UniProt Accession

 NUDT5_HUMAN; Q9UKK9; A8K516; Q6IAG0; Q9UH49 

Genbank Protein ID

 AF155832; AF218818; AF161464; CR457195; AK291131; CH471072; BC000025 

Genbank Nucleotide ID

 AAF06734.1; AAF25479.1; AAF29079.1; CAG33476.1; BAF83820.1; EAW86322.1; AAH00025.1 

Protein Name

 ADP-sugar pyrophosphatase 

Protein Synonyms/Alias

 8-oxo-dGDP phosphatase; Nucleoside diphosphate-linked moiety X motif 5; Nudix motif 5; YSA1H 

Gene Name

 NUDT5 

Gene Synonyms/Alias

 HSPC115 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
42	TYMDPTGKTRTWESV	acetylation	[1]
42	TYMDPTGKTRTWESV	ubiquitination	[2]
55	SVKRTTRKEQTADGV	ubiquitination	[2]
175	VEVISLPKNDLLQRL	ubiquitination	[3, 4]
210	ALKHANAKPFEVPFL	acetylation	[1]
210	ALKHANAKPFEVPFL	ubiquitination	[2, 3, 4]
218	PFEVPFLKF******	acetylation	[1]
218	PFEVPFLKF******	ubiquitination	[2, 3, 4]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] 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]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional Description

 Hydrolyzes with similar activities ADP-ribose ADP- mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze other nucleotide sugars with low activity. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. 

Sequence Annotation

 DOMAIN 57 197 Nudix hydrolase.
 REGION 46 47 Substrate binding; shared with dimeric
 MOTIF 97 118 Nudix box.
 METAL 96 96 Magnesium 1; via carbonyl oxygen.
 METAL 112 112 Magnesium 2.
 METAL 112 112 Magnesium 3.
 METAL 116 116 Magnesium 1.
 METAL 116 116 Magnesium 3.
 METAL 166 166 Magnesium 3.
 BINDING 28 28 Substrate.
 BINDING 51 51 Substrate; shared with dimeric partner.
 BINDING 84 84 Substrate.
 BINDING 98 98 Substrate; via amide nitrogen.
 BINDING 133 133 Substrate.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 3 3 Phosphoserine.
 MOD_RES 9 9 Phosphoserine (By similarity).
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 74 74 Phosphotyrosine.
 MOD_RES 210 210 N6-acetyllysine.
 MOD_RES 218 218 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Hydrolase; Magnesium; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 219 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0047631; F:ADP-ribose diphosphatase activity; EXP:Reactome.
 GO:0019144; F:ADP-sugar diphosphatase activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0017110; F:nucleoside-diphosphatase activity; IEA:Compara.
 GO:0030515; F:snoRNA binding; ISS:UniProtKB.
 GO:0019303; P:D-ribose catabolic process; NAS:UniProtKB.
 GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome.
 GO:0009117; P:nucleotide metabolic process; NAS:ProtInc.
 GO:0009191; P:ribonucleoside diphosphate catabolic process; IDA:UniProtKB. 

Interpro

 IPR020476; Nudix_hydrolase.
 IPR020084; NUDIX_hydrolase_CS.
 IPR000086; NUDIX_hydrolase_dom.
 IPR015797; NUDIX_hydrolase_dom-like. 

Pfam

 PF00293; NUDIX 

SMART

  

PROSITE

 PS51462; NUDIX
 PS00893; NUDIX_BOX 

PRINTS

 PR00502; NUDIXFAMILY.