Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P09838

- TDT_MOUSE

UniProt

P09838 - TDT_MOUSE

Protein

DNA nucleotidylexotransferase

Gene

Dntt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (16 Nov 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.

    Catalytic activityi

    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi253 – 2531Sodium; via carbonyl oxygen
    Metal bindingi255 – 2551Sodium; via carbonyl oxygen
    Metal bindingi343 – 3431Magnesium
    Metal bindingi345 – 3451Magnesium
    Metal bindingi434 – 4341Magnesium

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. DNA-directed DNA polymerase activity Source: InterPro
    3. DNA nucleotidylexotransferase activity Source: MGI
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA metabolic process Source: MGI
    2. DNA modification Source: UniProtKB-KW

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Terminal addition

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA nucleotidylexotransferase (EC:2.7.7.31)
    Alternative name(s):
    Terminal addition enzyme
    Terminal deoxynucleotidyltransferase
    Short name:
    TDT
    Short name:
    Terminal transferase
    Gene namesi
    Name:Dntt
    Synonyms:Tdt
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:98659. Dntt.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 530530DNA nucleotidylexotransferasePRO_0000218792Add
    BLAST

    Proteomic databases

    PRIDEiP09838.

    PTM databases

    PhosphoSiteiP09838.

    Expressioni

    Gene expression databases

    ArrayExpressiP09838.
    BgeeiP09838.
    CleanExiMM_DNTT.
    GenevestigatoriP09838.

    Interactioni

    Subunit structurei

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

    Structurei

    Secondary structure

    1
    530
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi154 – 1563
    Helixi166 – 18116
    Helixi185 – 19915
    Helixi208 – 2114
    Helixi219 – 23113
    Helixi235 – 2428
    Helixi244 – 25310
    Helixi260 – 2689
    Helixi274 – 2796
    Helixi287 – 2948
    Helixi296 – 3005
    Helixi305 – 32218
    Beta strandi327 – 3304
    Helixi332 – 3354
    Beta strandi339 – 3424
    Beta strandi344 – 3496
    Helixi355 – 37218
    Beta strandi375 – 3817
    Beta strandi394 – 3963
    Beta strandi401 – 41111
    Helixi412 – 4143
    Beta strandi425 – 43713
    Helixi440 – 4423
    Helixi443 – 4519
    Helixi454 – 46815
    Beta strandi470 – 4723
    Beta strandi477 – 4793
    Turni480 – 4823
    Beta strandi504 – 5063
    Helixi511 – 5188
    Helixi525 – 5273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JMSX-ray2.36A130-530[»]
    1KDHX-ray3.00A148-530[»]
    1KEJX-ray3.00A148-530[»]
    4I27X-ray2.60A132-530[»]
    4I28X-ray2.15A132-530[»]
    4I29X-ray2.20A132-530[»]
    4I2AX-ray1.90A132-530[»]
    4I2BX-ray2.20A132-530[»]
    4I2CX-ray2.10A132-530[»]
    4I2DX-ray2.30A132-530[»]
    4I2EX-ray2.00A132-530[»]
    4I2FX-ray2.10A132-530[»]
    4I2GX-ray2.50A132-530[»]
    4I2HX-ray2.75A132-530[»]
    4I2IX-ray2.50A132-530[»]
    4I2JX-ray2.70A132-530[»]
    4IQTX-ray2.60A132-530[»]
    4IQUX-ray2.40A132-530[»]
    4IQVX-ray2.90A132-530[»]
    4IQWX-ray2.60A132-530[»]
    ProteinModelPortaliP09838.
    SMRiP09838. Positions 23-125, 149-530.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09838.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 12498BRCTPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni151 – 530380Mediates interaction with DNTTIP2By similarityAdd
    BLAST
    Regioni336 – 34510Involved in ssDNA bindingBy similarity

    Sequence similaritiesi

    Belongs to the DNA polymerase type-X family.Curated
    Contains 1 BRCT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1796.
    GeneTreeiENSGT00530000063002.
    HOGENOMiHOG000263600.
    HOVERGENiHBG003670.
    InParanoidiP09838.
    KOiK00977.
    OMAiRRTTLNN.
    OrthoDBiEOG7BS4BH.
    PhylomeDBiP09838.
    TreeFamiTF103012.

