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Protein

Probable 8-oxo-dGTP diphosphatase NUDT15

Gene

NUDT15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can degrade 8-oxo-dGTP in vitro, suggesting that it may remove an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool, thereby preventing misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G transversions. Its substrate specificity in vivo however remains unclear (By similarity). May have a role in DNA synthesis and cell cycle progression through the interaction with PCNA.By similarity2 Publications

Catalytic activityi

8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate.1 Publication

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Magnesium may be the real cofactor in vivo.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Magnesium or manganeseBy similarity
Metal bindingi67 – 671Magnesium or manganeseBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-2393930. Phosphate bond hydrolysis by NUDT proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 8-oxo-dGTP diphosphatase NUDT15 (EC:3.6.1.55)
Short name:
8-oxo-dGTPase NUDT15
Alternative name(s):
7,8-dihydro-8-oxoguanine-triphosphatase NUDT15
MutT homolog 2
Short name:
MTH2
Nucleoside diphosphate-linked moiety X motif 15
Short name:
Nudix motif 15
Gene namesi
Name:NUDT15
Synonyms:MTH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:23063. NUDT15.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134963132.

Polymorphism and mutation databases

BioMutaiNUDT15.
DMDMi68565944.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Probable 8-oxo-dGTP diphosphatase NUDT15PRO_0000057115Add
BLAST

Proteomic databases

EPDiQ9NV35.
MaxQBiQ9NV35.
PaxDbiQ9NV35.
PeptideAtlasiQ9NV35.
PRIDEiQ9NV35.

PTM databases

iPTMnetiQ9NV35.
PhosphoSiteiQ9NV35.

Expressioni

Gene expression databases

BgeeiQ9NV35.
CleanExiHS_NUDT15.
GenevisibleiQ9NV35. HS.

Organism-specific databases

HPAiHPA038968.
HPA038969.

Interactioni

Subunit structurei

Interacts with PCNA; interaction is disrupted in response to UV irradiation.1 Publication

Protein-protein interaction databases

BioGridi120559. 5 interactions.
IntActiQ9NV35. 1 interaction.
MINTiMINT-4657900.
STRINGi9606.ENSP00000258662.

Structurei

Secondary structure

1
164
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 219Combined sources
Beta strandi28 – 347Combined sources
Turni38 – 414Combined sources
Beta strandi42 – 443Combined sources
Beta strandi46 – 494Combined sources
Helixi56 – 6813Combined sources
Beta strandi72 – 8514Combined sources
Helixi86 – 883Combined sources
Beta strandi90 – 10112Combined sources
Turni114 – 1163Combined sources
Beta strandi117 – 1248Combined sources
Helixi125 – 1273Combined sources
Helixi131 – 1333Combined sources
Helixi136 – 1438Combined sources
Helixi154 – 1563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BONX-ray1.80A/B/C/D/E/F/G/H1-164[»]
ProteinModelPortaliQ9NV35.
SMRiQ9NV35. Positions 12-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 145137Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 16489Interaction with PCNAAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi48 – 6922Nudix boxAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410J0G8. Eukaryota.
COG1051. LUCA.
GeneTreeiENSGT00390000003338.
HOGENOMiHOG000261967.
HOVERGENiHBG061816.
InParanoidiQ9NV35.
KOiK03574.
OMAiIMEPEKC.
OrthoDBiEOG7P02KG.
PhylomeDBiQ9NV35.
TreeFamiTF106353.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NV35-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASAQPRGR RPGVGVGVVV TSCKHPRCVL LGKRKGSVGA GSFQLPGGHL
60 70 80 90 100
EFGETWEECA QRETWEEAAL HLKNVHFASV VNSFIEKENY HYVTILMKGE
110 120 130 140 150
VDVTHDSEPK NVEPEKNESW EWVPWEELPP LDQLFWGLRC LKEQGYDPFK
160
EDLNHLVGYK GNHL
Length:164
Mass (Da):18,609
Last modified:October 1, 2000 - v1
Checksum:i9FF20DA411C9E9C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001818 mRNA. Translation: BAA91925.1.
AL158196 Genomic DNA. Translation: CAI17017.1.
CH471075 Genomic DNA. Translation: EAX08782.1.
BC064607 mRNA. Translation: AAH64607.1.
BC107875 mRNA. Translation: AAI07876.1.
BC133015 mRNA. Translation: AAI33016.1.
BC133017 mRNA. Translation: AAI33018.1.
CCDSiCCDS9407.1.
RefSeqiNP_001291674.1. NM_001304745.1.
NP_060753.1. NM_018283.3.
UniGeneiHs.144407.

