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UniProtKB - P36639 (8ODP_HUMAN)

Entry version 202 (25 May 2022)
Sequence version 4 (29 Sep 2021)
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Protein

Oxidized purine nucleoside triphosphate hydrolase

Gene

NUDT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 Publications

Caution

The role in cancer cell survival is under debate. Was originally considered to play a role as a sanitizing enzyme for oxidized nucleotide pools, and thus important for the survival of cancer cells (PubMed:24695224, PubMed:24695225). A later study indicates that NUDT1 plays a redundant role in eliminating oxidized nucleotides and that it is not essential for cancer cell proliferation and survival (PubMed:28679043).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity1 PublicationNote: Binds 2 Mg2+ ion per subunit.By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by 2-oxo-dADP and 8-oxo-dGDP.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 13.9 sec(-1) with 2-oxo-dATP as substrate (at 30 degrees Celsius and pH 8.0) (PubMed:10373420). kcat is 4.7 sec(-1) with 2-oxo-dATP as substrate (at 30 degrees Celsius and pH 7.2) (PubMed:10373420). kcat is 4.7 sec(-1) with 2-oxo-ATP as substrate (at 30 degrees Celsius and pH 8.0) (PubMed:11139615). kcat is 12.3 sec(-1) with 8-oxo-dGTP as substrate (at 30 degrees Celsius and pH 8.0) (PubMed:10373420). kcat is 2.1 sec(-1) with 8-oxo-dGTP as substrate (at 30 degrees Celsius and pH 7.2) (PubMed:10373420). kcat is 10.8 sec(-1) with 8-oxo-dATP as substrate (at 30 degrees Celsius and pH 8.0) (PubMed:10373420). kcat is 5.4 sec(-1) with O6-methyl-dGTP as substrate (at pH 7.5) (PubMed:32144205). kcat is 2.0 sec(-1) with N6-methyl-dATP as substrate (at pH 7.5) (PubMed:32144205). kcat is 8.2 sec(-1) with O6-methyl-dGTP as substrate (PubMed:30304478). kcat is 0.3 sec(-1) with O6-methyl-GTP as substrate (PubMed:30304478). Shows the best catalytic efficiency for the 2-oxo-dATP substrate (PubMed:10373420, PubMed:11139615). Shows a similar catalytic efficiency for 8-oxo-dGTP and O6-methyl-dGTP (PubMed:30304478).4 Publications
  1. KM=8.3 µM for 2-oxo-dATP (at 30 degrees Celsius and pH 8.0)1 Publication
  2. KM=5.7 µM for 2-oxo-dATP (at 30 degrees Celsius and pH 7.2)1 Publication
  3. KM=4.3 µM for 2-oxo-ATP (at 30 degrees Celsius and pH 8.0)1 Publication
  4. KM=13.9 µM for 8-oxo-dATP (at 30 degrees Celsius and pH 8.0)1 Publication
  5. KM=15.2 µM for 8-oxo-dGTP (at 30 degrees Celsius and pH 8.0)1 Publication
  6. KM=12.8 µM for 8-oxo-dGTP (at 30 degrees Celsius and pH 7.2)1 Publication
  7. KM=13.2 µM for 8-oxo-dGTP (at 22 degrees Celsius and pH 7.5)1 Publication
  8. KM=258 µM for dGTP (at 30 degrees Celsius and pH 8.0)1 Publication
  9. KM=40.9 µM for N6-methyl-dATP (at pH 7.5)1 Publication
  10. KM=15.6 µM for O6-methyl-dGTP (at 22 degrees Celsius and pH 7.5)1 Publication
  11. KM=16.5 µM for O6-methyl-dGTP (at pH 7.5)1 Publication
  12. KM=236 µM for O6-methyl-GTP (at 22 degrees Celsius and pH 7.5)1 Publication

