UniProtKB - P36639 (8ODP_HUMAN)
Oxidized purine nucleoside triphosphate hydrolase
NUDT1
Functioni
Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool (PubMed:8226881, PubMed:7713500, PubMed:10608900, PubMed:12857738, PubMed:22556419, PubMed:26238318, PubMed:24695224, PubMed:24695225, PubMed:28679043).
Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP (PubMed:10373420).
Has also a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP (PubMed:10373420, PubMed:11139615).
Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A (PubMed:8226881, PubMed:10373420, PubMed:10608900, PubMed:11756418, PubMed:12857738, PubMed:16607562, PubMed:24695224, PubMed:24695225, PubMed:26999531, PubMed:28035004).
Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA (PubMed:30304478, PubMed:32144205).
Through this antimutagenic activity protects cells from oxidative stress (PubMed:8226881, PubMed:7713500, PubMed:10608900, PubMed:12857738, PubMed:24695224, PubMed:24695225, PubMed:30304478, PubMed:32144205).
17 PublicationsCaution
Catalytic activityi
- EC:3.6.1.5615 PublicationsThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
Cofactori
Activity regulationi
Kineticsi
- KM=8.3 µM for 2-oxo-dATP (at 30 degrees Celsius and pH 8.0)1 Publication
- KM=5.7 µM for 2-oxo-dATP (at 30 degrees Celsius and pH 7.2)1 Publication
- KM=4.3 µM for 2-oxo-ATP (at 30 degrees Celsius and pH 8.0)1 Publication
- KM=13.9 µM for 8-oxo-dATP (at 30 degrees Celsius and pH 8.0)1 Publication
- KM=15.2 µM for 8-oxo-dGTP (at 30 degrees Celsius and pH 8.0)1 Publication
- KM=12.8 µM for 8-oxo-dGTP (at 30 degrees Celsius and pH 7.2)1 Publication
- KM=13.2 µM for 8-oxo-dGTP (at 22 degrees Celsius and pH 7.5)1 Publication
- KM=258 µM for dGTP (at 30 degrees Celsius and pH 8.0)1 Publication
- KM=40.9 µM for N6-methyl-dATP (at pH 7.5)1 Publication
- KM=15.6 µM for O6-methyl-dGTP (at 22 degrees Celsius and pH 7.5)1 Publication
- KM=16.5 µM for O6-methyl-dGTP (at pH 7.5)1 Publication
- KM=236 µM for O6-methyl-GTP (at 22 degrees Celsius and pH 7.5)1 Publication
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 8 | 2-oxo-dATP; via carbonyl oxygenCombined sources1 Publication | 1 | |
Binding sitei | 8 | 8-oxo-dGMP; via carbonyl oxygenCombined sources1 Publication | 1 | |
Binding sitei | 8 | 8-oxo-dGTP; via carbonyl oxygenCombined sources2 Publications | 1 | |
Binding sitei | 8 | N(6)-methyl-AMP; via carbonyl oxygenCombined sources1 Publication | 1 | |
Binding sitei | 8 | O(6)-methyl-dGMP; via carbonyl oxygenCombined sources1 Publication | 1 | |
Binding sitei | 23 | 8-oxo-dGMPCombined sources1 Publication | 1 | |
Binding sitei | 23 | 8-oxo-dGTPCombined sources1 Publication | 1 | |
Binding sitei | 23 | N(6)-methyl-AMPCombined sources1 Publication | 1 | |
Binding sitei | 23 | O(6)-methyl-dGMPCombined sources1 Publication | 1 | |
Binding sitei | 27 | 8-oxo-ATP; via carbonyl oxygenCombined sources1 Publication | 1 | |
Binding sitei | 33 | 2-oxo-dATPCombined sources1 Publication | 1 | |
Binding sitei | 33 | 8-oxo-dGMPCombined sources1 Publication | 1 | |
Binding sitei | 33 | 8-oxo-dGTPCombined sources2 Publications | 1 | |
Binding sitei | 33 | O(6)-methyl-dGMPCombined sources1 Publication | 1 | |
Metal bindingi | 36 | Magnesium 1; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 52 | Magnesium 2By similarity | 1 | |
Binding sitei | 52 | 8-oxo-ATPCombined sources1 Publication | 1 | |
Metal bindingi | 55 | Magnesium 2By similarity | 1 | |
Metal bindingi | 56 | Magnesium 1By similarity | 1 | |
Binding sitei | 56 | 8-oxo-ATPCombined sources1 Publication | 1 | |
Metal bindingi | 100 | Magnesium 1By similarity | 1 |
GO - Molecular functioni
- 2-hydroxy-ATP hydrolase activity Source: UniProtKB
- 2-hydroxy-dATP hydrolase activity Source: UniProtKB
- 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity Source: UniProtKB
- 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity Source: UniProtKB
- ATP diphosphatase activity Source: UniProtKB
- dATP pyrophosphohydrolase activity Source: GO_Central
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides Source: GO_Central
- metal ion binding Source: UniProtKB-KW
