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UniProtKB - P09838 (TDT_MOUSE)

Protein

DNA nucleotidylexotransferase

Gene

Dntt

Organism
Mus musculus (Mouse)
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

Isoform TDT-S: Transferase that catalyzes the nontemplated addition of nucleoside triphosphate to coding ends during V(D)J recombination (N addition). Involved in the generation of diversity in the antigen-binding region of immunoglobulin heavy and light chains and T-cell receptors during B-and T-cell development. Does not act on double-stranded DNA with blunt ends.5 Publications
Isoform TDT-L: 3'-to-5' DNA exonuclease. Involved in the generation of diversity in the antigen-binding region of immunoglobulin heavy and light chains and T-cell receptors during B-and T-cell development. Acts on single-stranded and double-stranded DNA with 3' or 5' extensions, but not on double-stranded DNA with blunt ends. Attenuates not only isoform TDT-S-catalyzed N addition, but also P (palindromic) addition in coding joins (PubMed:11938351). Lacks terminal transferase activity (PubMed:11136823, PubMed:7556063).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: Can also utilize other divalent cations, such as Mn2+ and Co2+ (in vitro).Curated1 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

In assays with isoform TDT-S.1 Publication
  1. KM=300 µM for dATP (at 35 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi343MagnesiumCombined sourcesCurated1
    Metal bindingi345MagnesiumCombined sourcesCurated1
    Metal bindingi434MagnesiumCombined sourcesCurated1

    <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, Nucleotidyltransferase, Transferase
    Biological processTerminal addition
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.7.31 3474

    <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:
    DNA nucleotidylexotransferase (EC:2.7.7.313 Publications, EC:3.1.11.-1 Publication)
    Alternative name(s):
    Terminal addition enzyme
    Terminal deoxynucleotidyltransferase1 Publication
    Short name:
    TDT
    Short name:
    Terminal transferase
    <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:Dntt
    Synonyms:Tdt
    <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>OrganismiMus musculus (Mouse)
    <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 identifieri10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
    <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
    • UP000000589 <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 19

    Organism-specific databases

    Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

    More...    MGIi    		MGI:98659 Dntt

    <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

    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>Mutagenesisi29D → A: Almost complete loss of exonuclease activity in TDT-L; when associated with A-170 and A-473. Decreased transferase activity in TDT-S; when associated with A-170 and A-473. 1 Publication1
    Mutagenesisi170D → A: Almost complete loss of exonuclease activity in TDT-L; when associated with A-29 and A-473. Decreased transferase activity in TDT-S; when associated with A-29 and A-473. 1 Publication1
    Mutagenesisi342H → A: Nearly abolishes enzyme activity. 1 Publication1
    Mutagenesisi398L → A: Nearly abolishes enzyme activity. 1 Publication1
    Mutagenesisi399D → A: Nearly abolishes enzyme activity. 1 Publication1
    Mutagenesisi400H → A: Reduces enzyme activity. 1 Publication1
    Mutagenesisi403K → A: Nearly abolishes enzyme activity. 1 Publication1
    Mutagenesisi473D → A: Almost complete loss of exonuclease activity in TDT-L; when associated with A-29 and A-170. Decreased transferase activity in TDT-S; when associated with A-29 and A-170. 1 Publication1
    Mutagenesisi473D → A: Nearly abolishes enzyme activity. 1 Publication1
    Mutagenesisi475H → A: Nearly abolishes enzyme activity. 1 Publication1

    <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_00002187921 – 510DNA nucleotidylexotransferaseAdd BLAST510

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei134PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P09838

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

    More...    PaxDbi    		P09838

    PRoteomics IDEntifications database

    More...    PRIDEi    		P09838

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P09838

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

    More...    PhosphoSitePlusi    		P09838

    <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

    Isoform TDT-L: Expressed in the thymus, and, at lower levels, in the bone marrow (PubMed:8464703, PubMed:11136823, PubMed:7556063). Detected in both cycling and noncycling pro-B and pre-B cells (at protein level) (PubMed:11938351). Isoform TDT-S: Expressed in both cycling and noncycling pro-B, but not pre-B, cells (at protein level) (PubMed:11938351). Not detected in mature peripheral or germinal center B cells (PubMed:11938351).4 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSMUSG00000025014 Expressed in 27 organ(s), highest expression level in thymus

