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Reviewed, UniProtKB/Swiss-Prot P04053 (TDT_HUMAN)

Last modified November 3, 2009. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Keywords
   Biological processTerminal addition
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandMagnesium
Metal-binding
   Molecular functionNucleotidyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processDNA modification

Inferred from electronic annotation. Source: UniProtKB-KW

DNA replication

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA nucleotidylexotransferase activity Ref.1

Traceable author statement. Source: ProtInc

DNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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

Natural variant1121G → R: dbSNP rs6584066. Ref.5
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
Sequence conflict4541Missing in AAA36726. Ref.1
Sequence conflict4541Missing in AAA61136. Ref.8

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P04053-1 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 4F33A95A983B7287

FASTA50958,437
        10         20         30         40         50         60 
MDPPRASHLS PRKKRPRQTG ALMASSPQDI KFQDLVVFIL EKKMGTTRRA FLMELARRKG 

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

       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

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: 2863268] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 2833741] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 11554927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
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: 15164054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-112.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 3395350] [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: 6087320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-508.
[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: 11473582] [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: 12786946] [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: 12960389] [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: 8163485] [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

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.
IPIIPI00219676.
PIRWXHU. A23924.
RefSeqNP_001017520.1.
NP_004079.3.
UniGeneHs.534206

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2COENMR-A19-125[»]
SMRP04053. Positions 148-509.
ModBaseSearch...

Protein-protein interaction databases

STRINGP04053.

PTM databases

PhosphoSiteP04053.

Proteomic databases

PRIDEP04053.

Genome annotation databases

EnsemblENST00000371174; ENSP00000360216; ENSG00000107447; Homo sapiens. [Genome view]
ENST00000419175; ENSP00000401169; ENSG00000107447; Homo sapiens. [Genome view]
GeneID1791.
KEGGhsa:1791.
UCSCuc001kmf.1. human.

Organism-specific databases

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

Phylogenomic databases

HOGENOMP04053.
HOVERGENP04053.

Enzyme and pathway databases

BRENDA2.7.7.31. 247.

Gene expression databases

ArrayExpressP04053.
BgeeP04053.
CleanExHS_DNTT.
GenevestigatorP04053.
GermOnlineENSG00000107447. Homo sapiens.

Family and domain databases

InterProIPR001357. BRCT.
IPR002054. DNA-dir_DNA_pol_X.
IPR010996. DNA-dir_DNA_pol_X_beta-like_N.
IPR001726. DNA_nucleotidylexotransferase.
IPR019843. DNA_pol-X_BS.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR002934. Nucleotidyltransferase.
[Graphical view]
Gene3DG3DSA:1.10.150.110. DNA_pol_b_N-like. 1 hit.
PANTHERPTHR11276:SF6. DNA_polXtrans. 1 hit.
PfamPF00533. BRCT. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFPIRSF000817. DNA_NT. 1 hit.
PRINTSPR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTSM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
PROSITEPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio7299.
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 28, 2002
Last modified: November 3, 2009
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 10

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents