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P04053 (TDT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA nucleotidylexotransferase

EC=2.7.7.31
Alternative name(s):
Terminal addition enzyme
Terminal deoxynucleotidyltransferase
Short name=Terminal transferase
Gene names
Name:DNTT
Synonyms:TDT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Magnesium.

Subunit structure

Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA. Ref.9 Ref.10 Ref.11

Subcellular location

Nucleus.

Sequence similarities

Belongs to the DNA polymerase type-X family.

Contains 1 BRCT domain.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P04053-1)

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.
Isoform 2 (identifier: P04053-2)

The sequence of this isoform differs from the canonical sequence as follows:
     454-454: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509DNA nucleotidylexotransferase
PRO_0000218791

Regions

Domain27 – 12498BRCT
Region151 – 509359Mediates interaction with DNTTIP2
Region336 – 34510Involved in ssDNA binding By similarity

Sites

Metal binding2531Sodium; via carbonyl oxygen By similarity
Metal binding2551Sodium; via carbonyl oxygen By similarity
Metal binding3431Magnesium By similarity
Metal binding3451Magnesium By similarity
Metal binding4331Magnesium By similarity

Natural variations

Alternative sequence4541Missing in isoform 2.
VSP_038397
Natural variant1121R → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs6584066 [ dbSNP | Ensembl ].
VAR_058200

Experimental info

Sequence conflict511F → L in BAD97037. Ref.4
Sequence conflict2991L → P in BAD97037. Ref.4
Sequence conflict3291T → A in BAD97037. Ref.4
Sequence conflict3831T → A in BAD97037. Ref.4
Sequence conflict3891L → M in BAD97037. Ref.4
Sequence conflict4521S → SP in AAA53100. Ref.2

Secondary structure

.................. 509
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: 0EC01E380FA7E5A2

FASTA50958,536
        10         20         30         40         50         60 
MDPPRASHLS PRKKRPRQTG ALMASSPQDI KFQDLVVFIL EKKMGTTRRA FLMELARRKG 

        70         80         90        100        110        120 
FRVENELSDS VTHIVAENNS GSDVLEWLQA QKVQVSSQPE LLDVSWLIEC IRAGKPVEMT 

       130        140        150        160        170        180 
GKHQLVVRRD YSDSTNPGPP KTPPIAVQKI SQYACQRRTT LNNCNQIFTD AFDILAENCE 

       190        200        210        220        230        240 
FRENEDSCVT FMRAASVLKS LPFTIISMKD TEGIPCLGSK VKGIIEEIIE DGESSEVKAV 

       250        260        270        280        290        300 
LNDERYQSFK LFTSVFGVGL KTSEKWFRMG FRTLSKVRSD KSLKFTRMQK AGFLYYEDLV 

       310        320        330        340        350        360 
SCVTRAEAEA VSVLVKEAVW AFLPDAFVTM TGGFRRGKKM GHDVDFLITS PGSTEDEEQL 

       370        380        390        400        410        420 
LQKVMNLWEK KGLLLYYDLV ESTFEKLRLP SRKVDALDHF QKCFLIFKLP RQRVDSDQSS 

       430        440        450        460        470        480 
WQEGKTWKAI RVDLVLCPYE RRAFALLGWT GSRQFERDLR RYATHERKMI LDNHALYDKT 

       490        500 
KRIFLKAESE EEIFAHLGLD YIEPWERNA 

« Hide

Isoform 2 [UniParc].

Checksum: C72DABE3ACAEADD1
Show »