Genome annotation databases

EnsembliENST00000258662; ENSP00000258662; ENSG00000136159.
GeneIDi55270.
KEGGihsa:55270.
UCSCiuc001vbw.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001818 mRNA. Translation: BAA91925.1.
AL158196 Genomic DNA. Translation: CAI17017.1.
CH471075 Genomic DNA. Translation: EAX08782.1.
BC064607 mRNA. Translation: AAH64607.1.
BC107875 mRNA. Translation: AAI07876.1.
BC133015 mRNA. Translation: AAI33016.1.
BC133017 mRNA. Translation: AAI33018.1.
CCDSiCCDS9407.1.
RefSeqiNP_001291674.1. NM_001304745.1.
NP_060753.1. NM_018283.3.
UniGeneiHs.144407.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5BONX-ray1.80A/B/C/D/E/F/G/H1-164[»]
ProteinModelPortaliQ9NV35.
SMRiQ9NV35. Positions 12-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120559. 5 interactions.
IntActiQ9NV35. 1 interaction.
MINTiMINT-4657900.
STRINGi9606.ENSP00000258662.

PTM databases

iPTMnetiQ9NV35.
PhosphoSiteiQ9NV35.

Polymorphism and mutation databases

BioMutaiNUDT15.
DMDMi68565944.

Proteomic databases

EPDiQ9NV35.
MaxQBiQ9NV35.
PaxDbiQ9NV35.
PeptideAtlasiQ9NV35.
PRIDEiQ9NV35.

Protocols and materials databases

DNASUi55270.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258662; ENSP00000258662; ENSG00000136159.
GeneIDi55270.
KEGGihsa:55270.
UCSCiuc001vbw.2. human.

Organism-specific databases

CTDi55270.
GeneCardsiNUDT15.
HGNCiHGNC:23063. NUDT15.
HPAiHPA038968.
HPA038969.
MIMi615792. gene.
neXtProtiNX_Q9NV35.
PharmGKBiPA134963132.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J0G8. Eukaryota.
COG1051. LUCA.
GeneTreeiENSGT00390000003338.
HOGENOMiHOG000261967.
HOVERGENiHBG061816.
InParanoidiQ9NV35.
KOiK03574.
OMAiIMEPEKC.
OrthoDBiEOG7P02KG.
PhylomeDBiQ9NV35.
TreeFamiTF106353.

Enzyme and pathway databases

ReactomeiR-HSA-2393930. Phosphate bond hydrolysis by NUDT proteins.

Miscellaneous databases

GenomeRNAii55270.
PROiQ9NV35.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NV35.
CleanExiHS_NUDT15.
GenevisibleiQ9NV35. HS.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  2. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Lymph.
  5. "Proliferating cell nuclear antigen is protected from degradation by forming a complex with MutT Homolog2."
    Yu Y., Cai J.-P., Tu B., Wu L., Zhao Y., Liu X., Li L., McNutt M.A., Feng J., He Q., Yang Y., Wang H., Sekiguchi M., Zhu W.-G.
    J. Biol. Chem. 284:19310-19320(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PCNA.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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.

Entry informationi

Entry nameiNUD15_HUMAN
AccessioniPrimary (citable) accession number: Q9NV35
Secondary accession number(s): A2RUR6, Q32Q27, Q6P2C9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 117 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.