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UniProtKB - Q96DE0 (NUD16_HUMAN)

Protein

U8 snoRNA-decapping enzyme

Gene

NUDT16

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

RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms (PubMed:20385596, PubMed:26121039). The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP (PubMed:20385596). Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (PubMed:20385596).7 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+3 Publications, Mn2+2 Publications, Co2+2 PublicationsNote: Binds 3 or 4 divalent metal cations. Acts specifically on U8 snoRNA with magnesium as cofactor. Has broad substrate specificity with bound manganese or cobalt (in vitro).2 Publications

<p>This subsection of the ‘Function’ 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

The phosphatase activity is inhibited by the product IMP.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 0.931 sec(-1) with IDP. kcat is 0.966 sec(-1) with dIDP. kcat is 0.518 sec(-1) with GDP. kcat is 0.492 sec(-1) with dGDP. kcat is 2.6 sec(-1) with XDP. kcat is 3.06 sec(-1) with ITP. kcat is 3.2 sec(-1) with dITP. The catalytic efficiency for IDP is at least 1.3-fold higher than for dIDP, 9.6-fold higher than for GDP and dGDP, 100-fold higher than for XDP, ITP and dITP.1 Publication
  1. KM=0.062 µM for IDP (at 37 degrees Celsius)1 Publication
  2. KM=0.088 µM for dIDP (at 37 degrees Celsius)1 Publication
  3. KM=0.330 µM for GDP (at 37 degrees Celsius)1 Publication
  4. KM=0.319 mM for dGDP (at 37 degrees Celsius)1 Publication
  5. KM=15.7 mM for XDP (at 37 degrees Celsius)1 Publication
  6. KM=22.1 mM for ITP (at 37 degrees Celsius)1 Publication
  7. KM=24.1 mM for dITP (at 37 degrees Celsius)1 Publication

    pH dependencei

    Gradually increased from pH 6.5 to 8.5 in its IDP hydrolyzing activity.1 Publication

    Temperature dependencei

    Exhibited a temperature-dependent increase in its IDP hydrolyzing activity up to 60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei24Substrate1 Publication1
    Binding sitei50Substrate1 Publication1
    Binding sitei57Substrate; via amide nitrogen1 Publication1
    <p>This subsection of the ‘Function’ 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 bindingi59Magnesium or manganese 1; via carbonyl oxygen1 Publication1
    Metal bindingi76Magnesium or manganese 21 Publication1
    Metal bindingi76Magnesium or manganese 3By similarity1
    Metal bindingi80Magnesium or manganese 11 Publication1
    Metal bindingi80Magnesium or manganese 3By similarity1
    Metal bindingi136Magnesium or manganese 3By similarity1
    Metal bindingi136Magnesium or manganese 4By similarity1
    Binding sitei170Substrate1 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

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the 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
    Biological processNucleotide metabolism
    LigandMagnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:MONOMER-17869

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.6.1.62 2681
    3.6.1.64 2681

    Reactome - a knowledgebase of biological pathways and processes

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

    <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:
    U8 snoRNA-decapping enzyme (EC:3.6.1.625 Publications)
    Alternative name(s):
    IDP phosphatase (EC:3.6.1.642 Publications)
    Short name:
    IDPase
    Inosine diphosphate phosphatase
    Nucleoside diphosphate-linked moiety X motif 16
    Short name:
    Nudix motif 16
    Nudix hydrolase 16
    U8 snoRNA-binding protein H29K1 Publication
    m7GpppN-mRNA hydrolase
    <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:NUDT16
    <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 3

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000198585.11

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:26442 NUDT16

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		617381 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_Q96DE0

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, 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

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		131870

    Open Targets

    More...    OpenTargetsi    		ENSG00000198585

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA134955224

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		NUDT16

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		68565926

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000571171 – 195U8 snoRNA-decapping enzymeAdd BLAST195

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		Q96DE0

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		Q96DE0

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

    More...    PaxDbi    		Q96DE0

    PeptideAtlas

    More...    PeptideAtlasi    		Q96DE0

    PRoteomics IDEntifications database

    More...    PRIDEi    		Q96DE0

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		76283

    Consortium for Top Down Proteomics

    More...    TopDownProteomicsi    		Q96DE0-1 [Q96DE0-1]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		Q96DE0

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

    More...    PhosphoSitePlusi    		Q96DE0

    <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

    Expressed strongly in lung, kidney, adrenal gland, testis, heart and brain.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000198585 Expressed in 196 organ(s), highest expression level in amniotic fluid

    CleanEx database of gene expression profiles

    More...    CleanExi    		HS_NUDT16

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		Q96DE0 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		HPA060452
    HPA062492