pH dependencei

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei82-oxo-dATP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei88-oxo-dGMP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei88-oxo-dGTP; via carbonyl oxygenCombined sources2 Publications1
Binding sitei8N(6)-methyl-AMP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei8O(6)-methyl-dGMP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei238-oxo-dGMPCombined sources1 Publication1
Binding sitei238-oxo-dGTPCombined sources1 Publication1
Binding sitei23N(6)-methyl-AMPCombined sources1 Publication1
Binding sitei23O(6)-methyl-dGMPCombined sources1 Publication1
Binding sitei278-oxo-ATP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei332-oxo-dATPCombined sources1 Publication1
Binding sitei338-oxo-dGMPCombined sources1 Publication1
Binding sitei338-oxo-dGTPCombined sources2 Publications1
Binding sitei33O(6)-methyl-dGMPCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi36Magnesium 1; via carbonyl oxygenBy similarity1
Metal bindingi52Magnesium 2By similarity1
Binding sitei528-oxo-ATPCombined sources1 Publication1
Metal bindingi55Magnesium 2By similarity1
Metal bindingi56Magnesium 1By similarity1
Binding sitei568-oxo-ATPCombined sources1 Publication1
Metal bindingi100Magnesium 1By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, RNA-binding
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.1.55, 2681
3.6.1.56, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P36639

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2393930, Phosphate bond hydrolysis by NUDT proteins

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P36639

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P36639

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NUDT1
Synonyms:MTH11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:8048, NUDT1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600312, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P36639

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000106268

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi27F → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities. 1 Publication1
Mutagenesisi36G → R: Reduces activity by 97%. 1 Publication1
Mutagenesisi37G → F: Loss of activity. 1 Publication1
Mutagenesisi39V → E: Loss of activity. 1 Publication1
Mutagenesisi40Q → P: Reduces activity by 97%. 1 Publication1
Mutagenesisi42G → I: Reduces activity by 60%. 1 Publication1
Mutagenesisi45I → K: Loss of activity. 1 Publication1
Mutagenesisi47D → P: Loss of activity. 1 Publication1
Mutagenesisi48G → M: Loss of activity. 1 Publication1
Mutagenesisi49A → P: Loss of activity. 1 Publication1
Mutagenesisi53L → P: Loss of activity. 1 Publication1
Mutagenesisi54Q → P: Loss of activity. 1 Publication1
Mutagenesisi55E → G: Loss of activity. 1 Publication1
Mutagenesisi56E → A: Loss of ability to prevent DNA damage. Expected to cause loss of enzyme activity. 1 Publication1
Mutagenesisi56E → Y: Loss of activity. 1 Publication1
Mutagenesisi57S → R: Loss of activity. 1 Publication1
Mutagenesisi117W → A: Greatly reduces or abolishes 2-oxo-dATPase and 8-oxo-dGTPase activities. 1 Publication1
Mutagenesisi117W → Y: Enhances 2-oxo-dATPase activity and greatly reduces 8-oxo-dGTPase activity. 1 Publication1
Mutagenesisi119D → A or N: Loss of 2-oxo-dATPase activity, reduces 8-oxo-dGTPase activity. 1 Publication1
Mutagenesisi120D → A or N: Mildly decreased 2-oxo-dATPase activity, nearly abolishes 8-oxo-dGTPase activity. 1 Publication1
Mutagenesisi150L → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
Mutagenesisi151 – 156Missing : Almost abolishes 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication6
Mutagenesisi151R → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
Mutagenesisi152 – 156Missing : Greatly reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication5
Mutagenesisi152E → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
Mutagenesisi153 – 156Missing : Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication4
Mutagenesisi153V → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
Mutagenesisi154 – 156Missing : Slightly enhances 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication3
Mutagenesisi154D → A: Enhances 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
Mutagenesisi155T → A: Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
Mutagenesisi156V → A: Slightly reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		4521

Open Targets

More...OpenTargetsi		ENSG00000106268

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA31830

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P36639, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3708265

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		NUDT1

Domain mapping of disease mutations (DMDM)

More...DMDMi		254763430

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000199441 – 156Oxidized purine nucleoside triphosphate hydrolaseAdd BLAST156

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P36639

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P36639

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P36639

MaxQB - The MaxQuant DataBase

More...MaxQBi		P36639

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P36639

PeptideAtlas

More...PeptideAtlasi		P36639

PRoteomics IDEntifications database

More...PRIDEi		P36639

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		55217 [P36639-1]
55218 [P36639-2]
55219 [P36639-3]
55220 [P36639-4]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P36639-4 [P36639-4]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P36639, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P36639