    CleanEx database of gene expression profiles

    More...    CleanExi    		MM_DNTT

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P09838 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P09838 MM

    <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

    Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA. Interacts with TRERF1.By similarity

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		10090.ENSMUSP00000062078

    <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

    1510
    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    		P09838

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

    More...    SMRi    		P09838

    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    		P09838

    <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>Domaini27 – 124BRCTPROSITE-ProRule annotationAdd BLAST98

    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>Regioni151 – 510Mediates interaction with DNTTIP2By similarityAdd BLAST360
    Regioni258 – 262Involved in DNA binding2 Publications5
    Regioni333 – 338Deoxynucleoside triphosphate bindingCombined sourcesCurated6
    Regioni342 – 345Deoxynucleoside triphosphate bindingCombined sourcesCurated4
    Regioni449 – 450Deoxynucleoside triphosphate bindingCombined sourcesCurated2

    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>Motifi11 – 17Nuclear localization signalBy similarity7

    <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 DNA polymerase type-X family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG2534 Eukaryota
    COG1796 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000158584

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000263600

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG003670

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P09838

    KEGG Orthology (KO)

    More...    KOi    		K00977

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		KTWKAIR

    Database of Orthologous Groups

    More...    OrthoDBi    		EOG091G073W

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P09838

    TreeFam database of animal gene trees

    More...    TreeFami    		TF103012

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00027 BRCT, 1 hit
    cd00141 NT_POLXc, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		1.10.150.110, 1 hit
    3.30.210.10, 1 hit
    3.40.50.10190, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR001357 BRCT_dom
    IPR036420 BRCT_dom_sf
    IPR002054 DNA-dir_DNA_pol_X
    IPR019843 DNA_pol-X_BS
    IPR010996 DNA_pol_b-like_N
    IPR028207 DNA_pol_B_palm_palm
    IPR018944 DNA_pol_lambd_fingers_domain
    IPR027421 DNA_pol_lamdba_lyase_dom_sf
    IPR037160 DNA_Pol_thumb_sf
    IPR022312 DNA_pol_X
    IPR029398 PolB_thumb
    IPR027292 TdT
    IPR001726 TdT/Mu

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00533 BRCT, 1 hit
    PF14792 DNA_pol_B_palm, 1 hit
    PF14791 DNA_pol_B_thumb, 1 hit
    PF10391 DNA_pol_lambd_f, 1 hit
    PF14716 HHH_8, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF000817 DNA_NT, 1 hit
    PIRSF501175 TDT, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00869 DNAPOLX
    PR00871 DNAPOLXTDT

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00292 BRCT, 1 hit
    SM00483 POLXc, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF47802 SSF47802, 1 hit
    SSF52113 SSF52113, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS50172 BRCT, 1 hit
    PS00522 DNA_POLYMERASE_X, 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 (2)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 2 <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 TDT-S (identifier: P09838-2) [UniParc]FASTAAdd to basket
    Also known as: TDT-Small, TdtS1 Publication

    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
    MDPLQAVHLG PRKKRPRQLG TPVASTPYDI RFRDLVLFIL EKKMGTTRRA 
            60         70         80         90        100
    FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQL QNIKASSELE 
           110        120        130        140        150
    LLDISWLIEC MGAGKPVEMM GRHQLVVNRN SSPSPVPGSQ NVPAPAVKKI 
           160        170        180        190        200
    SQYACQRRTT LNNYNQLFTD ALDILAENDE LRENEGSCLA FMRASSVLKS 
           210        220        230        240        250
    LPFPITSMKD TEGIPCLGDK VKSIIEGIIE DGESSEAKAV LNDERYKSFK 
           260        270        280        290        300
    LFTSVFGVGL KTAEKWFRMG FRTLSKIQSD KSLRFTQMQK AGFLYYEDLV 
           310        320        330        340        350
    SCVNRPEAEA VSMLVKEAVV TFLPDALVTM TGGFRRGKMT GHDVDFLITS 
           360        370        380        390        400
    PEATEDEEQQ LLHKVTDFWK QQGLLLYCDI LESTFEKFKQ PSRKVDALDH 
           410        420        430        440        450
    FQKCFLILKL DHGRVHSEKS GQQEGKGWKA IRVDLVMCPY DRRAFALLGW 
           460        470        480        490        500
    TGSRQFERDL RRYATHERKM MLDNHALYDR TKRVFLEAES EEEIFAHLGL 
           510
    DYIEPWERNA
    Note: Major form in the thymus and the bone marrow (PubMed:8464703, PubMed:11136823). Catalyzes the nontemplated addition of nucleoside triphosphate to coding ends during V(D)J recombination (PubMed:23856622). May have a longer half-life than isoform TDT-L (PubMed:7556063).4 Publications
    Length:510
    Mass (Da):58,266
    Last modified:December 5, 2018 - 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:iCF6E850EE36EE3BF
    GO
    Isoform TDT-L (identifier: P09838-1) [UniParc]FASTAAdd to basket
    Also known as: TDT-Large, TdtL1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         482-482: K → KGKTVTISPLDGKVSKLQKAL