FASTA50858,408

References

« Hide 'large scale' references
[1]"Expression of human terminal deoxynucleotidyl transferase in Escherichia coli."
Peterson R.C., Cheung L.C., Mattaliano R.J., White S.T., Chang L.M.S., Bollum F.J.
J. Biol. Chem. 260:10495-10502(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLY-112.
[2]"Human terminal deoxyribonucleotidyltransferase: molecular cloning and structural analysis of the gene and 5' flanking region."
Riley L.K., Morrow J.K., Danton M.J., Coleman M.S.
Proc. Natl. Acad. Sci. U.S.A. 85:2489-2493(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-112.
[3]"Terminal deoxynucleotidyltransferase is negatively regulated by direct interaction with proliferating cell nuclear antigen."
Ibe S., Fujita K., Toyomoto T., Shimazaki N., Kaneko R., Tanabe A., Takebe I., Kuroda S., Kobayashi T., Toji S., Tamai K., Yamamoto H., Koiwai O.
Genes Cells 6:815-824(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-112.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-112.
Tissue: Thymus.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-112.
Tissue: Testis.
[7]"Isolation of putative promoter region for human terminal deoxynucleotidyltransferase gene."
Koiwai O., Morita A.
Biochem. Biophys. Res. Commun. 154:91-100(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
[8]"Molecular cloning of human terminal deoxynucleotidyltransferase."
Peterson R.C., Cheung L.C., Mattaliano R.J., Chang L.M.S., Bollum F.J.
Proc. Natl. Acad. Sci. U.S.A. 81:4363-4367(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-508 (ISOFORM 2).
[9]"Terminal deoxynucleotidyltransferase directly interacts with a novel nuclear protein that is homologous to p65."
Yamashita N., Shimazaki N., Ibe S., Kaneko R., Tanabe A., Toyomoto T., Fujita K., Hasegawa T., Toji S., Tamai K., Yamamoto H., Koiwai O.
Genes Cells 6:641-652(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TDIF1.
Tissue: Thymus.
[10]"Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone."
Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O.
Genes Cells 8:559-571(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNTTIP2 AND CORE HISTONE.
[11]"Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase."
Mahajan K.N., Mitchell B.S.
Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRP19.
[12]"Mutational analysis of residues in the nucleotide binding domain of human terminal deoxynucleotidyl transferase."
Yang B., Gathy K.N., Coleman M.S.
J. Biol. Chem. 269:11859-11868(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[13]"Solution structure of BRCT domain of terminal deoxynucleotidyltransferase."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 19-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11722 mRNA. Translation: AAA36726.1.
M20703 expand/collapse EMBL AC list , M22968, M20694, M20695, M20696, M20697, M20698, M20699, M20700, M20701, M20702 mRNA. Translation: AAA53100.1.
AB046378 mRNA. Translation: BAB72001.1.
AK223317 mRNA. Translation: BAD97037.1.
AL136181 Genomic DNA. Translation: CAH72984.1.
BC012920 mRNA. Translation: AAH12920.1.
M21195 Genomic DNA. Translation: AAA61137.1.
K01919 mRNA. Translation: AAA61136.1.
CCDSCCDS44465.1. [P04053-2]
CCDS7447.1. [P04053-1]
PIRWXHU. A23924.
RefSeqNP_001017520.1. NM_001017520.1. [P04053-2]
NP_004079.3. NM_004088.3. [P04053-1]
UniGeneHs.534206.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2COENMR-A19-125[»]
ProteinModelPortalP04053.
SMRP04053. Positions 21-125, 149-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108127. 9 interactions.
IntActP04053. 1 interaction.
STRING9606.ENSP00000360216.

Chemistry

BindingDBP04053.
ChEMBLCHEMBL4810.

PTM databases

PhosphoSiteP04053.

Polymorphism databases

DMDM311033533.

Proteomic databases

MaxQBP04053.
PaxDbP04053.
PRIDEP04053.

Protocols and materials databases

DNASU1791.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371174; ENSP00000360216; ENSG00000107447. [P04053-1]
ENST00000419175; ENSP00000401169; ENSG00000107447. [P04053-2]
GeneID1791.
KEGGhsa:1791.
UCSCuc001kmf.3. human. [P04053-1]
uc001kmg.3. human. [P04053-2]

Organism-specific databases

CTD1791.
GeneCardsGC10P098054.
H-InvDBHIX0009072.
HGNCHGNC:2983. DNTT.
HPAHPA044194.
MIM187410. gene.
neXtProtNX_P04053.
PharmGKBPA27449.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1796.
HOGENOMHOG000263600.
HOVERGENHBG003670.
InParanoidP04053.
KOK00977.
OMARRTTLNN.
OrthoDBEOG7BS4BH.
PhylomeDBP04053.
TreeFamTF103012.

Enzyme and pathway databases

SABIO-RKP04053.
SignaLinkP04053.

Gene expression databases

BgeeP04053.
CleanExHS_DNTT.
GenevestigatorP04053.

Family and domain databases

Gene3D1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. 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]
PfamPF00533. 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]
PIRSFPIRSF000817. DNA_NT. 1 hit.
PIRSF501175. TDT. 1 hit.
PRINTSPR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTSM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF81585. SSF81585. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04053.
GeneWikiTerminal_deoxynucleotidyl_transferase.
GenomeRNAi1791.
NextBio7299.
PROP04053.
SOURCESearch...

Entry information

Entry nameTDT_HUMAN
AccessionPrimary (citable) accession number: P04053
Secondary accession number(s): Q53FH1, Q5W103, Q96E50
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM