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Q6ZVK8

- NUD18_HUMAN

UniProt

Q6ZVK8 - NUD18_HUMAN

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Protein
8-oxo-dGDP phosphatase NUDT18
Gene
NUDT18, MTH3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mediates the hydrolyzis of oxidized nucleoside diphosphate derivatives. Hydrolyzes 8-oxo-7,8-dihydroguanine (8-oxo-Gua)-containing deoxyribo- and ribonucleoside diphosphates to the monophosphates. Hydrolyzes 8-oxo-dGDP and 8-oxo-GDP with the same efficiencies. Hydrolyzes also 8-OH-dADP and 2-OH-dADP. Exhibited no or minimal hydrolyzis activity against 8-oxo-dGTP, 8-oxo-GTP, dGTP, GTP, dGDP and GDP. Probably removes oxidized guanine nucleotides from both the DNA and RNA precursor pools.1 Publication

Catalytic activityi

8-oxo-dGDP + H2O = 8-oxo-dGMP + phosphate.1 Publication

Cofactori

Manganese By similarity. Magnesium.1 Publication

Kineticsi

  1. KM=10.7 µM for 8-Oxo-dGDP1 Publication
  2. KM=11.7 µM for 8-Oxo-GDP

Vmax=212 pmol/min/µg enzyme toward 8-Oxo-dGDP (at 30 degrees Celsius)

Vmax=246 pmol/min/µg enzyme toward 8-Oxo-GDP (at 30 degrees Celsius)

pH dependencei

Optimum pH is 8.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Magnesium or manganese By similarity
Metal bindingi95 – 951Magnesium or manganese By similarity

GO - Molecular functioni

  1. 8-hydroxy-dADP phosphatase activity Source: UniProtKB
  2. 8-oxo-GDP phosphatase activity Source: UniProtKB
  3. 8-oxo-dGDP phosphatase activity Source: UniProtKB
  4. magnesium ion binding Source: UniProtKB
  5. protein binding Source: IntAct

GO - Biological processi

  1. GDP catabolic process Source: UniProtKB
  2. dADP catabolic process Source: UniProtKB
  3. dGDP catabolic process Source: UniProtKB
  4. nucleobase-containing small molecule catabolic process Source: Reactome
  5. nucleobase-containing small molecule metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000173566-MONOMER.
ReactomeiREACT_150237. Phosphate bond hydrolysis by NUDT proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
8-oxo-dGDP phosphatase NUDT18 (EC:3.6.1.58)
Alternative name(s):
2-hydroxy-dADP phosphatase
7,8-dihydro-8-oxoguanine phosphatase
MutT homolog 3
Nucleoside diphosphate-linked moiety X motif 18
Short name:
Nudix motif 18
Gene namesi
Name:NUDT18
Synonyms:MTH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:26194. NUDT18.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671238.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3233238-oxo-dGDP phosphatase NUDT18
PRO_0000324567Add
BLAST

Proteomic databases

MaxQBiQ6ZVK8.
PaxDbiQ6ZVK8.
PRIDEiQ6ZVK8.

PTM databases

PhosphoSiteiQ6ZVK8.

Expressioni

Gene expression databases

ArrayExpressiQ6ZVK8.
BgeeiQ6ZVK8.
CleanExiHS_NUDT18.
GenevestigatoriQ6ZVK8.

Organism-specific databases

HPAiHPA028581.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
APIPQ96GX93EBI-740486,EBI-359248
DHPSP493663EBI-740486,EBI-741925
DUTP333163EBI-740486,EBI-353224
EVI5LQ96CN43EBI-740486,EBI-749523
HSD17B14Q9BPX13EBI-740486,EBI-742664
NT5C2P499023EBI-740486,EBI-742084
PAICSP222343EBI-740486,EBI-712261
RAB3IL1Q8TBN03EBI-740486,EBI-743796
RABAC1Q9UI143EBI-740486,EBI-712367

Protein-protein interaction databases

BioGridi122961. 34 interactions.
IntActiQ6ZVK8. 32 interactions.
MINTiMINT-1436358.
STRINGi9606.ENSP00000307852.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 497
Beta strandi55 – 617
Helixi65 – 673
Beta strandi74 – 774
Helixi84 – 9613
Beta strandi98 – 11215
Beta strandi115 – 12713
Helixi132 – 1343
Beta strandi136 – 1383
Beta strandi140 – 1467
Beta strandi152 – 1554
Helixi158 – 17215

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GG6X-ray2.10A26-179[»]
4HVYX-ray1.46A26-179[»]
ProteinModelPortaliQ6ZVK8.
SMRiQ6ZVK8. Positions 36-179.

Miscellaneous databases

EvolutionaryTraceiQ6ZVK8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 167131Nudix hydrolase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi76 – 9722Nudix box
Add
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family.

Phylogenomic databases

eggNOGiCOG1051.
HOGENOMiHOG000035136.
HOVERGENiHBG108203.
InParanoidiQ6ZVK8.
KOiK17817.
OMAiQEAKKEC.
PhylomeDBiQ6ZVK8.
TreeFamiTF106355.