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P36639

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000106268, Expressed in right testis and 192 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P36639, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P36639, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000106268, Tissue enhanced (bone)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		110621, 27 interactors

Protein interaction database and analysis system

More...IntActi		P36639, 29 interactors

Molecular INTeraction database

More...MINTi		P36639

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000380241

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P36639

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P36639, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P36639

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P36639

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P36639

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3 – 132Nudix hydrolasePROSITE-ProRule annotationAdd BLAST130

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni35 – 382-oxo-dATP bindingCombined sources1 Publication4
Regioni35 – 388-oxo-ATP bindingCombined sources1 Publication4
Regioni35 – 388-oxo-dGTP bindingCombined sources2 Publications4
Regioni117 – 1202-oxo-dATP bindingCombined sources1 Publication4
Regioni117 – 1208-oxo-ATP bindingCombined sources1 Publication4
Regioni117 – 1208-oxo-dGMP bindingCombined sources1 Publication4
Regioni117 – 1208-oxo-dGTP bindingCombined sources2 Publications4
Regioni117 – 120N(6)-methyl-AMP bindingCombined sources1 Publication4
Regioni117 – 120O(6)-methyl-dGMP bindingCombined sources1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi37 – 58Nudix boxPROSITE-ProRule annotationAdd BLAST22

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502S254, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000000341

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_037162_11_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P36639

Database for complete collections of gene phylogenies

More...PhylomeDBi		P36639

TreeFam database of animal gene trees

More...TreeFami		TF106348

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003563, 8ODP
IPR020476, Nudix_hydrolase
IPR015797, NUDIX_hydrolase-like_dom_sf
IPR020084, NUDIX_hydrolase_CS
IPR000086, NUDIX_hydrolase_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00293, NUDIX, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01403, 8OXTPHPHTASE
PR00502, NUDIXFAMILY

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55811, SSF55811, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51462, NUDIX, 1 hit
PS00893, NUDIX_BOX, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 4 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform p18 (identifier: P36639-4) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
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
Length:156
Mass (Da):17,952
Last modified:September 29, 2021 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB9FB669FF0ACFF5F
GO
Isoform p26 (identifier: P36639-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MYWSNQITRRLGERVQGFMSGISPQQMGEPEGSWSGKNPGTM

Note: Contains a predicted transit peptide (1-18) for localization to the mitochondrion.Sequence analysis 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.
Show »
Length:197
Mass (Da):22,520
Checksum:i82AFF5E1CE287957
GO
Isoform p22 (identifier: P36639-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSGISPQQMGEPEGSWSGKNPGTM

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:
     1-1: M → MGEPEGSWSGKNPGTM

Show »
Length:171
Mass (Da):19,467
Checksum:i06DE501D75A8B3D6
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9J361C9J361_HUMAN
Oxidized purine nucleoside triphosp...
NUDT1
37Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>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
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06871536G → W. Corresponds to variant dbSNP:rs11547459Ensembl.1
Natural variantiVAR_01375783V → 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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0611881M → MGEPEGSWSGKNPGTM in isoform p21. 1
Alternative sequenceiVSP_0611891M → MSGISPQQMGEPEGSWSGKN PGTM in isoform p22. 1
Alternative sequenceiVSP_0611901M → MYWSNQITRRLGERVQGFMS GISPQQMGEPEGSWSGKNPG TM in isoform p26. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS5329.1 [P36639-2]
CCDS5330.1 [P36639-4]

NCBI Reference Sequences

More...RefSeqi		NP_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]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000339737.6; ENSP00000343439.2; ENSG00000106268.16
ENST00000343985.8; ENSP00000339503.4; ENSG00000106268.16 [P36639-2]
ENST00000356714.6; ENSP00000349148.1; ENSG00000106268.16
ENST00000397046.5; ENSP00000380239.1; ENSG00000106268.16
ENST00000397048.5; ENSP00000380241.1; ENSG00000106268.16 [P36639-2]
ENST00000397049.2; ENSP00000380242.2; ENSG00000106268.16

