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Protein

7,8-dihydro-8-oxoguanine triphosphatase

Gene

NUDT1

Organism
Homo sapiens (Human)
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.5 Publications

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

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.1 Publication

Kineticsi

The kinetic constants are determined for the recombinant enzyme expressed in E.coli. 2-hydroxy-rATP shows the best catalytic efficiency.

  1. KM=8.3 µM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 8.0, PubMed:11139615)3 Publications
  2. KM=5.7 µM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 7.2, PubMed:11139615)3 Publications
  3. KM=4.3 µM for 2-hydroxy-rATP (at 30 degrees Celsius and pH 8.0, PubMed:11139615)3 Publications
  4. KM=13.9 µM for 8-hydroxy-dATP (at 30 degrees Celsius and pH 8.0, PubMed:11139615)3 Publications
  5. KM=51.0 µM for 8-hydroxy-rATP (at 30 degrees Celsius and pH 8.0, PubMed:11139615)3 Publications
  6. KM=15.2 µM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 8.0, PubMed:11139615)3 Publications
  7. KM=12.8 µM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 7.2, PubMed:11139615)3 Publications
  8. KM=13.2 µM for 8-hydroxy-dGTP (at 22 degrees Celsius and pH 7.5, PubMed:21787772)3 Publications
  9. KM=55.0 µM for 8-hydroxy-rGTP (at 30 degrees Celsius and pH 8.0, PubMed:11139615)3 Publications
  10. KM=258 µM for dGTP (at 30 degrees Celsius and pH 8.0, PubMed:11139615)3 Publications

    pH dependencei

    Optimum pH is 7.8-8.2 with 8-hydroxy-dGTP as substrate, and 8.0-8.5 with 2-hydroxy-dATP as substrate.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491Substrate; via carbonyl oxygen
    Binding sitei68 – 681Substrate
    Sitei68 – 681Important for 2-OH-dATPase and 8-oxo-dGTPase activities
    Binding sitei74 – 741Substrate
    Metal bindingi78 – 781Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi93 – 931MagnesiumBy similarity
    Metal bindingi96 – 961MagnesiumBy similarity
    Metal bindingi97 – 971MagnesiumBy similarity
    Sitei158 – 1581Essential for 2-OH-dATPase and 8-oxo-dGTPase activities
    Sitei160 – 1601Essential for 2-OH-dATPase activity and important for 8-oxo-dGTPase activity

    GO - Molecular functioni

    GO - Biological processi

    • dATP catabolic process Source: UniProtKB
    • dGTP catabolic process Source: UniProtKB
    • DNA protection Source: UniProtKB
    • DNA repair Source: UniProtKB
    • nucleobase-containing small molecule catabolic process Source: Reactome
    • purine nucleotide catabolic process Source: UniProtKB
    • response to oxidative stress Source: ProtInc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02879-MONOMER.
    BRENDAi3.6.1.55. 2681.
    3.6.1.56. 2681.
    ReactomeiR-HSA-2393930. Phosphate bond hydrolysis by NUDT proteins.
    SABIO-RKP36639.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:8048. NUDT1.

    Subcellular locationi

    Isoform p18 :