- snoRNA binding Source: UniProtKB
GO - Biological processi
- aging Source: Ensembl
- DNA protection Source: UniProtKB
- DNA repair Source: UniProtKB
- male gonad development Source: Ensembl
- purine nucleoside catabolic process Source: UniProtKB
- response to cadmium ion Source: Ensembl
- response to oxidative stress Source: ProtInc
Keywordsi
Molecular function | Hydrolase, RNA-binding |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.6.1.55, 2681 3.6.1.56, 2681 |
PathwayCommonsi | P36639 |
Reactomei | R-HSA-2393930, Phosphate bond hydrolysis by NUDT proteins |
SABIO-RKi | P36639 |
SignaLinki | P36639 |
Names & Taxonomyi
Protein namesi | Recommended name: Oxidized purine nucleoside triphosphate hydrolase1 Publication (EC:3.6.1.567 Publications)Alternative name(s): 2-hydroxy-dATP diphosphatase 7,8-dihydro-8-oxoguanine triphosphatase 8-oxo-dGTPase Methylated purine nucleoside triphosphate hydrolase1 Publication (EC:3.6.1.-2 Publications) Nucleoside diphosphate-linked moiety X motif 1 Short name: Nudix motif 1 |
Gene namesi | Name:NUDT1 Synonyms:MTH11 Publication |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:8048, NUDT1 |
MIMi | 600312, gene |
neXtProti | NX_P36639 |
VEuPathDBi | HostDB:ENSG00000106268 |
Subcellular locationi
Nucleus
- Nucleus 2 Publications
Mitochondrion
- Mitochondrion matrix 2 Publications1 Publication
Cytoplasm and Cytosol
- cytosol 3 Publications
Note: Mostly present in cytosol (PubMed:7782328). A minor proportion is mitochondrial (PubMed:7782328). A very small amount of the protein is associated with nuclei (PubMed:7782328).2 Publications
Mitochondrion
- Mitochondrion matrix 1 Publication
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular space Source: Ensembl
Mitochondrion
- mitochondrial matrix Source: UniProtKB
- mitochondrion Source: UniProtKB
Nucleus
- nuclear membrane Source: Ensembl
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: Ensembl
Other locations
- acrosomal vesicle Source: Ensembl
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, Mitochondrion, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 27 | F → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities. 1 Publication | 1 | |
Mutagenesisi | 36 | G → R: Reduces activity by 97%. 1 Publication | 1 | |
Mutagenesisi | 37 | G → F: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 39 | V → E: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 40 | Q → P: Reduces activity by 97%. 1 Publication | 1 | |
Mutagenesisi | 42 | G → I: Reduces activity by 60%. 1 Publication | 1 | |
Mutagenesisi | 45 | I → K: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 47 | D → P: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 48 | G → M: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 49 | A → P: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 53 | L → P: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 54 | Q → P: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 55 | E → G: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 56 | E → A: Loss of ability to prevent DNA damage. Expected to cause loss of enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 56 | E → Y: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 57 | S → R: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 117 | W → A: Greatly reduces or abolishes 2-oxo-dATPase and 8-oxo-dGTPase activities. 1 Publication | 1 | |
Mutagenesisi | 117 | W → Y: Enhances 2-oxo-dATPase activity and greatly reduces 8-oxo-dGTPase activity. 1 Publication | 1 | |
Mutagenesisi | 119 | D → A or N: Loss of 2-oxo-dATPase activity, reduces 8-oxo-dGTPase activity. 1 Publication | 1 | |
Mutagenesisi | 120 | D → A or N: Mildly decreased 2-oxo-dATPase activity, nearly abolishes 8-oxo-dGTPase activity. 1 Publication | 1 | |
Mutagenesisi | 150 | L → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 1 | |
Mutagenesisi | 151 – 156 | Missing : Almost abolishes 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 6 | |
Mutagenesisi | 151 | R → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 1 | |
Mutagenesisi | 152 – 156 | Missing : Greatly reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 5 | |
