Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA nucleotidylexotransferase

Gene

Dntt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator (PubMed:23856622). 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.Curated1 Publication

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).2 Publications

Cofactori

Mg2+1 PublicationNote: Can also utilize other divalent cations, such as Mn(2+) and Co2+ (in vitro).Curated1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi343 – 3431MagnesiumCombined sourcesCurated
Metal bindingi345 – 3451MagnesiumCombined sourcesCurated
Metal bindingi434 – 4341MagnesiumCombined sourcesCurated

GO - Molecular functioni

GO - Biological processi

  • DNA metabolic process Source: MGI
  • DNA modification Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Terminal addition

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi2.7.7.31. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA nucleotidylexotransferase (EC:2.7.7.312 Publications)
Alternative name(s):
Terminal addition enzyme
Terminal deoxynucleotidyltransferase1 Publication
Short name:
TDT
Short name:
Terminal transferase
Gene namesi
Name:Dntt
Synonyms:Tdt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:98659. Dntt.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi342 – 3421H → A: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi398 – 3981L → A: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi399 – 3991D → A: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi400 – 4001H → A: Reduces enzyme activity. 1 Publication
Mutagenesisi403 – 4031K → A: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi473 – 4731D → A: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi475 – 4751H → A: Nearly abolishes enzyme activity. 1 Publication

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

BgeeiP09838.
CleanExiMM_DNTT.
ExpressionAtlasiP09838. baseline and differential.
GenevisibleiP09838. MM.

Interactioni

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

STRINGi10090.ENSMUSP00000062078.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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
Regioni258 – 2625Involved in DNA binding2 Publications
Regioni333 – 3386Deoxynucleoside triphosphate bindingCombined sourcesCurated
Regioni342 – 3454Deoxynucleoside triphosphate bindingCombined sourcesCurated
Regioni449 – 4502Deoxynucleoside triphosphate bindingCombined sourcesCurated

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.
OMAiKTWKAIR.
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. AlignAdd to basket

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

        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 TKGKTVTISP LDGKVSKLQK
510 520 530
ALRVFLEAES EEEIFAHLGL DYIEPWERNA
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:
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.

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:
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:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000062078.

PTM databases

PhosphoSiteiP09838.

Proteomic databases

PRIDEiP09838.

Protocols and materials databases

DNASUi21673.
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

CTDi1791.
MGIiMGI:98659. Dntt.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi2.7.7.31. 3474.

Miscellaneous databases

EvolutionaryTraceiP09838.
NextBioi300956.
PROiP09838.
SOURCEiSearch...

Gene expression databases

BgeeiP09838.
CleanExiMM_DNTT.
ExpressionAtlasiP09838. baseline and differential.
GenevisibleiP09838. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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) IN COMPLEXES WITH MAGNESIUM; COBALT AND ATP ANALOG.
  11. "New nucleotide-competitive non-nucleoside inhibitors of terminal deoxynucleotidyl transferase: discovery, characterization, and crystal structure in complex with the target."
    Costi R., Crucitti G.C., Pescatori L., Messore A., Scipione L., Tortorella S., Amoroso A., Crespan E., Campiglia P., Maresca B., Porta A., Granata I., Novellino E., Gouge J., Delarue M., Maga G., Di Santo R.
    J. Med. Chem. 56:7431-7441(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 132-530 IN COMPLEXES WITH SYNTHETIC INHIBITORS AND NUCLEOTIDE, CATALYTIC ACTIVITY.
  12. "Structures of intermediates along the catalytic cycle of terminal deoxynucleotidyltransferase: dynamical aspects of the two-metal ion mechanism."
    Gouge J., Rosario S., Romain F., Beguin P., Delarue M.
    J. Mol. Biol. 425:4334-4352(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 132-530 IN COMPLEXES WITH ATP; CTP; TTP; NUCLEOTIDE; MAGNESIUM; MANGANESE AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF HIS-342; LEU-398; ASP-399; HIS-400; LYS-403; ASP-473 AND HIS-475.

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: June 24, 2015
This is version 163 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.