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • mitochondrial matrix Source: UniProtKB
    • mitochondrion Source: UniProtKB
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi68 – 681F → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities. 1 Publication
    Mutagenesisi77 – 771G → R: Reduces activity by 97%. 1 Publication
    Mutagenesisi78 – 781G → F: Loss of activity. 1 Publication
    Mutagenesisi80 – 801V → E: Loss of activity. 1 Publication
    Mutagenesisi81 – 811Q → P: Reduces activity by 97%. 1 Publication
    Mutagenesisi83 – 831G → I: Reduces activity by 60%. 1 Publication
    Mutagenesisi86 – 861I → K: Loss of activity. 1 Publication
    Mutagenesisi88 – 881D → P: Loss of activity. 1 Publication
    Mutagenesisi89 – 891G → M: Loss of activity. 1 Publication
    Mutagenesisi90 – 901A → P: Loss of activity. 1 Publication
    Mutagenesisi94 – 941L → P: Loss of activity. 1 Publication
    Mutagenesisi95 – 951Q → P: Loss of activity. 1 Publication
    Mutagenesisi96 – 961E → G: Loss of activity. 1 Publication
    Mutagenesisi97 – 971E → Y: Loss of activity. 1 Publication
    Mutagenesisi98 – 981S → R: Loss of activity. 1 Publication
    Mutagenesisi158 – 1581W → A: Greatly reduces or abolishes 2-OH-dATPase and 8-oxo-dGTPase activities. 1 Publication
    Mutagenesisi158 – 1581W → Y: Enhances 2-OH-dATPase activity and greatly reduces 8-oxo-dGTPase activity. 1 Publication
    Mutagenesisi160 – 1601D → A or N: Loss of 2-OH-dATPase activity, reduces 8-oxo-dGTPase activity. 1 Publication
    Mutagenesisi191 – 1911L → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi192 – 1976Missing : Almost abolishes 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi192 – 1921R → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi193 – 1975Missing : Greatly reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi193 – 1931E → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi194 – 1974Missing : Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi194 – 1941V → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi195 – 1973Missing : Slightly enhances 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi195 – 1951D → A: Enhances 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi196 – 1961T → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication
    Mutagenesisi197 – 1971V → A: Slightly reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication

    Organism-specific databases

    PharmGKBiPA31830.

    Polymorphism and mutation databases

    DMDMi254763430.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1818MitochondrionSequence analysisAdd
    BLAST
    Chaini19 – 1971797,8-dihydro-8-oxoguanine triphosphatasePRO_0000019944Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    EPDiP36639.
    MaxQBiP36639.
    PaxDbiP36639.
    PeptideAtlasiP36639.
    PRIDEiP36639.
    TopDownProteomicsiP36639-4. [P36639-4]

    PTM databases

    iPTMnetiP36639.
    PhosphoSiteiP36639.

    Expressioni

    Tissue specificityi

    Widely expressed with highest expression in thymus, testis, embryo and proliferating blood lymphocytes.1 Publication

    Developmental stagei

    In peripheral blood lymphocytes, expressed at much higher levels in proliferating cells than in resting cells.1 Publication

    Gene expression databases

    BgeeiP36639.
    CleanExiHS_NUDT1.
    ExpressionAtlasiP36639. baseline and differential.
    GenevisibleiP36639. HS.

    Organism-specific databases

    HPAiHPA012636.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HEL-S-5V9HWA03EBI-1048967,EBI-10207332

    Protein-protein interaction databases

    BioGridi110621. 13 interactions.
    IntActiP36639. 5 interactions.
    STRINGi9606.ENSP00000339503.

    Structurei

    Secondary structure

    1
    197
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi45 – 5410Combined sources
    Beta strandi56 – 649Combined sources
    Turni68 – 714Combined sources
    Beta strandi72 – 743Combined sources
    Beta strandi76 – 794Combined sources
    Helixi86 – 9813Combined sources
    Beta strandi101 – 1033Combined sources
    Beta strandi106 – 11510Combined sources
    Beta strandi121 – 1299Combined sources
    Beta strandi132 – 1343Combined sources
    Beta strandi140 – 1489Combined sources
    Helixi149 – 1513Combined sources
    Helixi154 – 1563Combined sources
    Helixi161 – 1699Combined sources
    Beta strandi173 – 1819Combined sources
    Turni182 – 1843Combined sources
    Beta strandi185 – 19511Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IRYNMR-A42-197[»]
    3Q93X-ray1.80A/B42-197[»]
    3WHWX-ray2.70A/B42-197[»]
    3ZR0X-ray1.80A/B42-197[»]
    3ZR1X-ray1.90A/B42-197[»]
    4C9WX-ray1.65A42-197[»]
    4C9XX-ray1.20A42-197[»]
    4N1TX-ray1.60A42-197[»]
    4N1UX-ray1.60A/B42-196[»]
    5ANSX-ray1.60A42-197[»]
    5ANTX-ray2.00A/B/C42-197[»]
    5ANUX-ray1.80A42-197[»]
    5ANVX-ray1.16A42-197[»]
    5ANWX-ray1.37A42-197[»]
    ProteinModelPortaliP36639.
    SMRiP36639. Positions 44-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36639.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 173130Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni76 – 794Substrate bindingCurated
    Regioni158 – 1614Substrate binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi78 – 9922Nudix boxAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiENOG410IXIA. Eukaryota.
    COG0494. LUCA.
    GeneTreeiENSGT00390000000341.
    HOGENOMiHOG000261970.
    HOVERGENiHBG000032.
    InParanoidiP36639.
    KOiK17816.
    OMAiGAGKWNG.
    OrthoDBiEOG7BS4BT.
    PhylomeDBiP36639.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative initiation. AlignAdd to basket