    Note: Exhibits 3'-to-5' DNA exonuclease activity (EC=3.1.11.-) (PubMed:23856622). May have a shorter half-life than isoform TDT-S (PubMed:7556063, PubMed:10878023).3 Publications
    Show »
    Length:530
    Mass (Da):60,331
    Checksum:iE6B109DCF39C8107
    GO

    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 conflicti26T → M in CAA48634 (PubMed:8464703).Curated1
    Sequence conflicti99L → F in CAA48634 (PubMed:8464703).Curated1
    Sequence conflicti193R → G in CAA27735 (PubMed:3755527).Curated1
    Sequence conflicti287Q → K in CAA27735 (PubMed:3755527).Curated1
    Sequence conflicti309E → Q in CAA27735 (PubMed:3755527).Curated1
    Sequence conflicti367D → H in CAA27735 (PubMed:3755527).Curated1
    Sequence conflicti441 – 445DRRAF → ECAC in CAA27735 (PubMed:3755527).Curated5

    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_059967482K → KGKTVTISPLDGKVSKLQKA L in isoform TDT-L. 3 Publications1

    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
    		X04123 mRNA Translation: CAA27735.1
    X68670 mRNA Translation: CAA48634.2
    AF316014 mRNA Translation: AAK07884.1
    AF316015 mRNA Translation: AAK07885.1
    AK087978 mRNA Translation: BAC40071.1
    AK088709 mRNA Translation: BAC40518.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS29807.1 [P09838-1]
    CCDS37984.1 [P09838-2]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		B23595

    NCBI Reference Sequences

    More...    RefSeqi    		NP_001036693.1, NM_001043228.1 [P09838-2]
    NP_033371.2, NM_009345.2 [P09838-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Mm.25620

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014 [P09838-1]
    ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014 [P09838-2]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		21673

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		mmu:21673

    UCSC genome browser

    More...    UCSCi    		uc008hlo.1 mouse [P09838-1]

    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
    		X04123 mRNA Translation: CAA27735.1
    X68670 mRNA Translation: CAA48634.2
    AF316014 mRNA Translation: AAK07884.1
    AF316015 mRNA Translation: AAK07885.1
    AK087978 mRNA Translation: BAC40071.1
    AK088709 mRNA Translation: BAC40518.1
    CCDSiCCDS29807.1 [P09838-1]
    CCDS37984.1 [P09838-2]
    PIRiB23595
    RefSeqiNP_001036693.1, NM_001043228.1 [P09838-2]
    NP_033371.2, NM_009345.2 [P09838-1]
    UniGeneiMm.25620

    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
    1JMSX-ray2.36A130-510[»]
    1KDHX-ray3.00A148-510[»]
    1KEJX-ray3.00A148-510[»]
    4I27X-ray2.60A132-510[»]
    4I28X-ray2.15A132-510[»]
    4I29X-ray2.20A132-510[»]
    4I2AX-ray1.90A132-510[»]
    4I2BX-ray2.20A132-510[»]
    4I2CX-ray2.10A132-510[»]
    4I2DX-ray2.30A132-510[»]
    4I2EX-ray2.00A132-510[»]
    4I2FX-ray2.10A132-510[»]
    4I2GX-ray2.50A132-510[»]
    4I2HX-ray2.75A132-510[»]
    4I2IX-ray2.50A132-510[»]
    4I2JX-ray2.70A132-510[»]
    4IQTX-ray2.60A132-510[»]
    4IQUX-ray2.40A132-510[»]
    4IQVX-ray2.90A132-510[»]
    4IQWX-ray2.60A132-510[»]
    4QZ8X-ray2.70A132-510[»]
    4QZ9X-ray2.05A132-510[»]
    4QZAX-ray2.15A132-510[»]
    4QZBX-ray2.15A132-510[»]
    4QZCX-ray2.75A132-510[»]
    4QZDX-ray2.70A132-510[»]
    4QZEX-ray2.25A132-510[»]
    4QZFX-ray2.60A132-510[»]
    4QZGX-ray2.75A132-510[»]
    4QZHX-ray2.60A132-510[»]
    4QZIX-ray2.65A132-510[»]
    5D46X-ray2.80A132-510[»]
    5D49X-ray1.99A132-510[»]
    5D4BX-ray2.66A/B132-510[»]
    ProteinModelPortaliP09838
    SMRiP09838
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000062078