    <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

    Homodimer.3 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
    itself2EBI-5464685,EBI-5464685

    GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		126295, 13 interactors

    Protein interaction database and analysis system

    More...    IntActi    		Q96DE0, 1 interactor

    Molecular INTeraction database

    More...    MINTi    		Q96DE0

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000422375

    <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

    1195
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		Q96DE0

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

    More...    SMRi    		Q96DE0

    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    		Q96DE0

    <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>Domaini18 – 173Nudix hydrolasePROSITE-ProRule annotationAdd BLAST156

    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>Motifi61 – 82Nudix boxAdd 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. NUDT16 subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG410IYGP Eukaryota
    ENOG4111QA1 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00390000016224

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000007083

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG067297

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		Q96DE0

    KEGG Orthology (KO)

    More...    KOi    		K16855

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		PRVVTHF

    Database of Orthologous Groups

    More...    OrthoDBi    		EOG091G0XY4

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		Q96DE0

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR015797 NUDIX_hydrolase-like_dom_sf
    IPR000086 NUDIX_hydrolase_dom

    Pfam protein domain database

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

    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

    <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>.<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.

    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 splicing. AlignAdd to basket
    Isoform 1 (identifier: Q96DE0-1) [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
    MAGARRLELG EALALGSGWR HACHALLYAP DPGMLFGRIP LRYAILMQMR 
            60         70         80         90        100
    FDGRLGFPGG FVDTQDRSLE DGLNRELREE LGEAAAAFRV ERTDYRSSHV 
           110        120        130        140        150
    GSGPRVVAHF YAKRLTLEEL LAVEAGATRA KDHGLEVLGL VRVPLYTLRD 
           160        170        180        190 
    GVGGLPTFLE NSFIGSAREQ LLEALQDLGL LQSGSISGLK IPAHH
    Length:195
    Mass (Da):21,273
    Last modified:July 5, 2005 - v2
    <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:i4AC7EA679D1D7468
    GO
    Isoform 2 (identifier: Q96DE0-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         138-195: LGLVRVPLYT...ISGLKIPAHH → GPAWDSVPFP...MSLCCSLLTV

    Note: No experimental confirmation available.
    Show »
    Length:194
    Mass (Da):21,816
    Checksum:iF41E209A5248D017
    GO
    Isoform 3 (identifier: Q96DE0-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-46: Missing.
         174-195: ALQDLGLLQSGSISGLKIPAHH → AALHGPMKTEMRTLVLGREGRTWECFLIGSER

    Note: No experimental confirmation available.Curated
    Show »
    Length:159
    Mass (Da):17,676
    Checksum:iA73EF509993E7BB5
    GO
    Isoform 4 (identifier: Q96DE0-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-195: LGLVRVPLYT...ISGLKIPAHH → GPAWDSVPFP...MSLCCSLLTV

    Show »
    Length:227
    Mass (Da):25,259
    Checksum:iFCD1CBE3CCC3F086
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence BAB71024 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti22A → V in AAH31215 (PubMed:15489334).Curated1
    Isoform 3 (identifier: Q96DE0-3)
    Sequence conflicti128Missing in BP199028 (PubMed:16344560).Curated1

    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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0454491 – 46Missing in isoform 3. 1 PublicationAdd BLAST46
    Alternative sequenceiVSP_0454501 – 33Missing in isoform 2. 1 PublicationAdd BLAST33
    Alternative sequenceiVSP_045451138 – 195LGLVR…IPAHH → GPAWDSVPFPISSSPKAFSP PRKHPWRKVFAPLTLPSPQL SWWSWDRDHLYSELVLPTWA FCKGLSHPLPGEILSRTHSS MSLCCSLLTV in isoform 2 and isoform 4. 1 PublicationAdd BLAST58
    Alternative sequenceiVSP_045452174 – 195ALQDL…IPAHH → AALHGPMKTEMRTLVLGREG RTWECFLIGSER in isoform 3. 1 PublicationAdd BLAST22

    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
    		AK055827 mRNA Translation: BAB71024.1 Different initiation.
    AK304650 mRNA Translation: BAG65426.1
    BP199028 mRNA No translation available.
    AC010210 Genomic DNA No translation available.
    BC009546 mRNA Translation: AAH09546.1
    BC031215 mRNA Translation: AAH31215.2

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS3070.2 [Q96DE0-1]
    CCDS54640.1 [Q96DE0-4]
    CCDS54641.1 [Q96DE0-3]

    NCBI Reference Sequences

    More...    RefSeqi    		NP_001165376.1, NM_001171905.1 [Q96DE0-3]
    NP_001165377.1, NM_001171906.1 [Q96DE0-4]
    NP_689608.2, NM_152395.2 [Q96DE0-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Hs.282050