    Isoform p26 (identifier: P36639-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MYWSNQITRR LGERVQGFMS GISPQQMGEP EGSWSGKNPG TMGASRLYTL
    60 70 80 90 100
    VLVLQPQRVL LGMKKRGFGA GRWNGFGGKV QEGETIEDGA RRELQEESGL
    110 120 130 140 150
    TVDALHKVGQ IVFEFVGEPE LMDVHVFCTD SIQGTPVESD EMRPCWFQLD
    160 170 180 190
    QIPFKDMWPD DSYWFPLLLQ KKKFHGYFKF QGQDTILDYT LREVDTV
    Note: Derived from a B-type mRNA with a polymorphic alteration (GU-->GC) at the beginning of exon 2c that converts an in-frame UGA to CGA yielding another in-frame AUG further upstream.
    Length:197
    Mass (Da):22,520
    Last modified:July 28, 2009 - v3
    Checksum:i82AFF5E1CE287957
    GO
    Isoform p22 (identifier: P36639-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: Missing.

    Show »
    Length:179
    Mass (Da):20,296
    Checksum:i7C9F192384F66C61
    GO
    Isoform p21 (identifier: P36639-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: Missing.

    Show »
    Length:171
    Mass (Da):19,467
    Checksum:i06DE501D75A8B3D6
    GO
    Isoform p18 (identifier: P36639-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: Missing.

    Show »
    Length:156
    Mass (Da):17,952
    Checksum:iB9FB669FF0ACFF5F
    GO

    Polymorphismi

    A polymorphism between Met-1 and Met-19 removes a stop codon before the initiation codon for isoform p22 and gives rise to the production of isoform p26. The allele frequency of isoform p26 is about 20%.1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti77 – 771G → W.
    Corresponds to variant rs11547459 [ dbSNP | Ensembl ].
    VAR_068715
    Natural varianti124 – 1241V → M Associated with type I diabetes in Japanese female population; may be associated with an increased risk for small cell lung carcinoma (SCLC). 4 Publications
    Corresponds to variant rs4866 [ dbSNP | Ensembl ].
    VAR_013757

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141Missing in isoform p18. 4 PublicationsVSP_018814Add
    BLAST
    Alternative sequencei1 – 2626Missing in isoform p21. CuratedVSP_018813Add
    BLAST
    Alternative sequencei1 – 1818Missing in isoform p22. 1 PublicationVSP_018812Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D16581 mRNA. Translation: BAA04013.1.
    D38594 Genomic DNA. Translation: BAA07601.1.
    AB025233 mRNA. Translation: BAA83791.1.
    AB025234 mRNA. Translation: BAA83792.1.
    AB025235 mRNA. Translation: BAA83793.1.
    AB025236 mRNA. Translation: BAA83794.1.
    AB025237 mRNA. Translation: BAA83795.1.
    AB025238 mRNA. Translation: BAA83796.1.
    AB025239 mRNA. Translation: BAA83797.1.
    AB025240 mRNA. Translation: BAA83798.1.
    AB025241 mRNA. Translation: BAA83799.1.
    AB025242 mRNA. Translation: BAA83800.1.
    DQ230907 Genomic DNA. Translation: ABB02181.1.
    CH236953 Genomic DNA. Translation: EAL23948.1.
    CH236953 Genomic DNA. Translation: EAL23949.1.
    CR407655 mRNA. Translation: CAG28583.1.
    CH471144 Genomic DNA. Translation: EAW87225.1.
    CH471144 Genomic DNA. Translation: EAW87227.1.
    AC004971 Genomic DNA. No translation available.
    BC014618 mRNA. Translation: AAH14618.1.
    BC040144 mRNA. Translation: AAH40144.2.
    BC051375 mRNA. Translation: AAH51375.2.
    BC065367 mRNA. Translation: AAH65367.1.
    CCDSiCCDS5329.1. [P36639-2]
    CCDS5330.1. [P36639-4]
    RefSeqiNP_002443.3. NM_002452.3. [P36639-4]
    NP_945186.1. NM_198948.1. [P36639-4]
    NP_945187.1. NM_198949.1. [P36639-2]
    NP_945188.1. NM_198950.1. [P36639-4]
    NP_945190.1. NM_198952.1. [P36639-2]
    NP_945191.1. NM_198953.1. [P36639-4]
    NP_945192.1. NM_198954.1. [P36639-2]
    UniGeneiHs.534331.

