSACK YTDLPRGTIS ENQAVGAGDP ASELRDQAST 170 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0047840; F:dCTP diphosphatase activity; IEA:EC.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IDA:UniProtKB.
 GO:0032556; F:pyrimidine deoxyribonucleotide binding; IDA:MGI.
 GO:0009143; P:nucleoside triphosphate catabolic process; IDA:UniProtKB.
 GO:0051289; P:protein homotetramerization; IDA:MGI. 
Interpro
 IPR009039; EAR.
 IPR004518; MazG_cat. 
Pfam
 PF03819; MazG 
SMART
  
PROSITE
 PS50912; EAR 
PRINTS