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UniProtKB - P36639 (8ODP_HUMAN)

Entry version 186 (05 Jun 2019)
Sequence version 3 (28 Jul 2009)
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Protein

7,8-dihydro-8-oxoguanine triphosphatase

Gene

NUDT1

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

Annotation score:5 out of 5

<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

Antimutagenic (PubMed:8226881, PubMed:7713500, PubMed:10608900). Plays a redundant role in sanitizing oxidized nucleotide pools, such as 8-oxo-dGTP pools (PubMed:28679043). Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress (PubMed:12857738, PubMed:24695224, PubMed:24695225). Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions (PubMed:8226881, PubMed:10373420, PubMed:10608900, PubMed:11756418, PubMed:12857738, PubMed:16607562, PubMed:24695224, PubMed:24695225, PubMed:26999531, PubMed:28035004). Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP (PubMed:10373420, PubMed:11139615). Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA (By similarity).By similarity14 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_section">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+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

2-hydroxy-dATPase activity is inhibited by 2-OH-dADP, 8-OH-dGDP and 8-OH-dGTP. 8-OH-dGTPase activity is inhibited by 8-OH-dGDP, 2-OH-dADP and 2-OH-dATP.1 Publication

<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

The kinetic constants are determined for the recombinant enzyme expressed in E.coli. 2-hydroxy-rATP shows the best catalytic efficiency.
  1. KM=8.3 µM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 8.0)1 Publication
  2. KM=5.7 µM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 7.2)1 Publication
  3. KM=4.3 µM for 2-hydroxy-rATP (at 30 degrees Celsius and pH 8.0)1 Publication
  4. KM=13.9 µM for 8-hydroxy-dATP (at 30 degrees Celsius and pH 8.0)1 Publication
  5. KM=51.0 µM for 8-hydroxy-rATP (at 30 degrees Celsius and pH 8.0)1 Publication
  6. KM=15.2 µM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 8.0)1 Publication
  7. KM=12.8 µM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 7.2)1 Publication
  8. KM=13.2 µM for 8-hydroxy-dGTP (at 22 degrees Celsius and pH 7.5)1 Publication
  9. KM=55.0 µM for 8-hydroxy-rGTP (at 30 degrees Celsius and pH 8.0)1 Publication
  10. KM=258 µM for dGTP (at 30 degrees Celsius and pH 8.0)1 Publication

    pH dependencei

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei49Substrate; via carbonyl oxygenCombined sources2 Publications1
    Binding sitei64SubstrateCombined sources2 Publications1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei68Important for 2-OH-dATPase and 8-oxo-dGTPase activities1 Publication1
    Binding sitei74SubstrateCombined sources2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi78Magnesium; via carbonyl oxygenBy similarity1
    Metal bindingi93MagnesiumBy similarity1
    Metal bindingi96MagnesiumBy similarity1
    Metal bindingi97MagnesiumBy similarity1
    Sitei158Essential for 2-OH-dATPase and 8-oxo-dGTPase activities1 Publication1
    Sitei160Essential for 2-OH-dATPase activity and important for 8-oxo-dGTPase activity1 Publication1

    <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

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:HS02879-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.6.1.55 2681
    3.6.1.56 2681

