Reviewed,
UniProtKB/Swiss-Prot P04053 (TDT_HUMAN)
Last modified
June 16, 2009.
Version 109.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: DNA nucleotidylexotransferase EC=2.7.7.31 Alternative name(s): Terminal addition enzyme Terminal deoxynucleotidyltransferase Short name=Terminal transferase | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 509 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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.7 Ref.8 Ref.9 |
| Subcellular location | |
| Involvement in disease | Very high levels of enzyme activity have been detected in certain acute leukemic cells. |
| Sequence similarities | Belongs to the DNA polymerase type-X family. Contains 1 BRCT domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Terminal addition |
| Cellular component | Nucleus |
| Ligand | Magnesium Metal-binding |
| Molecular function | Nucleotidyltransferase Transferase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | DNA modification Inferred from electronic annotation. Source: UniProtKB-KW DNA replicationInferred from electronic annotation. Source: InterPro |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: InterPro DNA nucleotidylexotransferase activity Ref.1Traceable author statement. Source: ProtInc DNA-directed DNA polymerase activityInferred from electronic annotation. Source: InterPro magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 509 | 509 | DNA nucleotidylexotransferase | PRO_0000218791 | ||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||
| Domain | 27 – 124 | 98 | BRCT | |||||||||||||||||||||||
| Region | 151 – 509 | 359 | Mediates interaction with DNTTIP2 | |||||||||||||||||||||||
| Region | 336 – 345 | 10 | Involved in ssDNA binding By similarity | |||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||
| Metal binding | 253 | 1 | Sodium; via carbonyl oxygen By similarity | |||||||||||||||||||||||
| Metal binding | 255 | 1 | Sodium; via carbonyl oxygen By similarity | |||||||||||||||||||||||
| Metal binding | 343 | 1 | Magnesium By similarity | |||||||||||||||||||||||
| Metal binding | 345 | 1 | Magnesium By similarity | |||||||||||||||||||||||
| Metal binding | 433 | 1 | Magnesium By similarity | |||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||
| Sequence conflict | 452 | 1 | S → SP in AAA53100. Ref.2 | |||||||||||||||||||||||
| Sequence conflict | 454 | 1 | Missing Ref.1 | |||||||||||||||||||||||
| Sequence conflict | 454 | 1 | Missing Ref.4 | |||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||
| Beta strand | 23 – 25 | 3 | ||||||||||||||||||||||||
| Beta strand | 36 – 40 | 5 | ||||||||||||||||||||||||
| Turn | 42 – 44 | 3 | ||||||||||||||||||||||||
| Helix | 46 – 58 | 13 | ||||||||||||||||||||||||
| Beta strand | 73 – 78 | 6 | ||||||||||||||||||||||||
| Helix | 81 – 90 | 10 | ||||||||||||||||||||||||
| Beta strand | 100 – 103 | 4 | ||||||||||||||||||||||||
| Helix | 104 – 112 | 9 | ||||||||||||||||||||||||
| Beta strand | 120 – 124 | 5 | ||||||||||||||||||||||||
Sequences
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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] | "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. |
| [5] | "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. |
| [6] | "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. |
| [7] | "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. |
| [8] | "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. |
| [9] | "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. |
| [10] | "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. |
| [11] | "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 | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| K01919 mRNA. Translation: AAA61136.1. M20703 M20702 mRNA. Translation: AAA53100.1. AB046378 mRNA. Translation: BAB72001.1. BC012920 mRNA. Translation: AAH12920.1. M11722 mRNA. Translation: AAA36726.1. M21195 Genomic DNA. Translation: AAA61137.1. | |||||||||||||
| IPI | IPI00219676. | ||||||||||||
| PIR | WXHU. A23924. | ||||||||||||
| RefSeq | NP_001017520.1. NP_004079.3. | ||||||||||||
| UniGene | Hs.534206 | ||||||||||||
3D structure databases | |||||||||||||
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| SMR | P04053. Positions 148-509. | ||||||||||||
| ModBase | Search... | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P04053. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P04053. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000107447. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 1791. | ||||||||||||
| KEGG | hsa:1791. | ||||||||||||
Organism-specific databases | |||||||||||||
| GeneCards | GC10P098054. | ||||||||||||
| H-InvDB | HIX0009072. | ||||||||||||
| HGNC | HGNC:2983. DNTT. | ||||||||||||
| MIM | 187410. gene. | ||||||||||||
| PharmGKB | PA27449. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P04053. | ||||||||||||
| HOVERGEN | P04053. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 2.7.7.31. 247. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P04053. | ||||||||||||
| Bgee | P04053. | ||||||||||||
| CleanEx | HS_DNTT. | ||||||||||||
| GermOnline | ENSG00000107447. Homo sapiens. | ||||||||||||
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. IPR019843. DNA_pol-X_BS. IPR018944. DNA_pol_lambd_fingers_domain. IPR002934. Nucleotidyltransferase. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.150.110. DNA_pol_b_N-like. 1 hit. | ||||||||||||
| PANTHER | PTHR11276:SF6. DNA_polXtrans. 1 hit. | ||||||||||||
| Pfam | PF00533. BRCT. 1 hit. PF10391. DNA_pol_lambd_f. 1 hit. PF01909. NTP_transf_2. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF000817. DNA_NT. 1 hit. | ||||||||||||
| PRINTS | PR00869. DNAPOLX. PR00871. DNAPOLXTDT. | ||||||||||||
| SMART | SM00292. BRCT. 1 hit. SM00483. POLXc. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS50172. BRCT. 1 hit. PS00522. DNA_POLYMERASE_X. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 7299. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | TDT_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P04053 Secondary accession number(s): Q96E50 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| 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 |

Clusters with


