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Protein

7,8-dihydro-8-oxoguanine triphosphatase

Gene

Nudt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Antimutagenic. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA.1 Publication

Catalytic activityi

8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate.1 Publication
2-hydroxy-dATP + H2O = 2-hydroxy-dAMP + diphosphate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Enzyme regulationi

2-hydroxy-dATPase activity is inhibited by 2-OH-dADP, 8-OH-dGDP and 8-OH-dGTP. 8-OH-dGTPase activity is inhibited by 8-OH-dGDP, 2-OH-dADP and 2-OH-dATP (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei8Substrate; via carbonyl oxygenBy similarity1
Binding sitei27SubstrateBy similarity1
Sitei27Important for 2-OH-dATPase and 8-oxo-dGTPase activitiesBy similarity1
Binding sitei33SubstrateBy similarity1
Metal bindingi37Magnesium; via carbonyl oxygenBy similarity1
Metal bindingi52MagnesiumBy similarity1
Metal bindingi55MagnesiumBy similarity1
Metal bindingi56MagnesiumBy similarity1
Sitei117Essential for 2-OH-dATPase and 8-oxo-dGTPase activitiesBy similarity1
Sitei119Essential for 2-OH-dATPase activity and important for 8-oxo-dGTPase activityBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BRENDAi3.6.1.56. 3474.
ReactomeiR-MMU-2393930. Phosphate bond hydrolysis by NUDT proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
7,8-dihydro-8-oxoguanine triphosphatase (EC:3.6.1.55)
Alternative name(s):
2-hydroxy-dATP diphosphatase (EC:3.6.1.56)
8-oxo-dGTPase
Nucleoside diphosphate-linked moiety X motif 1
Short name:
Nudix motif 1
Gene namesi
Name:Nudt1
Synonyms:Mth1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:109280. Nudt1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant mice appear normal, but have higher incidence of tumors in lung, liver and stomach.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000005710021 – 1567,8-dihydro-8-oxoguanine triphosphataseAdd BLAST136

Proteomic databases

EPDiP53368.
PaxDbiP53368.
PRIDEiP53368.

PTM databases

iPTMnetiP53368.
PhosphoSitePlusiP53368.

Expressioni

Tissue specificityi

High expression levels detected in thymus, liver, spleen, kidney, testis and large intestine, with lower levels detected in brain, heart, lung and stomach (at protein level). Expressed in kidney, liver and small intestine.1 Publication

Gene expression databases

BgeeiENSMUSG00000036639.
ExpressionAtlasiP53368. baseline and differential.
GenevisibleiP53368. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059983.

Structurei

3D structure databases

ProteinModelPortaliP53368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 132Nudix hydrolasePROSITE-ProRule annotationAdd BLAST112

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni35 – 38Substrate bindingBy similarity4
Regioni117 – 120Substrate bindingBy similarity4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi37 – 58Nudix boxAdd BLAST22

Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IXIA. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000000341.
HOGENOMiHOG000261970.
HOVERGENiHBG000032.
InParanoidiP53368.
KOiK17816.
OMAiGAGKWNG.
OrthoDBiEOG091G0O4Y.
PhylomeDBiP53368.
TreeFamiTF106348.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003563. OxG-triPHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01403. 8OXTPHPHTASE.
PR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53368-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSRLYTLV LVLQPQRVLL GMKKRGFGAG RWNGFGGKVQ EGETIEDGAK
60 70 80 90 100
RELLEESGLS VDTLHKVGHI SFEFVGSPEL MDVHIFSADH VHGTPTESEE
110 120 130 140 150
MRPQWFQLDQ IPFADLWPDD SYWFPLLLQK KKFCGHFKFQ DQDTILSYSL

REVDSF
Length:156
Mass (Da):17,908
Last modified:October 1, 1996 - v1
Checksum:i9E6C12EC2A6DE4B7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti116L → M in AAH21940 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49956 mRNA. Translation: BAA08711.1.
D88356 Genomic DNA. Translation: BAA19866.1.
AK011695 mRNA. Translation: BAB27785.1.
AK088309 mRNA. Translation: BAC40274.1.
AK168312 mRNA. Translation: BAE40252.1.
CH466529 Genomic DNA. Translation: EDL19122.1.
CH466529 Genomic DNA. Translation: EDL19123.1.
BC021940 mRNA. Translation: AAH21940.1.
BC098239 mRNA. Translation: AAH98239.1.
CCDSiCCDS19818.1.
PIRiI49446.
RefSeqiNP_032663.1. NM_008637.1.
XP_006504718.1. XM_006504655.2.
XP_006504719.1. XM_006504656.2.
XP_006504720.1. XM_006504657.2.
UniGeneiMm.118846.

Genome annotation databases

EnsembliENSMUST00000050205; ENSMUSP00000059983; ENSMUSG00000036639.
ENSMUST00000071881; ENSMUSP00000071778; ENSMUSG00000036639.
ENSMUST00000110826; ENSMUSP00000106450; ENSMUSG00000036639.
ENSMUST00000110827; ENSMUSP00000106451; ENSMUSG00000036639.
GeneIDi17766.
KEGGimmu:17766.
UCSCiuc009ahn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49956 mRNA. Translation: BAA08711.1.
D88356 Genomic DNA. Translation: BAA19866.1.
AK011695 mRNA. Translation: BAB27785.1.
AK088309 mRNA. Translation: BAC40274.1.
AK168312 mRNA. Translation: BAE40252.1.
CH466529 Genomic DNA. Translation: EDL19122.1.
CH466529 Genomic DNA. Translation: EDL19123.1.
BC021940 mRNA. Translation: AAH21940.1.
BC098239 mRNA. Translation: AAH98239.1.
CCDSiCCDS19818.1.
PIRiI49446.
RefSeqiNP_032663.1. NM_008637.1.
XP_006504718.1. XM_006504655.2.
XP_006504719.1. XM_006504656.2.
XP_006504720.1. XM_006504657.2.
UniGeneiMm.118846.

3D structure databases

ProteinModelPortaliP53368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059983.

PTM databases

iPTMnetiP53368.
PhosphoSitePlusiP53368.

Proteomic databases

EPDiP53368.
PaxDbiP53368.
PRIDEiP53368.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000050205; ENSMUSP00000059983; ENSMUSG00000036639.
ENSMUST00000071881; ENSMUSP00000071778; ENSMUSG00000036639.
ENSMUST00000110826; ENSMUSP00000106450; ENSMUSG00000036639.
ENSMUST00000110827; ENSMUSP00000106451; ENSMUSG00000036639.
GeneIDi17766.
KEGGimmu:17766.
UCSCiuc009ahn.1. mouse.

Organism-specific databases

CTDi4521.
MGIiMGI:109280. Nudt1.

Phylogenomic databases

eggNOGiENOG410IXIA. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000000341.
HOGENOMiHOG000261970.
HOVERGENiHBG000032.
InParanoidiP53368.
KOiK17816.
OMAiGAGKWNG.
OrthoDBiEOG091G0O4Y.
PhylomeDBiP53368.
TreeFamiTF106348.

Enzyme and pathway databases

BRENDAi3.6.1.56. 3474.
ReactomeiR-MMU-2393930. Phosphate bond hydrolysis by NUDT proteins.

Miscellaneous databases

PROiP53368.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000036639.
ExpressionAtlasiP53368. baseline and differential.
GenevisibleiP53368. MM.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003563. OxG-triPHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01403. 8OXTPHPHTASE.
PR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei8ODP_MOUSE
AccessioniPrimary (citable) accession number: P53368
Secondary accession number(s): P97795, Q542J4, Q8VDG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.