    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

    <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_and_taxonomy_section">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:
    7,8-dihydro-8-oxoguanine triphosphatase (EC:3.6.1.557 Publications)
    Alternative name(s):
    2-hydroxy-dATP diphosphatase (EC:3.6.1.565 Publications)
    8-oxo-dGTPase
    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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    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_and_biotech_section">'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>Mutagenesisi68F → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities. 1 Publication1
    Mutagenesisi77G → R: Reduces activity by 97%. 1 Publication1
    Mutagenesisi78G → F: Loss of activity. 1 Publication1
    Mutagenesisi80V → E: Loss of activity. 1 Publication1
    Mutagenesisi81Q → P: Reduces activity by 97%. 1 Publication1
    Mutagenesisi83G → I: Reduces activity by 60%. 1 Publication1
    Mutagenesisi86I → K: Loss of activity. 1 Publication1
    Mutagenesisi88D → P: Loss of activity. 1 Publication1
    Mutagenesisi89G → M: Loss of activity. 1 Publication1
    Mutagenesisi90A → P: Loss of activity. 1 Publication1
    Mutagenesisi94L → P: Loss of activity. 1 Publication1
    Mutagenesisi95Q → P: Loss of activity. 1 Publication1
    Mutagenesisi96E → G: Loss of activity. 1 Publication1
    Mutagenesisi97E → A: Loss of ability to prevent DNA damage. Expected to cause loss of enzyme activity. 1 Publication1
    Mutagenesisi97E → Y: Loss of activity. 1 Publication1
    Mutagenesisi98S → R: Loss of activity. 1 Publication1
    Mutagenesisi158W → A: Greatly reduces or abolishes 2-OH-dATPase and 8-oxo-dGTPase activities. 1 Publication1
    Mutagenesisi158W → Y: Enhances 2-OH-dATPase activity and greatly reduces 8-oxo-dGTPase activity. 1 Publication1
    Mutagenesisi160D → A or N: Loss of 2-OH-dATPase activity, reduces 8-oxo-dGTPase activity. 1 Publication1
    Mutagenesisi161D → A or N: Mildly decreased 2-OH-dATPase activity, nearly abolishes 8-oxo-dGTPase activity. 1 Publication1
    Mutagenesisi191L → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi192 – 197Missing : Almost abolishes 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication6
    Mutagenesisi192R → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi193 – 197Missing : Greatly reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication5
    Mutagenesisi193E → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi194 – 197Missing : Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication4
    Mutagenesisi194V → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi195 – 197Missing : Slightly enhances 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication3
    Mutagenesisi195D → A: Enhances 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi196T → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1
    Mutagenesisi197V → A: Slightly reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		4521

    Open Targets

    More...    OpenTargetsi    		ENSG00000106268

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA31830

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL3708265

    Polymorphism and mutation 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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 18MitochondrionSequence analysisAdd BLAST18
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001994419 – 1977,8-dihydro-8-oxoguanine triphosphataseAdd BLAST179

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

    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 human proteome resource

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

    Consortium for Top Down Proteomics

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

    PTM databases

    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 175 organ(s), highest expression level in right testis

    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    		HPA012636

    <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_section">'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_section">'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_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    HEL-S-5V9HWA03EBI-1048967,EBI-10207332

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		110621, 14 interactors

    Protein interaction database and analysis system

    More...    IntActi    		P36639, 9 interactors

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000380241

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P36639

    <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

    1197
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...    SMRi    		P36639

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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_and_domains_section">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>Domaini44 – 173Nudix 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>Regioni76 – 79Substrate bindingCombined sources1 Publication4
    Regioni158 – 161Substrate bindingCombined sources2 Publications4

    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>Motifi78 – 99Nudix 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    		ENOG410IXIA Eukaryota
    COG0494 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00390000000341

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000261970

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P36639

    KEGG Orthology (KO)

    More...    KOi    		K17816

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		WFPLMLQ

    Database of Orthologous Groups

    More...    OrthoDBi    		1602447at2759

    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
    IPR020476 Nudix_hydrolase
    IPR015797 NUDIX_hydrolase-like_dom_sf
    IPR020084 NUDIX_hydrolase_CS
    IPR000086 NUDIX_hydrolase_dom
    IPR003563 OxG-triPHTase

    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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    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 p26 (identifier: P36639-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MYWSNQITRR LGERVQGFMS GISPQQMGEP EGSWSGKNPG TMGASRLYTL 
            60         70         80         90        100
    VLVLQPQRVL LGMKKRGFGA GRWNGFGGKV QEGETIEDGA RRELQEESGL 
           110        120        130        140        150
    TVDALHKVGQ IVFEFVGEPE LMDVHVFCTD SIQGTPVESD EMRPCWFQLD 
           160        170        180        190 
    QIPFKDMWPD DSYWFPLLLQ KKKFHGYFKF QGQDTILDYT LREVDTV
    Note: Derived from a B-type mRNA with a polymorphic alteration (GU-->GC) at the beginning of exon 2c that converts an in-frame UGA to CGA yielding another in-frame AUG further upstream.
    Length:197
    Mass (Da):22,520
    Last modified:July 28, 2009 - v3
    <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:i82AFF5E1CE287957
    GO
    Isoform p22 (identifier: P36639-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: Missing.

