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UniProtKB/Swiss-Prot entry P04053


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TDT_HUMAN
Primary accession number P04053
Secondary accession number Q96E50
Integrated into Swiss-Prot on November 1, 1986
Sequence was last modified on November 28, 2002 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 103)
Name and origin of the protein
Protein name DNA nucleotidylexotransferase
Synonyms EC 2.7.7.31
Terminal addition enzyme
Terminal deoxynucleotidyltransferase
Terminal transferase
Gene name
Name: DNTT
Synonyms: TDT
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2863268 [NCBI, ExPASy, EBI, Israel, Japan]
Peterson R.C., Cheung L.C., Mattaliano R.J., White S.T., Chang L.M.S., Bollum F.J.;
"Expression of human terminal deoxynucleotidyl transferase in Escherichia coli.";
J. Biol. Chem. 260:10495-10502(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2833741 [NCBI, ExPASy, EBI, Israel, Japan]
Riley L.K., Morrow J.K., Danton M.J., Coleman M.S.;
"Human terminal deoxyribonucleotidyltransferase: molecular cloning and structural analysis of the gene and 5' flanking region.";
Proc. Natl. Acad. Sci. U.S.A. 85:2489-2493(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11554927 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Terminal deoxynucleotidyltransferase is negatively regulated by direct interaction with proliferating cell nuclear antigen.";
Genes Cells 6:815-824(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 271-508.
PubMed=6087320 [NCBI, ExPASy, EBI, Israel, Japan]
Peterson R.C., Cheung L.C., Mattaliano R.J., Chang L.M.S., Bollum F.J.;
"Molecular cloning of human terminal deoxynucleotidyltransferase.";
Proc. Natl. Acad. Sci. U.S.A. 81:4363-4367(1984).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
DOI=10.1016/0006-291X(88)90654-7; PubMed=3395350 [NCBI, ExPASy, EBI, Israel, Japan]
Koiwai O., Morita A.;
"Isolation of putative promoter region for human terminal deoxynucleotidyltransferase gene.";
Biochem. Biophys. Res. Commun. 154:91-100(1988).
[7]
INTERACTION WITH TDIF1.
TISSUE=Thymus;
PubMed=11473582 [NCBI, ExPASy, EBI, Israel, Japan]
Yamashita N., Shimazaki N., Ibe S., Kaneko R., Tanabe A., Toyomoto T., Fujita K., Hasegawa T., Toji S., Tamai K., Yamamoto H., Koiwai O.;
"Terminal deoxynucleotidyltransferase directly interacts with a novel nuclear protein that is homologous to p65.";
Genes Cells 6:641-652(2001).
[8]
INTERACTION WITH DNTTIP2 AND CORE HISTONE.
DOI=10.1046/j.1365-2443.2003.00656.x; PubMed=12786946 [NCBI, ExPASy, EBI, Israel, Japan]
Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O.;
"Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone.";
Genes Cells 8:559-571(2003).
[9]
INTERACTION WITH PRP19.
DOI=10.1073/pnas.1631060100; PubMed=12960389 [NCBI, ExPASy, EBI, Israel, Japan]
Mahajan K.N., Mitchell B.S.;
"Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase.";
Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003).
[10]
MUTAGENESIS.
PubMed=8163485 [NCBI, ExPASy, EBI, Israel, Japan]
Yang B., Gathy K.N., Coleman M.S.;
"Mutational analysis of residues in the nucleotide binding domain of human terminal deoxynucleotidyl transferase.";
J. Biol. Chem. 269:11859-11868(1994).
[11]
STRUCTURE BY NMR OF 19-125.
RIKEN structural genomics initiative (RSGI);
"Solution structure of BRCT domain of terminal deoxynucleotidyltransferase.";
Submitted (NOV-2005) to the PDB data bank.
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: Interacts with PRP19 and DNTTIP1. Forms a ternary complex with DNTTIP2 and core histone. Released from this complex by PCNA.
  • SUBCELLULAR LOCATION: Nucleus.
  • DISEASE: Very high levels of enzyme activity have been detected in certain acute leukemic cells.
  • SIMILARITY: Belongs to the DNA polymerase type-X family.