Mutagenesisi | 152 | E → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 1 | |
Mutagenesisi | 153 – 156 | Missing : Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 4 | |
Mutagenesisi | 153 | V → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 1 | |
Mutagenesisi | 154 – 156 | Missing : Slightly enhances 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 3 | |
Mutagenesisi | 154 | D → A: Enhances 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 1 | |
Mutagenesisi | 155 | T → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 1 | |
Mutagenesisi | 156 | V → A: Slightly reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 4521 |
OpenTargetsi | ENSG00000106268 |
PharmGKBi | PA31830 |
Miscellaneous databases
Pharosi | P36639, Tchem |
Chemistry databases
ChEMBLi | CHEMBL3708265 |
Genetic variation databases
BioMutai | NUDT1 |
DMDMi | 254763430 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000019944 | 1 – 156 | Oxidized purine nucleoside triphosphate hydrolaseAdd BLAST | 156 |
Post-translational modificationi
Proteomic databases
EPDi | P36639 |
jPOSTi | P36639 |
MassIVEi | P36639 |
MaxQBi | P36639 |
PaxDbi | P36639 |
PeptideAtlasi | P36639 |
PRIDEi | P36639 |
ProteomicsDBi | 55217 [P36639-1] 55218 [P36639-2] 55219 [P36639-3] 55220 [P36639-4] |
TopDownProteomicsi | P36639-4 [P36639-4] |
PTM databases
GlyGeni | P36639, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P36639 |
PhosphoSitePlusi | P36639 |
Expressioni
Tissue specificityi
Developmental stagei
Gene expression databases
Bgeei | ENSG00000106268, Expressed in right testis and 192 other tissues |
ExpressionAtlasi | P36639, baseline and differential |
Genevisiblei | P36639, HS |
Organism-specific databases
HPAi | ENSG00000106268, Tissue enhanced (bone) |
Interactioni
Subunit structurei
Monomer.
2 PublicationsBinary interactionsi
P36639
With | #Exp. | IntAct |
---|---|---|
HEL-S-5 [V9HWA0] | 3 | EBI-1048967,EBI-10207332 |
Isoform p22 [P36639-2]
With | #Exp. | IntAct |
---|---|---|
ACY1 [Q03154] | 4 | EBI-12380931,EBI-742064 |
FMNL3 - isoform 3 [Q8IVF7-3] | 3 | EBI-12380931,EBI-12414373 |
TRMT12 [Q53H54] | 3 | EBI-12380931,EBI-10242598 |
Isoform p18 [P36639-4]
Protein-protein interaction databases
BioGRIDi | 110621, 27 interactors |
IntActi | P36639, 29 interactors |
MINTi | P36639 |
STRINGi | 9606.ENSP00000380241 |
Chemistry databases
BindingDBi | P36639 |
Miscellaneous databases
RNActi | P36639, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P36639 |
SMRi | P36639 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P36639 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 3 – 132 | Nudix hydrolasePROSITE-ProRule annotationAdd BLAST | 130 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 35 – 38 | 2-oxo-dATP bindingCombined sources1 Publication | 4 | |
Regioni | 35 – 38 | 8-oxo-ATP bindingCombined sources1 Publication | 4 | |
Regioni | 35 – 38 | 8-oxo-dGTP bindingCombined sources2 Publications | 4 | |
Regioni | 117 – 120 | 2-oxo-dATP bindingCombined sources1 Publication | 4 | |
Regioni | 117 – 120 | 8-oxo-ATP bindingCombined sources1 Publication | 4 | |
Regioni | 117 – 120 | 8-oxo-dGMP bindingCombined sources1 Publication | 4 | |
Regioni | 117 – 120 | 8-oxo-dGTP bindingCombined sources2 Publications | 4 | |
Regioni | 117 – 120 | N(6)-methyl-AMP bindingCombined sources1 Publication | 4 | |
Regioni | 117 – 120 | O(6)-methyl-dGMP bindingCombined sources1 Publication | 4 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 37 – 58 | Nudix boxPROSITE-ProRule annotationAdd BLAST | 22 |
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | ENOG502S254, Eukaryota |
GeneTreei | ENSGT00390000000341 |
HOGENOMi | CLU_037162_11_1_1 |
InParanoidi | P36639 |
PhylomeDBi | P36639 |
TreeFami | TF106348 |
Family and domain databases
InterProi | View protein in InterPro IPR003563, 8ODP IPR020476, Nudix_hydrolase IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
PRINTSi | PR01403, 8OXTPHPHTASE PR00502, NUDIXFAMILY |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
s (4+)i Sequence
Sequence statusi: Complete.