    PTM databases

    iPTMnetiP09838
    PhosphoSitePlusiP09838

    Proteomic databases

    MaxQBiP09838
    PaxDbiP09838
    PRIDEiP09838

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		21673
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000051806; ENSMUSP00000062078; ENSMUSG00000025014 [P09838-1]
    ENSMUST00000112200; ENSMUSP00000107819; ENSMUSG00000025014 [P09838-2]
    GeneIDi21673
    KEGGimmu:21673
    UCSCiuc008hlo.1 mouse [P09838-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		1791
    MGIiMGI:98659 Dntt

    Phylogenomic databases

    eggNOGiKOG2534 Eukaryota
    COG1796 LUCA
    GeneTreeiENSGT00940000158584
    HOGENOMiHOG000263600
    HOVERGENiHBG003670
    InParanoidiP09838
    KOiK00977
    OMAiKTWKAIR
    OrthoDBiEOG091G073W
    PhylomeDBiP09838
    TreeFamiTF103012

    Enzyme and pathway databases

    BRENDAi2.7.7.31 3474

    Miscellaneous databases

    EvolutionaryTraceiP09838

    Protein Ontology

    More...    PROi    		PR:P09838

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSMUSG00000025014 Expressed in 27 organ(s), highest expression level in thymus
    CleanExiMM_DNTT
    ExpressionAtlasiP09838 baseline and differential
    GenevisibleiP09838 MM

    Family and domain databases

    CDDicd00027 BRCT, 1 hit
    cd00141 NT_POLXc, 1 hit
    Gene3Di1.10.150.110, 1 hit
    3.30.210.10, 1 hit
    3.40.50.10190, 1 hit
    InterProiView protein in InterPro
    IPR001357 BRCT_dom
    IPR036420 BRCT_dom_sf
    IPR002054 DNA-dir_DNA_pol_X
    IPR019843 DNA_pol-X_BS
    IPR010996 DNA_pol_b-like_N
    IPR028207 DNA_pol_B_palm_palm
    IPR018944 DNA_pol_lambd_fingers_domain
    IPR027421 DNA_pol_lamdba_lyase_dom_sf
    IPR037160 DNA_Pol_thumb_sf
    IPR022312 DNA_pol_X
    IPR029398 PolB_thumb
    IPR027292 TdT
    IPR001726 TdT/Mu
    PfamiView protein in Pfam
    PF00533 BRCT, 1 hit
    PF14792 DNA_pol_B_palm, 1 hit
    PF14791 DNA_pol_B_thumb, 1 hit
    PF10391 DNA_pol_lambd_f, 1 hit
    PF14716 HHH_8, 1 hit
    PIRSFiPIRSF000817 DNA_NT, 1 hit
    PIRSF501175 TDT, 1 hit
    PRINTSiPR00869 DNAPOLX
    PR00871 DNAPOLXTDT
    SMARTiView protein in SMART
    SM00292 BRCT, 1 hit
    SM00483 POLXc, 1 hit
    SUPFAMiSSF47802 SSF47802, 1 hit
    SSF52113 SSF52113, 1 hit
    PROSITEiView protein in PROSITE
    PS50172 BRCT, 1 hit
    PS00522 DNA_POLYMERASE_X, 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 nameiTDT_MOUSE
    <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: P09838
    Secondary accession number(s): Q99PD0, Q99PD1
    <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 1, 1989
    Last sequence update: December 5, 2018
    Last modified: December 5, 2018
    This is version 183 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

    <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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    UniProt is an ELIXIR core data resource
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