UniProt Accession

 DUT_HUMAN; P33316; A8K650; B4DPR5; O14785; Q16708; Q16860; Q6FHN1; Q6NSA3; Q96Q81 

Genbank Protein ID

 U31930; U62891; AF018432; AF018429; AF018430; AF018431; AF018432; AF018429; AF018430; AF018431; U90223; U90224; U90224; AB049113; AY935242; AK291515; AK312122; CR541720; CR541781; CH471082; AK298464; BC033645; BC070339; BC110377; M89913; L11877 

Genbank Nucleotide ID

 AAC50418.1; AAC51123.1; AAB71393.1; AAB71393.1; AAB71393.1; AAB71393.1; AAB71394.1; AAB71394.1; AAB71394.1; AAB71394.1; AAB94642.1; AAB93866.1; AAB93867.1; BAB13724.1; AAX14045.1; BAF84204.1; BAG35058.1; CAG46521.1; CAG46580.1; EAW77350.1; BAG60677.1; AAH33645.1; AAH70339.1; AAI10378.1; AAA58444.1; AAA36801.1 

Protein Name

 Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial 

Protein Synonyms/Alias

 dUTPase; dUTP pyrophosphatase 

Gene Name

 DUT 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
179	PRSGLAAKHFIDVGA	acetylation	[1]
179	PRSGLAAKHFIDVGA	ubiquitination	[2, 3]
251	GGFGSTGKN******	acetylation	[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] 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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330] 

Functional Description

 This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. 

Sequence Annotation

 REGION 173 175 Substrate binding.
 REGION 187 190 Substrate binding.
 REGION 246 247 Substrate binding.
 BINDING 198 198 Substrate; via amide nitrogen and
 BINDING 241 241 Substrate (By similarity).
 MOD_RES 88 88 Phosphoserine.
 MOD_RES 179 179 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Hydrolase; Magnesium; Mitochondrion; Nucleotide metabolism; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 252 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; TAS:ProtInc.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0004170; F:dUTP diphosphatase activity; EXP:Reactome.
 GO:0006260; P:DNA replication; TAS:ProtInc.
 GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0046080; P:dUTP metabolic process; IEA:InterPro.
 GO:0006206; P:pyrimidine nucleobase metabolic process; TAS:Reactome.
 GO:0046134; P:pyrimidine nucleoside biosynthetic process; TAS:Reactome. 

Interpro

 IPR008180; dUTP_pyroPase.
 IPR008181; dUTP_pyroPase_sf. 

Pfam

 PF00692; dUTPase 

SMART

  

PROSITE

  

PRINTS