This entry describes 4 produced by isoformsialternative initiation. AlignAdd to basketThis entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MGASRLYTLV LVLQPQRVLL GMKKRGFGAG RWNGFGGKVQ EGETIEDGAR
60 70 80 90 100
RELQEESGLT VDALHKVGQI VFEFVGEPEL MDVHVFCTDS IQGTPVESDE
110 120 130 140 150
MRPCWFQLDQ IPFKDMWPDD SYWFPLLLQK KKFHGYFKFQ GQDTILDYTL
REVDTV
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MYWSNQITRRLGERVQGFMSGISPQQMGEPEGSWSGKNPGTM
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MSGISPQQMGEPEGSWSGKNPGTM
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MGEPEGSWSGKNPGTM
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketC9J361 | C9J361_HUMAN | Oxidized purine nucleoside triphosp... | NUDT1 | 37 | Annotation score: |
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_068715 | 36 | G → W. Corresponds to variant dbSNP:rs11547459Ensembl. | 1 | |
Natural variantiVAR_013757 | 83 | V → M Associated with type I diabetes in Japanese female population; may be associated with an increased risk for small cell lung carcinoma (SCLC); decreased localization to mitochondrion. 5 PublicationsCorresponds to variant dbSNP:rs4866Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_061188 | 1 | M → MGEPEGSWSGKNPGTM in isoform p21. | 1 | |
Alternative sequenceiVSP_061189 | 1 | M → MSGISPQQMGEPEGSWSGKN PGTM in isoform p22. | 1 | |
Alternative sequenceiVSP_061190 | 1 | M → MYWSNQITRRLGERVQGFMS GISPQQMGEPEGSWSGKNPG TM in isoform p26. | 1 |
Sequence databases
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative initiationSimilar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1IRY | NMR | - | A | 1-156 | [»] | |
3Q93 | X-ray | 1.80 | A/B | 1-156 | [»] | |
3WHW | X-ray | 2.70 | A/B | 1-156 | [»] | |
3ZR0 | X-ray | 1.80 | A/B | 1-156 | [»] | |
3ZR1 | X-ray | 1.90 | A/B | 1-156 | [»] | |
4C9W | X-ray | 1.65 | A | 1-156 | [»] | |
4C9X | X-ray | 1.20 | A | 1-156 | [»] | |
4N1T | X-ray | 1.60 | A | 1-156 | [»] | |
4N1U | X-ray | 1.60 | A/B | 1-155 | [»] | |
5ANS | X-ray | 1.60 | A | 1-156 | [»] | |
5ANT | X-ray | 2.00 | A/B/C | 1-156 | [»] | |
5ANU | X-ray | 1.80 | A | 1-156 | [»] | |
5ANV | X-ray | 1.16 | A | 1-156 | [»] | |
5ANW | X-ray | 1.37 | A | 1-156 | [»] | |
5FSI | X-ray | 1.63 | A | 1-156 | [»] | |
5FSK | X-ray | 1.56 | A | 1-156 | [»] | |
5FSL | X-ray | 1.24 | A | 1-156 | [»] | |
5FSM | X-ray | 1.67 | A | 1-156 | [»] | |
5FSN | X-ray | 1.69 | A | 1-156 | [»] | |
5FSO | X-ray | 1.67 | A | 1-156 | [»] | |
5GHI | X-ray | 1.21 | A/B | 1-156 | [»] | |
5GHJ | X-ray | 1.20 | A/B | 1-156 | [»] | |
5GHM | X-ray | 1.50 | A/B | 1-156 | [»] | |
5GHN | X-ray | 1.39 | A/B | 1-156 | [»] | |
5GHO | X-ray | 1.19 | A/B | 1-156 | [»] | |
