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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)DescriptionActionsGraphical viewLength
    Binding sitei49Substrate; via carbonyl oxygen1
    Binding sitei68Substrate1
    Sitei68Important for 2-OH-dATPase and 8-oxo-dGTPase activities1
    Binding sitei74Substrate1
    Metal bindingi78Magnesium; via carbonyl oxygenBy similarity1
    Metal bindingi93MagnesiumBy similarity1
    Metal bindingi96MagnesiumBy similarity1
    Metal bindingi97MagnesiumBy similarity1
    Sitei158Essential for 2-OH-dATPase and 8-oxo-dGTPase activities1
    Sitei160Essential for 2-OH-dATPase activity and important for 8-oxo-dGTPase activity1

    GO - Molecular functioni

    GO - Biological processi

    • aging Source: Ensembl
    • dATP catabolic process Source: UniProtKB
    • dGTP catabolic process Source: UniProtKB
    • DNA protection Source: UniProtKB
    • DNA repair Source: UniProtKB
    • male gonad development Source: Ensembl
    • nucleobase-containing small molecule catabolic process Source: Reactome
    • purine nucleotide catabolic process Source: UniProtKB
    • response to cadmium ion Source: Ensembl
    • response to oxidative stress Source: ProtInc

    Keywordsi

    Molecular functionHydrolase, RNA-binding
    LigandMagnesium, Metal-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-RKiP36639.

    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

    • acrosomal vesicle Source: Ensembl
    • cytoplasm Source: UniProtKB
    • cytosol Source: HPA
    • extracellular exosome Source: UniProtKB
    • extracellular space Source: Ensembl
    • mitochondrial matrix Source: UniProtKB
    • mitochondrion Source: UniProtKB
    • nuclear membrane Source: Ensembl
    • nucleus Source: UniProtKB
    • plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi68F → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities. 1 Publication1
    Mutagenesisi77G → R: Reduces activity by 97%. 1 Publication1
    Mutagenesisi78G → F: Loss of activity. 1 Publication1
    Mutagenesisi80V → E: Loss of activity. 1 Publication1
    Mutagenesisi81Q → P: Reduces activity by 97%. 1 Publication1
    Mutagenesisi83G → I: Reduces activity by 60%. 1 Publication1
    Mutagenesisi86I → K: Loss of activity. 1 Publication1
    Mutagenesisi88D → P: Loss of activity. 1 Publication1
    Mutagenesisi89G → M: Loss of activity. 1 Publication1
    Mutagenesisi90A → P: Loss of activity. 1 Publication1
    Mutagenesisi94L → P: Loss of activity. 1 Publication1
    Mutagenesisi95Q → P: Loss of activity. 1 Publication1
    Mutagenesisi96E → G: Loss of activity. 1 Publication1
    Mutagenesisi97E → Y: Loss of activity. 1 Publication1
    Mutagenesisi98S → R: Loss of activity. 1 Publication1
    Mutagenesisi158W → A: Greatly reduces or abolishes 2-OH-dATPase and 8-oxo-dGTPase activities. 1 Publication1
    Mutagenesisi158W → Y: Enhances 2-OH-dATPase activity and greatly reduces 8-oxo-dGTPase activity. 1 Publication1
    Mutagenesisi160D → A or N: Loss of 2-OH-dATPase activity, reduces 8-oxo-dGTPase activity. 1 Publication1
    Mutagenesisi191L → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi192 – 197Missing : Almost abolishes 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication6
    Mutagenesisi192R → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi193 – 197Missing : Greatly reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication5
    Mutagenesisi193E → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi194 – 197Missing : Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication4
    Mutagenesisi194V → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi195 – 197Missing : Slightly enhances 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication3
    Mutagenesisi195D → A: Enhances 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi196T → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi197V → A: Slightly reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1

    Organism-specific databases

    DisGeNETi4521.
    OpenTargetsiENSG00000106268.
    PharmGKBiPA31830.

    Polymorphism and mutation databases

    DMDMi254763430.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 18MitochondrionSequence analysisAdd BLAST18
    ChainiPRO_000001994419 – 1977,8-dihydro-8-oxoguanine triphosphataseAdd BLAST179

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

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

    PTM databases

    iPTMnetiP36639.
    PhosphoSitePlusiP36639.

    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

    BgeeiENSG00000106268.
    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 interactors.
    IntActiP36639. 7 interactors.
    STRINGi9606.ENSP00000339503.

    Structurei

    Secondary structure

    1197
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi45 – 54Combined sources10
    Beta strandi56 – 64Combined sources9
    Turni68 – 71Combined sources4
    Beta strandi72 – 74Combined sources3
    Beta strandi76 – 79Combined sources4
    Helixi86 – 98Combined sources13
    Beta strandi101 – 103Combined sources3
    Beta strandi105 – 115Combined sources11
    Beta strandi120 – 131Combined sources12
    Beta strandi132 – 134Combined sources3
    Beta strandi140 – 148Combined sources9
    Helixi149 – 151Combined sources3
    Helixi154 – 156Combined sources3
    Helixi161 – 169Combined sources9
    Beta strandi173 – 181Combined sources9
    Turni182 – 184Combined sources3
    Beta strandi185 – 195Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5FSIX-ray1.63A42-197[»]
    5FSKX-ray1.56A42-197[»]
    5FSLX-ray1.24A42-197[»]
    5FSMX-ray1.67A42-197[»]
    5FSNX-ray1.69A42-197[»]
    5FSOX-ray1.67A42-197[»]
    5GHIX-ray1.21A/B42-197[»]
    5GHJX-ray1.20A/B42-197[»]
    5GHMX-ray1.50A/B42-197[»]
    5GHNX-ray1.39A/B42-197[»]
    5GHOX-ray1.19A/B42-197[»]
    5GHPX-ray1.19A/B42-197[»]
    5GHQX-ray1.18A/B42-197[»]
    5WS7X-ray1.00A/B42-197[»]
    ProteinModelPortaliP36639.
    SMRiP36639.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36639.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini44 – 173Nudix hydrolasePROSITE-ProRule annotationAdd BLAST130

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni76 – 79Substrate bindingCurated4
    Regioni158 – 161Substrate binding4

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi78 – 99Nudix boxAdd BLAST22

    Sequence similaritiesi

    Belongs to the Nudix hydrolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiENOG410IXIA. Eukaryota.
    COG0494. LUCA.
    GeneTreeiENSGT00390000000341.
    HOGENOMiHOG000261970.
    HOVERGENiHBG000032.
    InParanoidiP36639.
    KOiK17816.
    OMAiGAGKWNG.
    OrthoDBiEOG091G0O4Y.
    PhylomeDBiP36639.
    TreeFamiTF106348.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiView protein in InterPro
    IPR020476. Nudix_hydrolase.
    IPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    IPR003563. OxG-triPHTase.
    PfamiView protein in Pfam
    PF00293. NUDIX. 1 hit.
    PRINTSiPR01403. 8OXTPHPHTASE.
    PR00502. NUDIXFAMILY.
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiView protein in PROSITE
    PS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.

    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)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06871577G → W. Corresponds to variant dbSNP:rs11547459Ensembl.1
    Natural variantiVAR_013757124V → M Associated with type I diabetes in Japanese female population; may be associated with an increased risk for small cell lung carcinoma (SCLC). 4 PublicationsCorresponds to variant dbSNP:rs4866Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0188141 – 41Missing in isoform p18. 4 PublicationsAdd BLAST41
    Alternative sequenceiVSP_0188131 – 26Missing in isoform p21. CuratedAdd BLAST26
    Alternative sequenceiVSP_0188121 – 18Missing in isoform p22. 1 PublicationAdd BLAST18

    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
    PDB 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[»]
    5FSIX-ray1.63A42-197[»]
    5FSKX-ray1.56A42-197[»]
    5FSLX-ray1.24A42-197[»]
    5FSMX-ray1.67A42-197[»]
    5FSNX-ray1.69A42-197[»]
    5FSOX-ray1.67A42-197[»]
    5GHIX-ray1.21A/B42-197[»]
    5GHJX-ray1.20A/B42-197[»]
    5GHMX-ray1.50A/B42-197[»]
    5GHNX-ray1.39A/B42-197[»]
    5GHOX-ray1.19A/B42-197[»]
    5GHPX-ray1.19A/B42-197[»]
    5GHQX-ray1.18A/B42-197[»]
    5WS7X-ray1.00A/B42-197[»]
    ProteinModelPortaliP36639.
    SMRiP36639.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110621. 13 interactors.
    IntActiP36639. 7 interactors.
    STRINGi9606.ENSP00000339503.

    PTM databases

    iPTMnetiP36639.
    PhosphoSitePlusiP36639.

    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.
    DisGeNETi4521.
    GeneCardsiNUDT1.
    HGNCiHGNC:8048. NUDT1.
    HPAiHPA012636.
    MIMi600312. gene.
    neXtProtiNX_P36639.
    OpenTargetsiENSG00000106268.
    PharmGKBiPA31830.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiENOG410IXIA. Eukaryota.
    COG0494. LUCA.
    GeneTreeiENSGT00390000000341.
    HOGENOMiHOG000261970.
    HOVERGENiHBG000032.
    InParanoidiP36639.
    KOiK17816.
    OMAiGAGKWNG.
    OrthoDBiEOG091G0O4Y.
    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-RKiP36639.

    Miscellaneous databases

    EvolutionaryTraceiP36639.
    GeneWikiiNUDT1.
    GenomeRNAii4521.
    PROiPR:P36639.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000106268.
    CleanExiHS_NUDT1.
    ExpressionAtlasiP36639. baseline and differential.
    GenevisibleiP36639. HS.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiView protein in InterPro
    IPR020476. Nudix_hydrolase.
    IPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    IPR003563. OxG-triPHTase.
    PfamiView protein in Pfam
    PF00293. NUDIX. 1 hit.
    PRINTSiPR01403. 8OXTPHPHTASE.
    PR00502. NUDIXFAMILY.
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiView protein in PROSITE
    PS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry namei8ODP_HUMAN
    AccessioniPrimary (citable) accession number: P36639
    Secondary accession number(s): A4D205
    , Q6LES7, Q6P0Y6, Q7Z7N6, Q8IV95, Q9UBM0, Q9UBM9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: July 28, 2009
    Last modified: April 12, 2017
    This is version 167 of the entry and version 3 of the sequence. See 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.