CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020865
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inosine triphosphate pyrophosphatase 
Protein Synonyms/Alias
 ITPase; Inosine triphosphatase; Non-canonical purine NTP pyrophosphatase; Non-standard purine NTP pyrophosphatase; Nucleoside-triphosphate diphosphatase; Nucleoside-triphosphate pyrophosphatase; NTPase 
Gene Name
 Itpa 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
9AASLVGKKIVFVTGNacetylation[1]
56PDEISIQKCREAARQubiquitination[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] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. 
Sequence Annotation
 REGION 14 19 Substrate binding (By similarity).
 REGION 72 73 Substrate binding (By similarity).
 REGION 149 152 Substrate binding (By similarity).
 REGION 177 178 Substrate binding (By similarity).
 METAL 44 44 Magnesium or manganese (By similarity).
 METAL 72 72 Magnesium or manganese (By similarity).
 BINDING 56 56 Substrate (By similarity).
 BINDING 172 172 Substrate (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 198 AA 
Protein Sequence
MAASLVGKKI VFVTGNAKKL EEVIQILGDN FPCTLEAQKI DLPEYQGEPD EISIQKCREA 60
ARQVQGPVLV EDTCLCFNAL GGLPGPYIKW FLQKLKPEGL HQLLAGFEDK SAYALCTFAL 120
STGDPSQPVL LFRGQTSGQI VMPRGSRDFG WDPCFQPDGY EQTYAEMPKS EKNTISHRFR 180
ALHKLQEYFS VAAGAGDH 198 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0035870; F:dITP diphosphatase activity; IMP:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0051276; P:chromosome organization; IMP:MGI.
 GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:HAMAP.
 GO:0006193; P:ITP catabolic process; IMP:MGI. 
Interpro
 IPR002637; Ham1p-like.
 IPR027502; ITPase. 
Pfam
 PF01725; Ham1p_like 
SMART
  
PROSITE
  
PRINTS