5GHP | X-ray | 1.19 | A/B | 1-156 | [»] | |
5GHQ | X-ray | 1.18 | A/B | 1-156 | [»] | |
5NGR | X-ray | 2.20 | A/B | 1-156 | [»] | |
5NGS | X-ray | 1.85 | A/B | 1-156 | [»] | |
5NGT | X-ray | 1.54 | A | 1-156 | [»] | |
5NHY | X-ray | 1.72 | A/B | 1-156 | [»] | |
5OTM | X-ray | 1.80 | A/B | 1-156 | [»] | |
5WS7 | X-ray | 1.00 | A/B | 1-156 | [»] | |
6AA3 | X-ray | 2.00 | A | 3-156 | [»] | |
6AA4 | X-ray | 1.90 | A | 3-156 | [»] | |
6AA5 | X-ray | 1.90 | A | 3-156 | [»] | |
6EQ2 | X-ray | 1.80 | A | 1-156 | [»] | |
6EQ3 | X-ray | 1.80 | A | 1-156 | [»] | |
6EQ4 | X-ray | 1.40 | A | 1-156 | [»] | |
6EQ5 | X-ray | 1.80 | A | 1-156 | [»] | |
6EQ6 | X-ray | 2.00 | A | 1-156 | [»] | |
6EQ7 | X-ray | 1.50 | A | 1-156 | [»] | |
6F1X | X-ray | 1.90 | A/B | 1-156 | [»] | |
6F20 | X-ray | 2.00 | A/B | 1-156 | [»] | |
6F22 | X-ray | 1.55 | A/B | 1-156 | [»] | |
6F23 | X-ray | 1.84 | A/B | 1-156 | [»] | |
6GLE | X-ray | 1.40 | A | 1-156 | [»] | |
6GLF | X-ray | 2.00 | A | 1-156 | [»] | |
6GLG | X-ray | 1.31 | A | 1-156 | [»] | |
6GLH | X-ray | 1.20 | A | 1-156 | [»] | |
6GLI | X-ray | 1.60 | A | 1-156 | [»] | |
6GLJ | X-ray | 1.30 | A | 1-156 | [»] | |
6GLK | X-ray | 1.50 | A | 1-156 | [»] | |
6GLL | X-ray | 1.40 | A/B | 1-156 | [»] | |
6GLM | X-ray | 1.60 | A | 1-156 | [»] | |
6GLN | X-ray | 1.40 | A | 1-156 | [»] | |
6GLO | X-ray | 1.70 | A/B | 1-156 | [»] | |
6GLP | X-ray | 1.50 | A/B | 1-156 | [»] | |
6GLQ | X-ray | 1.60 | A/B | 1-156 | [»] | |
6GLR | X-ray | 1.60 | A/B | 1-156 | [»] | |
6GLS | X-ray | 1.50 | A/B | 1-156 | [»] | |
6GLT | X-ray | 1.60 | A | 1-156 | [»] | |
6GLU | X-ray | 1.70 | A | 1-156 | [»] | |
6GLV | X-ray | 1.60 | A | 1-156 | [»] | |
6IJY | X-ray | 1.04 | A/B | 1-156 | [»] | |
6ILI | X-ray | 1.45 | A/B | 1-156 | [»] | |
6IMZ | X-ray | 2.10 | A | 3-156 | [»] | |
6JVF | X-ray | 1.73 | A/B | 1-156 | [»] | |
6JVG | X-ray | 1.84 | A/B | 1-156 | [»] | |
6JVH | X-ray | 2.04 | A/B | 1-156 | [»] | |
6JVI | X-ray | 2.25 | A/B | 1-156 | [»] | |
6JVJ | X-ray | 2.30 | A/B | 1-156 | [»] | |
6JVK | X-ray | 2.10 | A/B | 1-156 | [»] | |
6JVL | X-ray | 1.90 | A/B | 1-156 | [»] | |
6JVM | X-ray | 2.10 | A/B | 1-156 | [»] | |
6JVN | X-ray | 2.10 | A/B | 1-156 | [»] | |
6JVO | X-ray | 1.90 | A/B | 2-156 | [»] | |
6JVP | X-ray | 2.21 | A/B | 1-156 | [»] | |
6JVQ | X-ray | 2.20 | A/B | 1-156 | [»] | |
6JVR | X-ray | 2.29 | A/B | 1-156 | [»] | |
6JVS | X-ray | 2.10 | A/B | 1-156 | [»] | |
6JVT | X-ray | 1.80 | A/B | 1-156 | [»] | |
6QVO | X-ray | 2.45 | A/B/C/D | 1-156 | [»] | |
6US2 | X-ray | 1.80 | A | 1-156 | [»] | |
6US3 | X-ray | 1.47 | A | 1-156 | [»] | |
6US4 | X-ray | 1.95 | A | 1-156 | [»] | |
7ESF | X-ray | 1.55 | A | 1-156 | [»] | |
7N03 | X-ray | 1.13 | A | 1-156 | [»] | |
