General Information of Target

Target ID LDTP09213
Target Name Diphosphoinositol polyphosphate phosphohydrolase 3-alpha (NUDT10)
Gene Name NUDT10
Gene ID 170685
Synonyms
APS2; DIPP3A; Diphosphoinositol polyphosphate phosphohydrolase 3-alpha; DIPP-3-alpha; DIPP3-alpha; hDIPP3alpha; EC 3.6.1.52; Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha; Diadenosine hexaphosphate hydrolase; AMP-forming); EC 3.6.1.60; Nucleoside diphosphate-linked moiety X motif 10; Nudix motif 10; hAps2
3D Structure
Download
2D Sequence (FASTA)
Download
3D Structure (PDB)
Download
Sequence
MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPGG
AAVREVYEEAGVKGKLGRLLGVFEQNQDPKHRTYVYVLTVTELLEDWEDSVSIGRKREWF
KVEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSMAPSSPDSDP
Target Bioclass
Enzyme
Family
Nudix hydrolase family, DIPP subfamily
Subcellular location
Cytoplasm
Function
Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.
Uniprot ID
Q8NFP7
Ensemble ID
ENST00000356450.3
HGNC ID
HGNC:17621
ChEMBL ID
CHEMBL4295904

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 19 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
TH211
 Probe Info 
Y67(15.61); Y11(11.97)  LDD0257  [1]
STPyne
 Probe Info 
K133(20.00)  LDD2217  [2]
Probe 1
 Probe Info 
Y67(48.83)  LDD3495  [3]
m-APA
 Probe Info 
10.72  LDD0403  [4]
BTD
 Probe Info 
C131(1.10)  LDD2094  [5]
AHL-Pu-1
 Probe Info 
C131(4.91)  LDD0168  [6]
HHS-475
 Probe Info 
Y67(0.77)  LDD0264  [7]
Acrolein
 Probe Info 
N.A.  LDD0222  [8]
4-Iodoacetamidophenylacetylene
 Probe Info 
C3(0.00); C131(0.00)  LDD0038  [9]
IA-alkyne
 Probe Info 
C3(0.00); C131(0.00)  LDD0036  [9]
Lodoacetamide azide
 Probe Info 
C3(0.00); C131(0.00)  LDD0037  [9]
ENE
 Probe Info 
N.A.  LDD0006  [10]
IPM
 Probe Info 
N.A.  LDD0005  [10]
NPM
 Probe Info 
N.A.  LDD0016  [10]
TFBX
 Probe Info 
C24(0.00); C131(0.00)  LDD0148  [11]
VSF
 Probe Info 
N.A.  LDD0007  [10]
Phosphinate-6
 Probe Info 
C3(0.00); C131(0.00)  LDD0018  [12]
AOyne
 Probe Info 
15.00  LDD0443  [13]
HHS-465
 Probe Info 
N.A.  LDD2240  [14]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0025  4SU-RNA HEK-293T C131(4.91)  LDD0168  [6]
 LDCM0026  4SU-RNA+native RNA HEK-293T C131(8.65)  LDD0169  [6]
 LDCM0156  Aniline NCI-H1299 10.72  LDD0403  [4]
 LDCM0108  Chloroacetamide HeLa N.A.  LDD0222  [8]
 LDCM0213  Electrophilic fragment 2 MDA-MB-231 C22(1.42); C24(1.42)  LDD1702  [5]
 LDCM0116  HHS-0101 DM93 Y67(0.77)  LDD0264  [7]
 LDCM0117  HHS-0201 DM93 Y67(0.82)  LDD0265  [7]
 LDCM0118  HHS-0301 DM93 Y67(0.74)  LDD0266  [7]
 LDCM0119  HHS-0401 DM93 Y67(1.07)  LDD0267  [7]
 LDCM0120  HHS-0701 DM93 Y67(0.90)  LDD0268  [7]
 LDCM0023  KB03 MDA-MB-231 C24(2.21)  LDD1701  [5]
 LDCM0501  Nucleophilic fragment 13b MDA-MB-231 C131(1.10)  LDD2094  [5]
 LDCM0516  Nucleophilic fragment 21a MDA-MB-231 C131(1.06)  LDD2109  [5]
 LDCM0526  Nucleophilic fragment 26a MDA-MB-231 C131(1.75)  LDD2119  [5]
 LDCM0527  Nucleophilic fragment 26b MDA-MB-231 C22(0.87)  LDD2120  [5]
 LDCM0530  Nucleophilic fragment 28a MDA-MB-231 C131(0.94)  LDD2123  [5]
 LDCM0532  Nucleophilic fragment 29a MDA-MB-231 C131(0.99)  LDD2125  [5]
 LDCM0542  Nucleophilic fragment 37 MDA-MB-231 C24(0.90)  LDD2135  [5]
 LDCM0544  Nucleophilic fragment 39 MDA-MB-231 C131(1.10); C24(1.03)  LDD2137  [5]
 LDCM0549  Nucleophilic fragment 43 MDA-MB-231 C24(0.94)  LDD2143  [5]
 LDCM0550  Nucleophilic fragment 5a MDA-MB-231 C24(1.01)  LDD2144  [5]
 LDCM0556  Nucleophilic fragment 8a MDA-MB-231 C131(0.37)  LDD2150  [5]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Enzyme
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
E3 ubiquitin-protein ligase TRIM8 (TRIM8) TRIM/RBCC family Q9BZR9
Transcription factor
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Transcription factor 4 (TCF4) . P15884
Other
Click To Hide/Show 4 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Microtubule-associated tumor suppressor candidate 2 (MTUS2) MTUS1 family Q5JR59
Heat shock factor 2-binding protein (HSF2BP) . O75031
PDZ and LIM domain protein 7 (PDLIM7) . Q9NR12
snRNA-activating protein complex subunit 5 (SNAPC5) . O75971