    Show »
    Length:179
    Mass (Da):20,296
    Checksum:i7C9F192384F66C61
    GO
    Isoform p21 (identifier: P36639-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: Missing.

    Show »
    Length:171
    Mass (Da):19,467
    Checksum:i06DE501D75A8B3D6
    GO
    Isoform p18 (identifier: P36639-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: Missing.

    Show »
    Length:156
    Mass (Da):17,952
    Checksum:iB9FB669FF0ACFF5F
    GO

    <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
    7,8-dihydro-8-oxoguanine triphospha...
    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_in_disease">'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_06871577G → W. Corresponds to variant dbSNP:rs11547459Ensembl.1
    Natural variantiVAR_013757124V → M Associated with type I diabetes in Japanese female population; may be associated with an increased risk for small cell lung carcinoma (SCLC); decreased efficiency of translocation to mitochondria. 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_0188141 – 41Missing in isoform p18. 4 PublicationsAdd BLAST41
    Alternative sequenceiVSP_0188131 – 26Missing in isoform p21. CuratedAdd BLAST26
    Alternative sequenceiVSP_0188121 – 18Missing in isoform p22. 1 PublicationAdd BLAST18

    Sequence databases

    Select the link destinations:

    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; ENSP00000343439; ENSG00000106268 [P36639-4]
    ENST00000343985; ENSP00000339503; ENSG00000106268 [P36639-2]
    ENST00000356714; ENSP00000349148; ENSG00000106268 [P36639-4]
    ENST00000397046; ENSP00000380239; ENSG00000106268 [P36639-4]
    ENST00000397048; ENSP00000380241; ENSG00000106268 [P36639-2]
    ENST00000397049; ENSP00000380242; ENSG00000106268 [P36639-4]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		4521

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:4521

    UCSC genome browser

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

    Keywords - Coding sequence diversityi

    Alternative initiation, Polymorphism

    <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_references_section">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-A42-197[»]
    3Q93X-ray1.80A/B42-197[»]
    3WHWX-ray2.70A/B42-197[»]
    3ZR0X-ray1.80A/B42-197[»]
    3ZR1X-ray1.90A/B42-197[»]
    4C9WX-ray1.65A42-197[»]
    4C9XX-ray1.20A42-197[»]
    4N1TX-ray1.60A42-197[»]
    4N1UX-ray1.60A/B42-196[»]
    5ANSX-ray1.60A42-197[»]
    5ANTX-ray2.00A/B/C42-197[»]
    5ANUX-ray1.80A42-197[»]
    5ANVX-ray1.16A42-197[»]
    5ANWX-ray1.37A42-197[»]
    5FSIX-ray1.63A42-197[»]
    5FSKX-ray1.56A42-197[»]
    5FSLX-ray1.24A42-197[»]
    5FSMX-ray1.67A42-197[»]
    5FSNX-ray1.69A42-197[»]
    5FSOX-ray1.67A42-197[»]
    5GHIX-ray1.21A/B42-197[»]
    5GHJX-ray1.20A/B42-197[»]
    5GHMX-ray1.50A/B42-197[»]
    5GHNX-ray1.39A/B42-197[»]
    5GHOX-ray1.19A/B42-197[»]
    5GHPX-ray1.19A/B42-197[»]
    5GHQX-ray1.18A/B42-197[»]
    5NGRX-ray2.20A/B42-197[»]
    5NGSX-ray1.85A/B42-197[»]
    5NGTX-ray1.54A42-197[»]
    5NHYX-ray1.72A/B42-197[»]
    5OTMX-ray1.80A/B42-197[»]
    5WS7X-ray1.00A/B42-197[»]
    6AA3X-ray2.00A44-197[»]
    6AA4X-ray1.90A44-197[»]
    6AA5X-ray1.90A44-197[»]
    6EQ2X-ray1.80A42-197[»]
    6EQ3X-ray1.80A42-197[»]
    6EQ4X-ray1.40A42-197[»]
    6EQ5X-ray1.80A42-197[»]
    6EQ6X-ray2.00A42-197[»]
    6EQ7X-ray1.50A42-197[»]
    6F1XX-ray1.90A/B42-197[»]
    6F20X-ray2.00A/B42-197[»]
    6F22X-ray1.55A/B42-197[»]
    6F23X-ray1.84A/B42-197[»]
    6GLEX-ray1.40A42-197[»]
    6GLFX-ray2.00A42-197[»]
    6GLGX-ray1.31A42-197[»]
    6GLHX-ray1.20A42-197[»]
    6GLIX-ray1.60A42-197[»]
    6GLJX-ray1.30A42-197[»]
    6GLKX-ray1.50A42-197[»]
    6GLLX-ray1.40A/B42-197[»]
    6GLMX-ray1.60A42-197[»]
    6GLNX-ray1.40A42-197[»]
    6GLOX-ray1.70A/B42-197[»]
    6GLPX-ray1.50A/B42-197[»]
    6GLQX-ray1.60A/B42-197[»]
    6GLRX-ray1.60A/B42-197[»]
    6GLSX-ray1.50A/B42-197[»]
    6GLTX-ray1.60A42-197[»]
    6GLUX-ray1.70A42-197[»]
    6GLVX-ray1.60A42-197[»]
    6IJYX-ray1.04A/B42-197[»]
    6ILIX-ray1.45A/B42-197[»]
    SMRiP36639
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110621, 14 interactors
    IntActiP36639, 9 interactors
    STRINGi9606.ENSP00000380241

    Chemistry databases

    BindingDBiP36639
    ChEMBLiCHEMBL3708265

    PTM databases

    iPTMnetiP36639
    PhosphoSitePlusiP36639

    Polymorphism and mutation databases

    BioMutaiNUDT1
    DMDMi254763430

    Proteomic databases

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

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		4521
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000339737; ENSP00000343439; ENSG00000106268 [P36639-4]
    ENST00000343985; ENSP00000339503; ENSG00000106268 [P36639-2]
    ENST00000356714; ENSP00000349148; ENSG00000106268 [P36639-4]
    ENST00000397046; ENSP00000380239; ENSG00000106268 [P36639-4]
    ENST00000397048; ENSP00000380241; ENSG00000106268 [P36639-2]
    ENST00000397049; ENSP00000380242; ENSG00000106268 [P36639-4]
    GeneIDi4521
    KEGGihsa:4521
    UCSCiuc003slr.1 human [P36639-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		4521
    DisGeNETi4521

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		NUDT1
    HGNCiHGNC:8048 NUDT1
    HPAiHPA012636
    MIMi600312 gene
    neXtProtiNX_P36639
    OpenTargetsiENSG00000106268
    PharmGKBiPA31830

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiENOG410IXIA Eukaryota
    COG0494 LUCA
    GeneTreeiENSGT00390000000341
    HOGENOMiHOG000261970
    InParanoidiP36639
    KOiK17816
    OMAiWFPLMLQ
    OrthoDBi1602447at2759
    PhylomeDBiP36639
    TreeFamiTF106348

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02879-MONOMER
    BRENDAi3.6.1.55 2681
    3.6.1.56 2681
    ReactomeiR-HSA-2393930 Phosphate bond hydrolysis by NUDT proteins
    SABIO-RKiP36639

    Miscellaneous databases

    EvolutionaryTraceiP36639

    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

    Protein Ontology

    More...    PROi    		PR:P36639

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000106268 Expressed in 175 organ(s), highest expression level in right testis
    ExpressionAtlasiP36639 baseline and differential
    GenevisibleiP36639 HS

    Family and domain databases

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

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		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_and_isoforms">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: July 28, 2009
    Last modified: June 5, 2019
    This is version 186 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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