7N13 | X-ray | 1.59 | A/B | 1-156 | [»] | |
AlphaFoldDBi | P36639 | |||||
SMRi | P36639 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 110621, 27 interactors |
IntActi | P36639, 29 interactors |
MINTi | P36639 |
STRINGi | 9606.ENSP00000380241 |
Chemistry databases
BindingDBi | P36639 |
ChEMBLi | CHEMBL3708265 |
PTM databases
GlyGeni | P36639, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P36639 |
PhosphoSitePlusi | P36639 |
Genetic variation databases
BioMutai | NUDT1 |
DMDMi | 254763430 |
Proteomic databases
EPDi | P36639 |
jPOSTi | P36639 |
MassIVEi | P36639 |
MaxQBi | P36639 |
PaxDbi | P36639 |
PeptideAtlasi | P36639 |
PRIDEi | P36639 |
ProteomicsDBi | 55217 [P36639-1] 55218 [P36639-2] 55219 [P36639-3] 55220 [P36639-4] |
TopDownProteomicsi | P36639-4 [P36639-4] |
Protocols and materials databases
Antibodypediai | 1866, 239 antibodies from 30 providers |
DNASUi | 4521 |
Genome annotation databases
Organism-specific databases
CTDi | 4521 |
DisGeNETi | 4521 |
GeneCardsi | NUDT1 |
HGNCi | HGNC:8048, NUDT1 |
HPAi | ENSG00000106268, Tissue enhanced (bone) |
MIMi | 600312, gene |
neXtProti | NX_P36639 |
OpenTargetsi | ENSG00000106268 |
PharmGKBi | PA31830 |
VEuPathDBi | HostDB:ENSG00000106268 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502S254, Eukaryota |
GeneTreei | ENSGT00390000000341 |
HOGENOMi | CLU_037162_11_1_1 |
InParanoidi | P36639 |
PhylomeDBi | P36639 |
TreeFami | TF106348 |
Enzyme and pathway databases
BRENDAi | 3.6.1.55, 2681 3.6.1.56, 2681 |
PathwayCommonsi | P36639 |
Reactomei | R-HSA-2393930, Phosphate bond hydrolysis by NUDT proteins |
SABIO-RKi | P36639 |
SignaLinki | P36639 |
Miscellaneous databases
BioGRID-ORCSi | 4521, 11 hits in 1083 CRISPR screens |
ChiTaRSi | NUDT1, human |
EvolutionaryTracei | P36639 |
GeneWikii | NUDT1 |
GenomeRNAii | 4521 |
Pharosi | P36639, Tchem |
PROi | PR:P36639 |
RNActi | P36639, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000106268, Expressed in right testis and 192 other tissues |
ExpressionAtlasi | P36639, baseline and differential |
Genevisiblei | P36639, HS |
Family and domain databases
InterProi | View protein in InterPro IPR003563, 8ODP IPR020476, Nudix_hydrolase IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
PRINTSi | PR01403, 8OXTPHPHTASE PR00502, NUDIXFAMILY |
SUPFAMi | SSF55811, SSF55811, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | 8ODP_HUMAN | |
Accessioni | P36639Primary (citable) accession number: P36639 Secondary accession number(s): A4D205 Q9UBM9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | September 29, 2021 | |
Last modified: | May 25, 2022 | |
This is version 202 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families