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Identification
HMDB Protein ID HMDBP08775
Secondary Accession Numbers
  • 14498
Name Diphosphoinositol polyphosphate phosphohydrolase 3-alpha
Synonyms
  1. DIPP-3-alpha
  2. DIPP3-alpha
  3. Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha
  4. Nucleoside diphosphate-linked moiety X motif 10
  5. Nudix motif 10
  6. hAps2
  7. hDIPP3alpha
  8. Diadenosine hexaphosphate hydrolase (AMP-forming)
Gene Name NUDT10
Protein Type Unknown
Biological Properties
General Function Involved in hydrolase activity
Specific 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.
Pathways Not Available
Reactions
Diphospho-myo-inositol polyphosphate + Water → myo-inositol polyphosphate + Phosphate details
Diadenosine hexaphosphate + Water → Adenosine 5'-pentaphosphate + Adenosine monophosphate details
P(1),P(5)-bis(5'-adenosyl)pentaphosphate + Water → Adenosine tetraphosphate + Adenosine monophosphate details
GO Classification
Cellular Component
cytoplasm
Function
catalytic activity
hydrolase activity
Molecular Function
diphosphoinositol-polyphosphate diphosphatase activity
inositol diphosphate tetrakisphosphate diphosphatase activity
inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity
inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity
inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity
inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity
inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity
inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity
metal ion binding
Cellular Location
  1. Cytoplasm (Probable)
Gene Properties
Chromosome Location X
Locus Xp11.23
SNPs NUDT10
Gene Sequence
>495 bp
ATGAAGTGCAAACCCAACCAGACACGGACCTACGACCCCGAGGGGTTCAAGAAGCGGGCG
GCGTGCCTGTGCTTCCGGAGCGAGCGCGAGGACGAGGTCCTGTTAGTGAGTAGCAGCCGG
TACCCGGACCGCTGGATCGTGCCGGGCGGGGGCATGGAGCCCGAGGAGGAGCCGGGCGGT
GCGGCGGTCCGAGAGGTGTACGAAGAGGCGGGAGTCAAGGGGAAGTTAGGCCGGCTCCTG
GGCGTCTTCGAACAGAACCAGGACCCCAAGCACAGAACGTACGTGTATGTACTGACTGTC
ACGGAGCTGCTGGAGGATTGGGAAGATTCGGTTAGCATTGGGAGGAAGCGAGAGTGGTTC
AAAGTCGAAGATGCCATCAAGGTTCTCCAGTGCCACAAGCCCGTGCACGCCGAATATCTG
GAGAAACTAAAGCTGGGCGGTTCCCCAACCAATGGAAACTCCATGGCCCCATCCTCGCCA
GATAGCGATCCCTAG
Protein Properties
Number of Residues 164
Molecular Weight 18499.765
Theoretical pI 5.678
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Diphosphoinositol polyphosphate phosphohydrolase 3-alpha
MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPGG
AAVREVYEEAGVKGKLGRLLGVFEQNQDPKHRTYVYVLTVTELLEDWEDSVSIGRKREWF
KVEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSMAPSSPDSDP
GenBank ID Protein 21591549
UniProtKB/Swiss-Prot ID Q8NFP7
UniProtKB/Swiss-Prot Entry Name NUD10_HUMAN
PDB IDs
GenBank Gene ID AF469196
GeneCard ID NUDT10
GenAtlas ID NUDT10
HGNC ID HGNC:17621
References
General References
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  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
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  5. Hidaka K, Caffrey JJ, Hua L, Zhang T, Falck JR, Nickel GC, Carrel L, Barnes LD, Shears SB: An adjacent pair of human NUDT genes on chromosome X are preferentially expressed in testis and encode two new isoforms of diphosphoinositol polyphosphate phosphohydrolase. J Biol Chem. 2002 Sep 6;277(36):32730-8. Epub 2002 Jun 24. [PubMed:12105228 ]
  6. Leslie NR, McLennan AG, Safrany ST: Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases. BMC Biochem. 2002 Jul 16;3:20. [PubMed:12121577 ]
  7. Fisher DI, Safrany ST, Strike P, McLennan AG, Cartwright JL: Nudix hydrolases that degrade dinucleoside and diphosphoinositol polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP) pyrophosphatase activity that generates the glycolytic activator ribose 1,5-bisphosphate. J Biol Chem. 2002 Dec 6;277(49):47313-7. Epub 2002 Oct 4. [PubMed:12370170 ]