CPLM-020348

Genbank Nucleotide ID

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; Putative oncogene protein hlc14-06-p

C20orf37; My049; OK/SW-cl.9

Homo sapiens (Human)

Position	Peptide	Type	References
8	MAASLVGKKIVFVTG	ubiquitination	[1]
9	AASLVGKKIVFVTGN	ubiquitination	[2, 3, 4, 5]
19	FVTGNAKKLEEVVQI	ubiquitination	[6]
30	VVQILGDKFPCTLVA	ubiquitination	[6]
56	PDEISIQKCQEAVRQ	ubiquitination	[1, 5, 6, 7]
96	KWFLEKLKPEGLHQL	ubiquitination	[2, 4]
169	QTYAEMPKAEKNAVS	ubiquitination	[6, 8]

[1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[2] 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]
[3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[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]
[5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[6] 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]
[7] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[8] 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]

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.

REGION 14 19 Substrate binding.
REGION 72 73 Substrate binding.
REGION 149 152 Substrate binding.
REGION 177 178 Substrate binding.
METAL 44 44 Magnesium.
METAL 72 72 Magnesium (By similarity).
BINDING 56 56 Substrate.
BINDING 172 172 Substrate.
MOD_RES 2 2 N-acetylalanine.

3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; Nucleotide-binding; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0035870; F:dITP diphosphatase activity; EXP:Reactome.
GO:0036220; F:ITP diphosphatase activity; EXP:Reactome.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO:0036222; F:XTP diphosphatase activity; EXP:Reactome.
GO:0051276; P:chromosome organization; IEA:Compara.
GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:HAMAP.
GO:0006193; P:ITP catabolic process; IEA:Compara.
GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome.

IPR002637; Ham1p-like.
IPR027502; ITPase.