    Family and domain databases

    Gene3Di1.10.150.110. 1 hit.
    3.30.210.10. 1 hit.
    3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR002054. DNA-dir_DNA_pol_X.
    IPR019843. DNA_pol-X_BS.
    IPR010996. DNA_pol_b-like_N.
    IPR018944. DNA_pol_lambd_fingers_domain.
    IPR022312. DNA_pol_X.
    IPR027421. DNA_pol_X_lyase_dom.
    IPR002934. Nucleotidyltransferase.
    IPR029398. PolB_thumb.
    IPR027292. TdT.
    IPR001726. TdT/Mu.
    [Graphical view]
    PfamiPF00533. BRCT. 1 hit.
    PF14791. DNA_pol_B_thumb. 1 hit.
    PF10391. DNA_pol_lambd_f. 1 hit.
    PF01909. NTP_transf_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000817. DNA_NT. 1 hit.
    PIRSF501175. TDT. 1 hit.
    PRINTSiPR00869. DNAPOLX.
    PR00871. DNAPOLXTDT.
    SMARTiSM00292. BRCT. 1 hit.
    SM00483. POLXc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47802. SSF47802. 1 hit.
    SSF52113. SSF52113. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    PS00522. DNA_POLYMERASE_X. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform TDT-L (identifier: P09838-1) [UniParc]FASTAAdd to Basket

    Also known as: TDT-Large, TdtL

    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

    MDPLQAVHLG PRKKRPRQLG TPVASTPYDI RFRDLVLFIL EKKMGTTRRA    50
    FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQL QNIKASSELE 100
    LLDISWLIEC MGAGKPVEMM GRHQLVVNRN SSPSPVPGSQ NVPAPAVKKI 150
    SQYACQRRTT LNNYNQLFTD ALDILAENDE LRENEGSCLA FMRASSVLKS 200
    LPFPITSMKD TEGIPCLGDK VKSIIEGIIE DGESSEAKAV LNDERYKSFK 250
    LFTSVFGVGL KTAEKWFRMG FRTLSKIQSD KSLRFTQMQK AGFLYYEDLV 300
    SCVNRPEAEA VSMLVKEAVV TFLPDALVTM TGGFRRGKMT GHDVDFLITS 350
    PEATEDEEQQ LLHKVTDFWK QQGLLLYCDI LESTFEKFKQ PSRKVDALDH 400
    FQKCFLILKL DHGRVHSEKS GQQEGKGWKA IRVDLVMCPY DRRAFALLGW 450
    TGSRQFERDL RRYATHERKM MLDNHALYDR TKGKTVTISP LDGKVSKLQK 500
    ALRVFLEAES EEEIFAHLGL DYIEPWERNA 530

    Note: Inactivated at physiological temperature but is stable at lower temperatures.

    Length:530
    Mass (Da):60,331
    Last modified:November 16, 2001 - v3
    Checksum:iE6B109DCF39C8107
    GO
    Isoform TDT-S (identifier: P09838-2) [UniParc]FASTAAdd to Basket

    Also known as: TDT-Small, TdtS

    The sequence of this isoform differs from the canonical sequence as follows:
         483-502: Missing.

    Note: Major form.

    Show »
    Length:510
    Mass (Da):58,266
    Checksum:iCF6E850EE36EE3BF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261T → M in CAA48634. (PubMed:8464703)Curated
    Sequence conflicti99 – 991L → F in CAA48634. (PubMed:8464703)Curated
    Sequence conflicti193 – 1931R → G in CAA27735. (PubMed:3755527)Curated
    Sequence conflicti287 – 2871Q → K in CAA27735. (PubMed:3755527)Curated
    Sequence conflicti309 – 3091E → Q in CAA27735. (PubMed:3755527)Curated
    Sequence conflicti367 – 3671D → H in CAA27735. (PubMed:3755527)Curated
    Sequence conflicti441 – 4455DRRAF → ECAC in CAA27735. (PubMed:3755527)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei483 – 50220Missing in isoform TDT-S. 1 PublicationVSP_001309Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

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

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS29807.1. [P09838-1 ]
    CCDS37984.1. [P09838-2 ]
    PIRi B23595.
    RefSeqi NP_001036693.1. NM_001043228.1. [P09838-2 ]
    NP_033371.2. NM_009345.2. [P09838-1 ]
    UniGenei Mm.25620.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JMS X-ray 2.36 A 130-530 [» ]
    1KDH X-ray 3.00 A 148-530 [» ]
    1KEJ X-ray 3.00 A 148-530 [» ]
    4I27 X-ray 2.60 A 132-530 [» ]
    4I28 X-ray 2.15 A 132-530 [» ]
    4I29 X-ray 2.20 A 132-530 [» ]
    4I2A X-ray 1.90 A 132-530 [» ]
    4I2B X-ray 2.20 A 132-530 [» ]
    4I2C X-ray 2.10 A 132-530 [» ]
    4I2D X-ray 2.30 A 132-530 [» ]
    4I2E X-ray 2.00 A 132-530 [» ]
    4I2F X-ray 2.10 A 132-530 [» ]
    4I2G X-ray 2.50 A 132-530 [» ]
    4I2H X-ray 2.75 A 132-530 [» ]
    4I2I X-ray 2.50 A 132-530 [» ]
    4I2J X-ray 2.70 A 132-530 [» ]
    4IQT X-ray 2.60 A 132-530 [» ]
    4IQU X-ray 2.40 A 132-530 [» ]
    4IQV X-ray 2.90 A 132-530 [» ]
    4IQW X-ray 2.60 A 132-530 [» ]
    ProteinModelPortali P09838.
    SMRi P09838. Positions 23-125, 149-530.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P09838.