References

1 Chemoproteomic profiling of kinases in live cells using electrophilic sulfonyl triazole probes. Chem Sci. 2021 Jan 21;12(9):3295-3307. doi: 10.1039/d0sc06623k.
2 Global profiling of lysine reactivity and ligandability in the human proteome. Nat Chem. 2017 Dec;9(12):1181-1190. doi: 10.1038/nchem.2826. Epub 2017 Jul 31.
3 An Azo Coupling-Based Chemoproteomic Approach to Systematically Profile the Tyrosine Reactivity in the Human Proteome. Anal Chem. 2021 Jul 27;93(29):10334-10342. doi: 10.1021/acs.analchem.1c01935. Epub 2021 Jul 12.
4 Quantitative and Site-Specific Chemoproteomic Profiling of Targets of Acrolein. Chem Res Toxicol. 2019 Mar 18;32(3):467-473. doi: 10.1021/acs.chemrestox.8b00343. Epub 2019 Jan 15.
5 Nucleophilic covalent ligand discovery for the cysteine redoxome. Nat Chem Biol. 2023 Nov;19(11):1309-1319. doi: 10.1038/s41589-023-01330-5. Epub 2023 May 29.
Mass spectrometry data entry: PXD039908 , PXD029761
6 Chemoproteomic capture of RNA binding activity in living cells. Nat Commun. 2023 Oct 7;14(1):6282. doi: 10.1038/s41467-023-41844-z.
Mass spectrometry data entry: PXD044625
7 Discovery of a Cell-Active SuTEx Ligand of Prostaglandin Reductase 2. Chembiochem. 2021 Jun 15;22(12):2134-2139. doi: 10.1002/cbic.202000879. Epub 2021 Apr 29.
8 ACR-Based Probe for the Quantitative Profiling of Histidine Reactivity in the Human Proteome. J Am Chem Soc. 2023 Mar 8;145(9):5252-5260. doi: 10.1021/jacs.2c12653. Epub 2023 Feb 27.
9 Enhancing Cysteine Chemoproteomic Coverage through Systematic Assessment of Click Chemistry Product Fragmentation. Anal Chem. 2022 Mar 8;94(9):3800-3810. doi: 10.1021/acs.analchem.1c04402. Epub 2022 Feb 23.
Mass spectrometry data entry: PXD028853
10 A modification-centric assessment tool for the performance of chemoproteomic probes. Nat Chem Biol. 2022 Aug;18(8):904-912. doi: 10.1038/s41589-022-01074-8. Epub 2022 Jul 21.
Mass spectrometry data entry: PXD027758 , PXD027755 , PXD027760 , PXD027762 , PXD027756 , PXD027591 , PXD007149 , PXD030064 , PXD032392 , PXD027789 , PXD027767 , PXD027764
11 Chemoproteomic Profiling by Cysteine Fluoroalkylation Reveals Myrocin G as an Inhibitor of the Nonhomologous End Joining DNA Repair Pathway. J Am Chem Soc. 2021 Dec 8;143(48):20332-20342. doi: 10.1021/jacs.1c09724. Epub 2021 Nov 24.
Mass spectrometry data entry: PXD029255
12 DFT-Guided Discovery of Ethynyl-Triazolyl-Phosphinates as Modular Electrophiles for Chemoselective Cysteine Bioconjugation and Profiling. Angew Chem Int Ed Engl. 2022 Oct 10;61(41):e202205348. doi: 10.1002/anie.202205348. Epub 2022 Aug 22.
Mass spectrometry data entry: PXD033004
13 Chemoproteomic profiling of targets of lipid-derived electrophiles by bioorthogonal aminooxy probe. Redox Biol. 2017 Aug;12:712-718. doi: 10.1016/j.redox.2017.04.001. Epub 2017 Apr 5.
14 Global profiling identifies a stress-responsive tyrosine site on EDC3 regulating biomolecular condensate formation. Cell Chem Biol. 2022 Dec 15;29(12):1709-1720.e7. doi: 10.1016/j.chembiol.2022.11.008. Epub 2022 Dec 6.
Mass spectrometry data entry: PXD038010