  • SIMILARITY: Contains 1 BRCT domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K01919; AAA61136.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20703; AAA53100.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22968; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20694; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20695; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20696; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20697; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20698; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20699; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20700; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20701; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20702; AAA53100.1; JOINED; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB046378; BAB72001.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012920; AAH12920.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11722; AAA36726.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21195; AAA61137.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A23924; WXHU.
RefSeq NP_001017520.1; -.
NP_004079.3; -.
UniGene Hs.534206
3D structure databases
PDB
2COE; NMR; -; A=19-125.[ExPASy / RCSB / EBI]
PDBsum 2COE; -.
SMR P04053; 148-509.
ModBase P04053.
PTM databases
PhosphoSite P04053; -.
Organism-specific databases
H-InvDB HIX0009072; -.
HGNC HGNC:2983; DNTT.
GenAtlas DNTT.
MIM 187410; gene. [NCBI / EBI]
PharmGKB PA27449; -.
GeneCards P04053.
Gene expression databases
ArrayExpress P04053; -.
CleanEx HS_DNTT; -.
GermOnline ENSG00000107447; Homo sapiens.
Ontologies
GO
GO:0003912; Molecular function: DNA nucleotidylexotransferase activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001357; BRCT.
IPR002054; DNA-dir_DNA_pol_X.
IPR010996; DNA-dir_DNA_pol_X_beta-like_N.
IPR001726; DNA_nucleotidylexotransferase.
IPR002934; Nucleotidyltransferase.
Graphical view of domain structure.
Gene3D G3DSA:1.10.150.110; DNA_pol_b_N-like; 1.
PANTHER PTHR11276:SF6; DNA_polXtrans; 1.
Pfam PF00533; BRCT; 1.
PF01909; NTP_transf_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000817; DNA_NT; 1.
PRINTS PR00869; DNAPOLX.
PR00871; DNAPOLXTDT.
SMART SM00292; BRCT; 1.
SM00483; POLXc; 1.
SMART graphical view of domain structure.
PROSITE PS50172; BRCT; 1.
PS00522; DNA_POLYMERASE_X; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P04053.
ProtoNet P04053.
Genome annotation databases
Ensembl ENSG00000107447; Homo sapiens. [Contig view]
GeneID 1791; -.
KEGG hsa:1791; -.
Phylogenomic databases
HOGENOM P04053; -.
HOVERGEN P04053; -.
Other
NextBio 7299; -.
SOURCE DNTT; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Terminal addition; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   509  509     DNA nucleotidylexotransferase. PRO_0000218791
DOMAIN   27   124  98     BRCT. 
REGION   151   509  359     Mediates interaction with DNTTIP2. 
REGION   336   345  10     Involved in ssDNA binding (By similarity). 
METAL   253   253        Sodium; via carbonyl oxygen (By similarity). 
METAL   255   255        Sodium; via carbonyl oxygen (By similarity). 
METAL   343   343        Magnesium (By similarity). 
METAL   345   345        Magnesium (By similarity). 
METAL   433   433        Magnesium (By similarity). 
CONFLICT   452   452        S -> SP (in Ref. 2; AAA53100). 
CONFLICT   454   454        Missing (in Ref. 1 and 4). 
STRAND   23    25  3      
STRAND   36    40  5      
TURN   42    44  3      
HELIX   46    58  13      
STRAND   73    78  6      
HELIX   81    90  10      
STRAND   100   103  4      
HELIX   104   112  9      
STRAND   120   124  5      
Sequence information
Length: 509 AA [This is the length of the unprocessed precursor] Molecular weight: 58437 Da [This is the MW of the unprocessed precursor] CRC64: 4F33A95A983B7287 [This is a checksum on the sequence]
        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 

P04053 in FASTA format

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