    Genome annotation databases

    EnsembliENST00000339737; ENSP00000343439; ENSG00000106268. [P36639-4]
    ENST00000343985; ENSP00000339503; ENSG00000106268. [P36639-2]
    ENST00000356714; ENSP00000349148; ENSG00000106268. [P36639-4]
    ENST00000397046; ENSP00000380239; ENSG00000106268. [P36639-4]
    ENST00000397048; ENSP00000380241; ENSG00000106268. [P36639-2]
    ENST00000397049; ENSP00000380242; ENSG00000106268. [P36639-4]
    GeneIDi4521.
    KEGGihsa:4521.
    UCSCiuc003slr.1. human. [P36639-1]

    Keywords - Coding sequence diversityi

    Alternative initiation, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D16581 mRNA. Translation: BAA04013.1.
    D38594 Genomic DNA. Translation: BAA07601.1.
    AB025233 mRNA. Translation: BAA83791.1.
    AB025234 mRNA. Translation: BAA83792.1.
    AB025235 mRNA. Translation: BAA83793.1.
    AB025236 mRNA. Translation: BAA83794.1.
    AB025237 mRNA. Translation: BAA83795.1.
    AB025238 mRNA. Translation: BAA83796.1.
    AB025239 mRNA. Translation: BAA83797.1.
    AB025240 mRNA. Translation: BAA83798.1.
    AB025241 mRNA. Translation: BAA83799.1.
    AB025242 mRNA. Translation: BAA83800.1.
    DQ230907 Genomic DNA. Translation: ABB02181.1.
    CH236953 Genomic DNA. Translation: EAL23948.1.
    CH236953 Genomic DNA. Translation: EAL23949.1.
    CR407655 mRNA. Translation: CAG28583.1.
    CH471144 Genomic DNA. Translation: EAW87225.1.
    CH471144 Genomic DNA. Translation: EAW87227.1.
    AC004971 Genomic DNA. No translation available.
    BC014618 mRNA. Translation: AAH14618.1.
    BC040144 mRNA. Translation: AAH40144.2.
    BC051375 mRNA. Translation: AAH51375.2.
    BC065367 mRNA. Translation: AAH65367.1.
    CCDSiCCDS5329.1. [P36639-2]
    CCDS5330.1. [P36639-4]
    RefSeqiNP_002443.3. NM_002452.3. [P36639-4]
    NP_945186.1. NM_198948.1. [P36639-4]
    NP_945187.1. NM_198949.1. [P36639-2]
    NP_945188.1. NM_198950.1. [P36639-4]
    NP_945190.1. NM_198952.1. [P36639-2]
    NP_945191.1. NM_198953.1. [P36639-4]
    NP_945192.1. NM_198954.1. [P36639-2]
    UniGeneiHs.534331.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IRYNMR-A42-197[»]
    3Q93X-ray1.80A/B42-197[»]
    3WHWX-ray2.70A/B42-197[»]
    3ZR0X-ray1.80A/B42-197[»]
    3ZR1X-ray1.90A/B42-197[»]
    4C9WX-ray1.65A42-197[»]
    4C9XX-ray1.20A42-197[»]
    4N1TX-ray1.60A42-197[»]
    4N1UX-ray1.60A/B42-196[»]
    5ANSX-ray1.60A42-197[»]
    5ANTX-ray2.00A/B/C42-197[»]
    5ANUX-ray1.80A42-197[»]
    5ANVX-ray1.16A42-197[»]
    5ANWX-ray1.37A42-197[»]
    ProteinModelPortaliP36639.
    SMRiP36639. Positions 44-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110621. 13 interactions.
    IntActiP36639. 5 interactions.
    STRINGi9606.ENSP00000339503.

    PTM databases

    iPTMnetiP36639.
    PhosphoSiteiP36639.

    Polymorphism and mutation databases

    DMDMi254763430.

    Proteomic databases

    EPDiP36639.
    MaxQBiP36639.
    PaxDbiP36639.
    PeptideAtlasiP36639.
    PRIDEiP36639.
    TopDownProteomicsiP36639-4. [P36639-4]

    Protocols and materials databases

    DNASUi4521.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000339737; ENSP00000343439; ENSG00000106268. [P36639-4]
    ENST00000343985; ENSP00000339503; ENSG00000106268. [P36639-2]
    ENST00000356714; ENSP00000349148; ENSG00000106268. [P36639-4]
    ENST00000397046; ENSP00000380239; ENSG00000106268. [P36639-4]
    ENST00000397048; ENSP00000380241; ENSG00000106268. [P36639-2]
    ENST00000397049; ENSP00000380242; ENSG00000106268. [P36639-4]
    GeneIDi4521.
    KEGGihsa:4521.
    UCSCiuc003slr.1. human. [P36639-1]

    Organism-specific databases

    CTDi4521.
    GeneCardsiNUDT1.
    HGNCiHGNC:8048. NUDT1.
    HPAiHPA012636.
    MIMi600312. gene.
    neXtProtiNX_P36639.
    PharmGKBiPA31830.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiENOG410IXIA. Eukaryota.
    COG0494. LUCA.
    GeneTreeiENSGT00390000000341.
    HOGENOMiHOG000261970.
    HOVERGENiHBG000032.
    InParanoidiP36639.
    KOiK17816.
    OMAiGAGKWNG.
    OrthoDBiEOG7BS4BT.
    PhylomeDBiP36639.
    TreeFamiTF106348.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02879-MONOMER.
    BRENDAi3.6.1.55. 2681.
    3.6.1.56. 2681.
    ReactomeiR-HSA-2393930. Phosphate bond hydrolysis by NUDT proteins.
    SABIO-RKP36639.

    Miscellaneous databases

    EvolutionaryTraceiP36639.
    GeneWikiiNUDT1.
    GenomeRNAii4521.
    PROiP36639.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP36639.
    CleanExiHS_NUDT1.
    ExpressionAtlasiP36639. baseline and differential.
    GenevisibleiP36639. HS.

