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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Substrate; via carbonyl oxygenBy similarity
Binding sitei27 – 271SubstrateBy similarity
Sitei27 – 271Important for 2-OH-dATPase and 8-oxo-dGTPase activitiesBy similarity
Binding sitei33 – 331SubstrateBy similarity
Metal bindingi37 – 371Magnesium; via carbonyl oxygenBy similarity
Metal bindingi52 – 521MagnesiumBy similarity
Metal bindingi55 – 551MagnesiumBy similarity
Metal bindingi56 – 561MagnesiumBy similarity
Sitei117 – 1171Essential for 2-OH-dATPase and 8-oxo-dGTPase activitiesBy similarity
Sitei119 – 1191Essential for 2-OH-dATPase activity and important for 8-oxo-dGTPase activityBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 1561367,8-dihydro-8-oxoguanine triphosphatasePRO_0000057100Add
BLAST

Proteomic databases

EPDiP53368.
PaxDbiP53368.
PRIDEiP53368.

PTM databases

iPTMnetiP53368.
PhosphoSiteiP53368.

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

BgeeiP53368.
ExpressionAtlasiP53368. baseline and differential.
GenevisibleiP53368. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059983.

Structurei

3D structure databases

ProteinModelPortaliP53368.
SMRiP53368. Positions 4-155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 132112Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 384Substrate bindingBy similarity
Regioni117 – 1204Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi37 – 5822Nudix boxAdd
BLAST

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.
OrthoDBiEOG7BS4BT.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161L → M in AAH21940 (PubMed:15489334).Curated

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.
SMRiP53368. Positions 4-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059983.

PTM databases

iPTMnetiP53368.
PhosphoSiteiP53368.

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.
OrthoDBiEOG7BS4BT.
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

BgeeiP53368.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse MTH1 protein with 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphatase activity that prevents transversion mutation. cDNA cloning and tissue distribution."
    Kakuma T., Nishida J., Tsuzuki T., Sekiguchi M.
    J. Biol. Chem. 270:25942-25948(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Strain: 129/Sv.
    Tissue: Embryonic stem cell.
  2. "Organization and expression of the mouse MTH1 gene for preventing transversion mutation."
    Igarashi H., Tsuzuki T., Kakuma T., Tominaga Y., Sekiguchi M.
    J. Biol. Chem. 272:3766-3772(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
    Tissue: Embryonic stem cell.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J, DBA/2J and NOD.
    Tissue: Embryo and Thymus.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland and Mammary tumor.
  6. Cited for: DISRUPTION PHENOTYPE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Multiple mRNA decapping enzymes in mammalian cells."
    Song M.G., Li Y., Kiledjian M.
    Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ABSENCE OF FUNCTION AS A DECAPPING ENZYME, RNA-BINDING.

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: June 8, 2016
This is version 116 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.