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.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6ZVK8-1) [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

MASEGLAGAL ASVLAGQGSS VHSCDSAPAG EPPAPVRLRK NVCYVVLAVF    50
LSEQDEVLLI QEAKRECRGS WYLPAGRMEP GETIVEALQR EVKEEAGLHC 100
EPETLLSVEE RGPSWVRFVF LARPTGGILK TSKEADAESL QAAWYPRTSL 150
PTPLRAHDIL HLVELAAQYR QQARHPLILP QELPCDLVCQ RLVATFTSAQ 200
TVWVLVGTVG MPHLPVTACG LDPMEQRGGM KMAVLRLLQE CLTLHHLVVE 250
IKGLLGLQHL GRDHSDGICL NVLVTVAFRS PGIQDEPPKV RGENFSWWKV 300
MEEDLQSQLL QRLQGSSVVP VNR 323
Length:323
Mass (Da):35,501
Last modified:March 6, 2013 - v3
Checksum:i8162BA4BDEC4374D
GO
Isoform 2 (identifier: Q6ZVK8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     101-125: EPETLLSVEERGPSWVRFVFLARPT → MSVDSARAALLSTQTLPAPSPTSPP

Note: No experimental confirmation available.

Show »
Length:223
Mass (Da):24,463
Checksum:iED9DD93D505E8709
GO

Sequence cautioni

The sequence BAC85853.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2.
VSP_032276Add
BLAST
Alternative sequencei101 – 12525EPETL…LARPT → MSVDSARAALLSTQTLPAPS PTSPP in isoform 2.
VSP_032277Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1771L → P in BAB15376. 1 Publication
Sequence conflicti224 – 2241M → V in BAB15376. 1 Publication
Sequence conflicti224 – 2241M → V in BAC85853. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK026147 mRNA. Translation: BAB15376.1.
AK124446 mRNA. Translation: BAC85853.1. Different initiation.
BC016902 mRNA. Translation: AAH16902.1.
RefSeqiNP_079091.3. NM_024815.3. [Q6ZVK8-1]
UniGeneiHs.527101.
Hs.745387.

Genome annotation databases

EnsembliENST00000309188; ENSP00000307852; ENSG00000173566. [Q6ZVK8-1]
GeneIDi79873.
KEGGihsa:79873.
UCSCiuc003xaq.1. human. [Q6ZVK8-1]

Polymorphism databases

DMDMi460018323.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK026147 mRNA. Translation: BAB15376.1 .
AK124446 mRNA. Translation: BAC85853.1 . Different initiation.
BC016902 mRNA. Translation: AAH16902.1 .
RefSeqi NP_079091.3. NM_024815.3. [Q6ZVK8-1 ]
UniGenei Hs.527101.
Hs.745387.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GG6 X-ray 2.10 A 26-179 [» ]
4HVY X-ray 1.46 A 26-179 [» ]
ProteinModelPortali Q6ZVK8.
SMRi Q6ZVK8. Positions 36-179.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122961. 34 interactions.
IntActi Q6ZVK8. 32 interactions.
MINTi MINT-1436358.
STRINGi 9606.ENSP00000307852.

PTM databases

PhosphoSitei Q6ZVK8.

Polymorphism databases

DMDMi 460018323.

Proteomic databases

MaxQBi Q6ZVK8.
PaxDbi Q6ZVK8.
PRIDEi Q6ZVK8.

Protocols and materials databases

DNASUi 79873.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309188 ; ENSP00000307852 ; ENSG00000173566 . [Q6ZVK8-1 ]
GeneIDi 79873.
KEGGi hsa:79873.
UCSCi uc003xaq.1. human. [Q6ZVK8-1 ]

Organism-specific databases

CTDi 79873.
GeneCardsi GC08M022021.
HGNCi HGNC:26194. NUDT18.
HPAi HPA028581.
MIMi 615791. gene.
neXtProti NX_Q6ZVK8.
PharmGKBi PA142671238.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1051.
HOGENOMi HOG000035136.
HOVERGENi HBG108203.
InParanoidi Q6ZVK8.
KOi K17817.
OMAi QEAKKEC.
PhylomeDBi Q6ZVK8.
TreeFami TF106355.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000173566-MONOMER.
Reactomei REACT_150237. Phosphate bond hydrolysis by NUDT proteins.

Miscellaneous databases

EvolutionaryTracei Q6ZVK8.
GenomeRNAii 79873.
NextBioi 69645.
PROi Q6ZVK8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6ZVK8.
Bgeei Q6ZVK8.
CleanExi HS_NUDT18.
Genevestigatori Q6ZVK8.

Family and domain databases

Gene3Di 3.90.79.10. 1 hit.
InterProi IPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view ]
Pfami PF00293. NUDIX. 1 hit.
[Graphical view ]
PRINTSi PR00502. NUDIXFAMILY.
SUPFAMi SSF55811. SSF55811. 1 hit.
PROSITEi PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view ]
ProtoNeti Search...

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] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum.
  2. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 1).
    Tissue: Uterus.
  4. "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: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, FUNCTION.
  5. "Crystal structure of the nudix domain of human nudt18."
    Structural genomics consortium (SGC)
    Submitted (MAR-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-179.

Entry informationi

Entry nameiNUD18_HUMAN
AccessioniPrimary (citable) accession number: Q6ZVK8
Secondary accession number(s): Q8IZ75, Q9H687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 6, 2013
Last modified: September 3, 2014
This is version 89 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, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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

External Data

Dasty 3

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