NUDT5

General Information

Full gene name:nudix (nucleoside diphosphate linked moiety X)-type motif 5 Entrez Gene ID:11164 Location:10p14 Synonyms:YSA1H, hYSAH1, YSA1 Type:protein-coding

User SNPs

SNPs given by the user that are near or inside this gene:

SNP	Distance (bp)	Direction
rs12779790	89867	upstream

NCBI Summary

Nudix hydrolases, such as NUDT5, eliminate toxic nucleotide derivatives from the cell and regulate the levels of important signaling nucleotides and their metabolites (McLennan, 1999 [PubMed 10373642]).[supplied by OMIM, Mar 2008]

OMIM

OMIM ID:`OMIM ID 609230 `_

NCBI Phenotypes

No phenotypes found linked to this gene.

Gene Ontology

• D-ribose catabolic process
• ribonucleoside diphosphate catabolic process
• magnesium ion binding
• nucleoside-diphosphatase activity
• nucleotide metabolic process
• ADP-ribose diphosphatase activity
• intracellular
• ADP-sugar diphosphatase activity

KEGG Pathways

• Purine metabolism

GeneRIFs

• human MTH1, MTH2, and NUDT5 proteins act as a defense against the mutagenesis induced by oxidized dGTP. [PMID 20144704]
• The broad substrate specificity of hNUDT5 is achieved by a diversity of not only substrate recognition, but also hydrolysis mechanisms. [PMID 21768126]
• NUDT5 protein eliminates various oxidized deoxyribonucleoside diphosphates from the nucleotide pool and prevents their toxic effects. [PMID 19699693]
• Results report the crystal structure of hNUDT5 in complex with a non-hydrolyzable ADPR analogue, alpha,beta-methyleneadenosine diphosphoribose, and three Mg(2+) ions representing the transition state of the enzyme during catalysis. [PMID 18462755]
• The human NUDT5, which has an intrinsic activity to cleave ADP sugars to AMP and sugar phosphate, possesses the ability to degrade 8-oxo-dGDP to the monophosphate. [PMID 21389046]
• degrades 8-oxo-dGDP to 8-oxo-dGMP, an unusable form for DNA synthesis, and promotes the cleavage of 8-oxo-dGTP by MTH1 to yield 8-oxo-dGMP also [PMID 12717453]
• Two-hybrid [PMID 21900206]
• Two-hybrid [PMID 21900206]
• Affinity Capture-MS [PMID 20360068]
• Results suggest that the NUDT5 protein may play significant roles in regulating the G1-S transition in HeLa cells. [PMID 22200976]
• Affinity Capture-MS [PMID 21906983]
• Two-hybrid [PMID 16169070]

PubMed Articles

Recent articles:

• Zhang LQ et al. “Lowered nudix type 5 (NUDT5) expression leads to cell cycle retardation in HeLa cells.” Mol Cell Biochem. 2012 Apr;363(1-2):377-84. PMID 22200976
• Arimori T et al. “Diverse substrate recognition and hydrolysis mechanisms of human NUDT5.” Nucleic Acids Res. 2011 Nov 1;39(20):8972-83. PMID 21768126
• Kim W et al. “Systematic and quantitative assessment of the ubiquitin-modified proteome.” Mol Cell. 2011 Oct 21;44(2):325-40. PMID 21906983
• Wagner SA et al. “A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.” Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. PMID 21890473
• Vinayagam A et al. “A directed protein interaction network for investigating intracellular signal transduction.” Sci Signal. 2011 Sep 6;4(189):rs8. PMID 21900206
• Ito R et al. “Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5 protein.” J Biochem. 2011 Jun;149(6):731-8. PMID 21389046
• Danielsen JM et al. “Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.” Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. PMID 21139048
• Hori M et al. “Suppression of mutagenesis by 8-hydroxy-2’-deoxyguanosine 5’-triphosphate (7,8-dihydro-8-oxo-2’-deoxyguanosine 5’-triphosphate) by human MTH1, MTH2, and NUDT5.” Free Radic Biol Med. 2010 May 1;48(9):1197-201. PMID 20144704
• Hutchins JR et al. “Systematic analysis of human protein complexes identifies chromosome segregation proteins.” Science. 2010 Apr 30;328(5978):593-9. PMID 20360068
• Kamiya H et al. “NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with broad substrate specificity.” DNA Repair (Amst). 2009 Oct 2;8(10):1250-4. PMID 19699693

Top Pubmed articles linked to gene NUDT5 matching any search term:

• Gasmi L et al. “Cloning, expression and characterization of YSA1H, a human adenosine 5’-diphosphosugar pyrophosphatase possessing a MutT motif.” Biochem J. 1999 Dec 1;344 Pt 2:331-7. PMID 10567213