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000502852; ENSP00000422375; ENSG00000198585 [Q96DE0-4]
    ENST00000521288; ENSP00000429274; ENSG00000198585 [Q96DE0-1]
    ENST00000537561; ENSP00000440230; ENSG00000198585 [Q96DE0-3]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		131870

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:131870

    UCSC genome browser

    More...    UCSCi    		uc003eog.3 human [Q96DE0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		AK055827 mRNA Translation: BAB71024.1 Different initiation.
    AK304650 mRNA Translation: BAG65426.1
    BP199028 mRNA No translation available.
    AC010210 Genomic DNA No translation available.
    BC009546 mRNA Translation: AAH09546.1
    BC031215 mRNA Translation: AAH31215.2
    CCDSiCCDS3070.2 [Q96DE0-1]
    CCDS54640.1 [Q96DE0-4]
    CCDS54641.1 [Q96DE0-3]
    RefSeqiNP_001165376.1, NM_001171905.1 [Q96DE0-3]
    NP_001165377.1, NM_001171906.1 [Q96DE0-4]
    NP_689608.2, NM_152395.2 [Q96DE0-1]
    UniGeneiHs.282050

    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
    2XSQX-ray1.72A1-195[»]
    3COUX-ray1.80A1-195[»]
    3MGMX-ray1.80A/B1-195[»]
    5WJIX-ray2.30A/B1-195[»]
    6CO2X-ray2.49A/B1-195[»]
    ProteinModelPortaliQ96DE0
    SMRiQ96DE0
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi126295, 13 interactors
    IntActiQ96DE0, 1 interactor
    MINTiQ96DE0
    STRINGi9606.ENSP00000422375

    PTM databases

    iPTMnetiQ96DE0
    PhosphoSitePlusiQ96DE0

    Polymorphism and mutation databases

    BioMutaiNUDT16
    DMDMi68565926

    Proteomic databases

    EPDiQ96DE0
    MaxQBiQ96DE0
    PaxDbiQ96DE0
    PeptideAtlasiQ96DE0
    PRIDEiQ96DE0
    ProteomicsDBi76283
    TopDownProteomicsiQ96DE0-1 [Q96DE0-1]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000502852; ENSP00000422375; ENSG00000198585 [Q96DE0-4]
    ENST00000521288; ENSP00000429274; ENSG00000198585 [Q96DE0-1]
    ENST00000537561; ENSP00000440230; ENSG00000198585 [Q96DE0-3]
    GeneIDi131870
    KEGGihsa:131870
    UCSCiuc003eog.3 human [Q96DE0-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		131870
    DisGeNETi131870
    EuPathDBiHostDB:ENSG00000198585.11

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		NUDT16

    H-Invitational Database, human transcriptome db

    More...    H-InvDBi    		HIX0003684
    HGNCiHGNC:26442 NUDT16
    HPAiHPA060452
    HPA062492
    MIMi617381 gene
    neXtProtiNX_Q96DE0
    OpenTargetsiENSG00000198585
    PharmGKBiPA134955224

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiENOG410IYGP Eukaryota
    ENOG4111QA1 LUCA
    GeneTreeiENSGT00390000016224
    HOGENOMiHOG000007083
    HOVERGENiHBG067297
    InParanoidiQ96DE0
    KOiK16855
    OMAiPRVVTHF
    OrthoDBiEOG091G0XY4
    PhylomeDBiQ96DE0

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17869
    BRENDAi3.6.1.62 2681
    3.6.1.64 2681
    ReactomeiR-HSA-2393930 Phosphate bond hydrolysis by NUDT proteins

    Miscellaneous databases

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

    More...    ChiTaRSi    		NUDT16 human
    EvolutionaryTraceiQ96DE0

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

    More...    GenomeRNAii    		131870

    Protein Ontology

    More...    PROi    		PR:Q96DE0

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000198585 Expressed in 196 organ(s), highest expression level in amniotic fluid
    CleanExiHS_NUDT16
    GenevisibleiQ96DE0 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR015797 NUDIX_hydrolase-like_dom_sf
    IPR000086 NUDIX_hydrolase_dom
    PfamiView protein in Pfam
    PF00293 NUDIX, 1 hit
    SUPFAMiSSF55811 SSF55811, 1 hit
    PROSITEiView protein in PROSITE
    PS51462 NUDIX, 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 nameiNUD16_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: Q96DE0
    Secondary accession number(s): B4E3B4
    , E9PED4, F5GYJ1, Q96N82
    <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: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: December 5, 2018
    This is version 141 of the entry and version 2 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, 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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