    Proteomic databases

    PRIDEi P09838.

    Protocols and materials databases

    DNASUi 21673.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000051806 ; ENSMUSP00000062078 ; ENSMUSG00000025014 . [P09838-1 ]
    ENSMUST00000112200 ; ENSMUSP00000107819 ; ENSMUSG00000025014 . [P09838-2 ]
    GeneIDi 21673.
    KEGGi mmu:21673.
    UCSCi uc008hlo.1. mouse. [P09838-1 ]

    Organism-specific databases

    CTDi 1791.
    MGIi MGI:98659. Dntt.

    Phylogenomic databases

    eggNOGi COG1796.
    GeneTreei ENSGT00530000063002.
    HOGENOMi HOG000263600.
    HOVERGENi HBG003670.
    InParanoidi P09838.
    KOi K00977.
    OMAi RRTTLNN.
    OrthoDBi EOG7BS4BH.
    PhylomeDBi P09838.
    TreeFami TF103012.

    Miscellaneous databases

    EvolutionaryTracei P09838.
    NextBioi 300956.
    PROi P09838.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09838.
    Bgeei P09838.
    CleanExi MM_DNTT.
    Genevestigatori P09838.

    Family and domain databases

    Gene3Di 1.10.150.110. 1 hit.
    3.30.210.10. 1 hit.
    3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR002054. DNA-dir_DNA_pol_X.
    IPR019843. DNA_pol-X_BS.
    IPR010996. DNA_pol_b-like_N.
    IPR018944. DNA_pol_lambd_fingers_domain.
    IPR022312. DNA_pol_X.
    IPR027421. DNA_pol_X_lyase_dom.
    IPR002934. Nucleotidyltransferase.
    IPR029398. PolB_thumb.
    IPR027292. TdT.
    IPR001726. TdT/Mu.
    [Graphical view ]
    Pfami PF00533. BRCT. 1 hit.
    PF14791. DNA_pol_B_thumb. 1 hit.
    PF10391. DNA_pol_lambd_f. 1 hit.
    PF01909. NTP_transf_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000817. DNA_NT. 1 hit.
    PIRSF501175. TDT. 1 hit.
    PRINTSi PR00869. DNAPOLX.
    PR00871. DNAPOLXTDT.
    SMARTi SM00292. BRCT. 1 hit.
    SM00483. POLXc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47802. SSF47802. 1 hit.
    SSF52113. SSF52113. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    PS00522. DNA_POLYMERASE_X. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of bovine and mouse terminal deoxynucleotidyltransferase cDNAs expressible in mammalian cells."
      Koiwai O., Yokota T., Kageyama T., Hirose T., Yoshida S., Arai K.
      Nucleic Acids Res. 14:5777-5792(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Differential splicing in mouse thymus generates two forms of terminal deoxynucleotidyl transferase."
      Doyen N., Fanton D'Andon M., Bentolila L.A., Nguyen T.Q., Rougeon F.
      Nucleic Acids Res. 21:1187-1191(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Thymus.
    3. Doyen N.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 443-445.
    4. "The long isoform of terminal deoxynucleotidyl transferase (TdtL) enters the nucleus and, rather than catalyzing N addition, modulates the catalytic activity of the short isoform."
      Benedict C.L., Gilfillan S., Kearney J.F.
      J. Exp. Med. 193:89-99(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TDT-L AND TDT-S), CHARACTERIZATION.
      Strain: C57BL/6.
      Tissue: Thymus.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
      Tissue: Thymus.
    6. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 388-393, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    7. "The two isoforms of mouse terminal deoxynucleotidyl transferase differ in both the ability to add N regions and subcellular localization."
      Bentolila L.A., Fanton D'Andon M., Nguyen T.Q., Martinez O., Rougeon F., Doyen N.
      EMBO J. 14:4221-4229(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY CHARACTERIZATION OF ALTERNATIVE FORMS.
    8. "Comparison of the two murine terminal deoxynucleotidyltransferase isoforms. A 20-amino acid insertion in the highly conserved carboxyl-terminal region modifies the thermosensitivity but not the catalytic activity."
      Boule J.-B., Rougeon F., Papanicolaou C.
      J. Biol. Chem. 275:28984-28988(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF ALTERNATIVE FORMS.
    9. Erratum
      Boule J.-B., Rougeon F., Papanicolaou C.
      J. Biol. Chem. 275:33184-33184(2000) [PubMed] [Europe PMC] [Abstract]
    10. "Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase."
      Delarue M., Boule J.-B., Lescar J., Expert-Bezancon N., Jourdan N., Sukumar N., Rougeon F., Papanicolaou C.
      EMBO J. 21:427-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 130-530 (ISOFORM TLT-S).

    Entry informationi

    Entry nameiTDT_MOUSE
    AccessioniPrimary (citable) accession number: P09838
    Secondary accession number(s): Q99PD0, Q99PD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 16, 2001
    Last modified: October 1, 2014
    This is version 154 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3