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4521

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4521

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000356714.6; ENSP00000349148.1; NM_002452.4; NP_002443.3

UCSC genome browser

More...UCSCi		uc003slr.1, human [P36639-4]

Keywords - Coding sequence diversityi

Alternative initiation

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IRYNMR-A1-156[»]
3Q93X-ray1.80A/B1-156[»]
3WHWX-ray2.70A/B1-156[»]
3ZR0X-ray1.80A/B1-156[»]
3ZR1X-ray1.90A/B1-156[»]
4C9WX-ray1.65A1-156[»]
4C9XX-ray1.20A1-156[»]
4N1TX-ray1.60A1-156[»]
4N1UX-ray1.60A/B1-155[»]
5ANSX-ray1.60A1-156[»]
5ANTX-ray2.00A/B/C1-156[»]
5ANUX-ray1.80A1-156[»]
5ANVX-ray1.16A1-156[»]
5ANWX-ray1.37A1-156[»]
5FSIX-ray1.63A1-156[»]
5FSKX-ray1.56A1-156[»]
5FSLX-ray1.24A1-156[»]
5FSMX-ray1.67A1-156[»]
5FSNX-ray1.69A1-156[»]
5FSOX-ray1.67A1-156[»]
5GHIX-ray1.21A/B1-156[»]
5GHJX-ray1.20A/B1-156[»]
5GHMX-ray1.50A/B1-156[»]
5GHNX-ray1.39A/B1-156[»]
5GHOX-ray1.19A/B1-156[»]
5GHPX-ray1.19A/B1-156[»]
5GHQX-ray1.18A/B1-156[»]
5NGRX-ray2.20A/B1-156[»]
5NGSX-ray1.85A/B1-156[»]
5NGTX-ray1.54A1-156[»]
5NHYX-ray1.72A/B1-156[»]
5OTMX-ray1.80A/B1-156[»]
5WS7X-ray1.00A/B1-156[»]
6AA3X-ray2.00A3-156[»]
6AA4X-ray1.90A3-156[»]
6AA5X-ray1.90A3-156[»]
6EQ2X-ray1.80A1-156[»]
6EQ3X-ray1.80A1-156[»]
6EQ4X-ray1.40A1-156[»]
6EQ5X-ray1.80A1-156[»]
6EQ6X-ray2.00A1-156[»]
6EQ7X-ray1.50A1-156[»]
6F1XX-ray1.90A/B1-156[»]
6F20X-ray2.00A/B1-156[»]
6F22X-ray1.55A/B1-156[»]
6F23X-ray1.84A/B1-156[»]
6GLEX-ray1.40A1-156[»]
6GLFX-ray2.00A1-156[»]
6GLGX-ray1.31A1-156[»]
6GLHX-ray1.20A1-156[»]
6GLIX-ray1.60A1-156[»]
6GLJX-ray1.30A1-156[»]
6GLKX-ray1.50A1-156[»]
6GLLX-ray1.40A/B1-156[»]
6GLMX-ray1.60A1-156[»]
6GLNX-ray1.40A1-156[»]
6GLOX-ray1.70A/B1-156[»]
6GLPX-ray1.50A/B1-156[»]
6GLQX-ray1.60A/B1-156[»]
6GLRX-ray1.60A/B1-156[»]
6GLSX-ray1.50A/B1-156[»]
6GLTX-ray1.60A1-156[»]
6GLUX-ray1.70A1-156[»]
6GLVX-ray1.60A1-156[»]
6IJYX-ray1.04A/B1-156[»]
6ILIX-ray1.45A/B1-156[»]
6IMZX-ray2.10A3-156[»]
6JVFX-ray1.73A/B1-156[»]
6JVGX-ray1.84A/B1-156[»]
6JVHX-ray2.04A/B1-156[»]
6JVIX-ray2.25A/B1-156[»]
6JVJX-ray2.30A/B1-156[»]
6JVKX-ray2.10A/B1-156[»]
6JVLX-ray1.90A/B1-156[»]
6JVMX-ray2.10A/B1-156[»]
6JVNX-ray2.10A/B1-156[»]
6JVOX-ray1.90A/B2-156[»]
6JVPX-ray2.21A/B1-156[»]
6JVQX-ray2.20A/B1-156[»]
6JVRX-ray2.29A/B1-156[»]
6JVSX-ray2.10A/B1-156[»]
6JVTX-ray1.80A/B1-156[»]
6QVOX-ray2.45A/B/C/D1-156[»]
6US2X-ray1.80A1-156[»]
6US3X-ray1.47A1-156[»]
6US4X-ray1.95A1-156[»]
7ESFX-ray1.55A1-156[»]
7N03X-ray1.13A1-156[»]
7N13X-ray1.59A/B1-156[»]
AlphaFoldDBiP36639
SMRiP36639
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi110621, 27 interactors
IntActiP36639, 29 interactors
MINTiP36639
STRINGi9606.ENSP00000380241

Chemistry databases

BindingDBiP36639
ChEMBLiCHEMBL3708265

PTM databases

GlyGeniP36639, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP36639
PhosphoSitePlusiP36639

Genetic variation databases

BioMutaiNUDT1
DMDMi254763430

Proteomic databases

EPDiP36639
jPOSTiP36639
MassIVEiP36639
MaxQBiP36639
PaxDbiP36639
PeptideAtlasiP36639
PRIDEiP36639
ProteomicsDBi55217 [P36639-1]
55218 [P36639-2]
55219 [P36639-3]
55220 [P36639-4]
TopDownProteomicsiP36639-4 [P36639-4]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1866, 239 antibodies from 30 providers

The DNASU plasmid repository

More...DNASUi		4521

Genome annotation databases

EnsembliENST00000339737.6; ENSP00000343439.2; ENSG00000106268.16
ENST00000343985.8; ENSP00000339503.4; ENSG00000106268.16 [P36639-2]
ENST00000356714.6; ENSP00000349148.1; ENSG00000106268.16
ENST00000397046.5; ENSP00000380239.1; ENSG00000106268.16
ENST00000397048.5; ENSP00000380241.1; ENSG00000106268.16 [P36639-2]
ENST00000397049.2; ENSP00000380242.2; ENSG00000106268.16
GeneIDi4521
KEGGihsa:4521
MANE-SelectiENST00000356714.6; ENSP00000349148.1; NM_002452.4; NP_002443.3
UCSCiuc003slr.1, human [P36639-4]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4521
DisGeNETi4521

GeneCards: human genes, protein and diseases

More...GeneCardsi		NUDT1
HGNCiHGNC:8048, NUDT1
HPAiENSG00000106268, Tissue enhanced (bone)
MIMi600312, gene
neXtProtiNX_P36639
OpenTargetsiENSG00000106268
PharmGKBiPA31830
VEuPathDBiHostDB:ENSG00000106268

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502S254, Eukaryota
GeneTreeiENSGT00390000000341
HOGENOMiCLU_037162_11_1_1
InParanoidiP36639
PhylomeDBiP36639
TreeFamiTF106348

Enzyme and pathway databases

BRENDAi3.6.1.55, 2681
3.6.1.56, 2681
PathwayCommonsiP36639
ReactomeiR-HSA-2393930, Phosphate bond hydrolysis by NUDT proteins
SABIO-RKiP36639
SignaLinkiP36639

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		4521, 11 hits in 1083 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		NUDT1, human
EvolutionaryTraceiP36639

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		NUDT1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		4521
PharosiP36639, Tchem

Protein Ontology

More...PROi		PR:P36639
RNActiP36639, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000106268, Expressed in right testis and 192 other tissues
ExpressionAtlasiP36639, baseline and differential
GenevisibleiP36639, HS

Family and domain databases

InterProiView protein in InterPro
IPR003563, 8ODP
IPR020476, Nudix_hydrolase
IPR015797, NUDIX_hydrolase-like_dom_sf
IPR020084, NUDIX_hydrolase_CS
IPR000086, NUDIX_hydrolase_dom
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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei8ODP_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P36639
Secondary accession number(s): A4D205
, Q6LES7, Q6P0Y6, Q7Z7N6, Q8IV95, Q9UBM0, Q9UBM9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated 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.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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 genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
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