    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. "Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis."
      Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M.
      J. Biol. Chem. 268:23524-23530(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY.
    2. "Genomic structure and chromosome location of the human mutT homologue gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G transversion."
      Furuichi M., Yoshida M.C., Oda H., Tajiri T., Nakabeppu Y., Tsuzuki T., Sekiguchi M.
      Genomics 24:485-490(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Regulation of expression of the human MTH1 gene encoding 8-oxo-dGTPase. Alternative splicing of transcription products."
      Oda H., Nakabeppu Y., Furuichi M., Sekiguchi M.
      J. Biol. Chem. 272:17843-17850(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANT MET-124.
    4. "Multi-forms of human MTH1 polypeptides produced by alternative translation initiation and single nucleotide polymorphism."
      Oda H., Taketomi A., Maruyama R., Itoh R., Nishioka K., Yakushiji H., Suzuki T., Sekiguchi M., Nakabeppu Y.
      Nucleic Acids Res. 27:4335-4343(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P18/P21/P22/P26), ALTERNATIVE INITIATION, POLYMORPHISM.
    5. NIEHS SNPs program
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P18).
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORMS P18 AND P22), VARIANT MET-124.
      Tissue: Bone, Lymph, Mammary gland and Muscle.
    11. "Intracellular localization of 8-oxo-dGTPase in human cells, with special reference to the role of the enzyme in mitochondria."
      Kang D., Nishida J., Iyama A., Nakabeppu Y., Furuichi M., Fujiwara T., Sekiguchi M., Takeshige K.
      J. Biol. Chem. 270:14659-14665(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein."
      Fujikawa K., Kamiya H., Yakushiji H., Fujii Y., Nakabeppu Y., Kasai H.
      J. Biol. Chem. 274:18201-18205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    13. "Functional significance of the conserved residues for the 23-residue module among MTH1 and MutT family proteins."
      Fujii Y., Shimokawa H., Sekiguchi M., Nakabeppu Y.
      J. Biol. Chem. 274:38251-38259(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-77; GLY-78; VAL-80; GLN-81; GLY-83; ILE-86; ASP-88; GLY-89; ALA-90; LEU-94; GLN-95; GLU-96; GLU-97 AND SER-98, FUNCTION, CATALYTIC ACTIVITY.
    14. "Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
      Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
      Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    15. "A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1."
      Sakai Y., Furuichi M., Takahashi M., Mishima M., Iwai S., Shirakawa M., Nakabeppu Y.
      J. Biol. Chem. 277:8579-8587(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-68; TRP-158; ASP-160; LEU-191; ARG-192; GLU-193; VAL-194; ASP-195; THR-196; VAL-197; 192-ARG--VAL-197; 193-GLU--VAL-197; 194-VAL-VAL-197 AND 195-ASP--VAL-197.
    16. "An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell death caused by oxidative stress."
      Yoshimura D., Sakumi K., Ohno M., Sakai Y., Furuichi M., Iwai S., Nakabeppu Y.
      J. Biol. Chem. 278:37965-37973(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    17. "The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal."
      Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S., Hara T., Nakabeppu Y.
      J. Mol. Med. 84:660-670(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates: comparison with MTH1 and MTH2."
      Takagi Y., Setoyama D., Ito R., Kamiya H., Yamagata Y., Sekiguchi M.
      J. Biol. Chem. 287:21541-21549(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    20. "Structure of human MTH1, a Nudix family hydrolase that selectively degrades oxidized purine nucleoside triphosphates."
      Mishima M., Sakai Y., Itoh N., Kamiya H., Furuichi M., Takahashi M., Yamagata Y., Iwai S., Nakabeppu Y., Shirakawa M.
      J. Biol. Chem. 279:33806-33815(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 42-197, SUBUNIT, COFACTOR, SUBSTRATE BINDING SITE.
    21. "Crystallization and preliminary X-ray analysis of human MTH1 complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP."
      Nakamura T., Kitaguchi Y., Miyazawa M., Kamiya H., Toma S., Ikemizu S., Shirakawa M., Nakabeppu Y., Yamagata Y.
      Acta Crystallogr. F 62:1283-1285(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
    22. "Crystal structure of human MTH1 and the 8-oxo-dGMP product complex."
      Svensson L.M., Jemth A.S., Desroses M., Loseva O., Helleday T., Hogbom M., Stenmark P.
      FEBS Lett. 585:2617-2621(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197 IN COMPLEX WITH 8-OXO-DGMP, BIOPHYSICOCHEMICAL PROPERTIES.
    23. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197.
    24. "Association study of human MTH1 gene polymorphisms with type 1 diabetes mellitus."
      Miyako K., Kohno H., Ihara K., Kuromaru R., Matsuura N., Hara T.
      Endocr. J. 51:493-498(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MET-124.
    25. Cited for: VARIANT MET-124.

    Entry informationi

    Entry namei8ODP_HUMAN
    AccessioniPrimary (citable) accession number: P36639
    Secondary accession number(s): A4D205
    , Q6LES7, Q6P0Y6, Q7Z7N6, Q8IV95, Q9UBM0, Q9UBM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: July 28, 2009
    Last modified: July 6, 2016
    This is version 160 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. 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.