ID TDT_HUMAN Reviewed; 509 AA. AC P04053; Q96E50; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2002, sequence version 2. DT 26-JUN-2007, entry version 88. DE DNA nucleotidylexotransferase (EC 2.7.7.31) (Terminal addition enzyme) DE (Terminal deoxynucleotidyltransferase) (Terminal transferase). GN Name=DNTT; Synonyms=TDT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=85289229; PubMed=2863268; RA Peterson R.C., Cheung L.C., Mattaliano R.J., White S.T., Chang L.M.S., RA Bollum F.J.; RT "Expression of human terminal deoxynucleotidyl transferase in RT Escherichia coli."; RL J. Biol. Chem. 260:10495-10502(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88190097; PubMed=2833741; RA Riley L.K., Morrow J.K., Danton M.J., Coleman M.S.; RT "Human terminal deoxyribonucleotidyltransferase: molecular cloning and RT structural analysis of the gene and 5' flanking region."; RL Proc. Natl. Acad. Sci. U.S.A. 85:2489-2493(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=21439269; PubMed=11554927; RA Ibe S., Fujita K., Toyomoto T., Shimazaki N., Kaneko R., Tanabe A., RA Takebe I., Kuroda S., Kobayashi T., Toji S., Tamai K., Yamamoto H., RA Koiwai O.; RT "Terminal deoxynucleotidyltransferase is negatively regulated by RT direct interaction with proliferating cell nuclear antigen."; RL Genes Cells 6:815-824(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 271-508. RX MEDLINE=84272638; PubMed=6087320; RA Peterson R.C., Cheung L.C., Mattaliano R.J., Chang L.M.S., RA Bollum F.J.; RT "Molecular cloning of human terminal deoxynucleotidyltransferase."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4363-4367(1984). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67. RX MEDLINE=88280821; PubMed=3395350; DOI=10.1016/0006-291X(88)90654-7; RA Koiwai O., Morita A.; RT "Isolation of putative promoter region for human terminal RT deoxynucleotidyltransferase gene."; RL Biochem. Biophys. Res. Commun. 154:91-100(1988). RN [7] RP INTERACTION WITH TDIF1. RC TISSUE=Thymus; RX MEDLINE=21367736; PubMed=11473582; RA Yamashita N., Shimazaki N., Ibe S., Kaneko R., Tanabe A., Toyomoto T., RA Fujita K., Hasegawa T., Toji S., Tamai K., Yamamoto H., Koiwai O.; RT "Terminal deoxynucleotidyltransferase directly interacts with a novel RT nuclear protein that is homologous to p65."; RL Genes Cells 6:641-652(2001). RN [8] RP INTERACTION WITH PRP19. RX MEDLINE=22858036; PubMed=12960389; DOI=10.1073/pnas.1631060100; RA Mahajan K.N., Mitchell B.S.; RT "Role of human Pso4 in mammalian DNA repair and association with RT terminal deoxynucleotidyl transferase."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003). RN [9] RP MUTAGENESIS. RX MEDLINE=94216289; PubMed=8163485; RA Yang B., Gathy K.N., Coleman M.S.; RT "Mutational analysis of residues in the nucleotide binding domain of RT human terminal deoxynucleotidyl transferase."; RL J. Biol. Chem. 269:11859-11868(1994). CC -!- FUNCTION: Template-independent DNA polymerase which catalyzes the CC random addition of deoxynucleoside 5'-triphosphate to the 3'-end CC of a DNA initiator. One of the in vivo functions of this enzyme is CC the addition of nucleotides at the junction (N region) of CC rearranged Ig heavy chain and T-cell receptor gene segments during CC the maturation of B- and T-cells. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- COFACTOR: Magnesium. CC -!- SUBUNIT: Interacts with PRP19 and TDIF1. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DISEASE: Very high levels of enzyme activity have been detected in CC certain acute leukemic cells. CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. CC -!- SIMILARITY: Contains 1 BRCT domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; K01919; AAA61136.1; -; mRNA. DR EMBL; M20703; AAA53100.1; -; mRNA. DR EMBL; M22968; AAA53100.1; JOINED; mRNA. DR EMBL; M20694; AAA53100.1; JOINED; mRNA. DR EMBL; M20695; AAA53100.1; JOINED; mRNA. DR EMBL; M20696; AAA53100.1; JOINED; mRNA. DR EMBL; M20697; AAA53100.1; JOINED; mRNA. DR EMBL; M20698; AAA53100.1; JOINED; mRNA. DR EMBL; M20699; AAA53100.1; JOINED; mRNA. DR EMBL; M20700; AAA53100.1; JOINED; mRNA. DR EMBL; M20701; AAA53100.1; JOINED; mRNA. DR EMBL; M20702; AAA53100.1; JOINED; mRNA. DR EMBL; AB046378; BAB72001.1; -; mRNA. DR EMBL; BC012920; AAH12920.1; -; mRNA. DR EMBL; M11722; AAA36726.1; -; mRNA. DR EMBL; M21195; AAA61137.1; -; Genomic_DNA. DR PIR; A23924; WXHU. DR UniGene; Hs.534206; -. DR PDB; 2COE; NMR; A=19-125. DR SMR; P04053; 148-509. DR IntAct; P04053; -. DR Ensembl; ENSG00000107447; Homo sapiens. DR KEGG; hsa:1791; -. DR H-InvDB; HIX0009072; -. DR HGNC; HGNC:2983; DNTT. DR MIM; 187410; gene. DR ArrayExpress; P04053; -. DR GermOnline; ENSG00000107447; Homo sapiens. DR RZPD-ProtExp; IOH11297; -. DR RZPD-ProtExp; RZPDo839E03123; -. DR GO; GO:0003912; F:DNA nucleotidylexotransferase activity; TAS:ProtInc. DR InterPro; IPR001357; BRCT. DR InterPro; IPR002934; DNA_pol_beta. DR InterPro; IPR002054; DNA_polX. DR InterPro; IPR001726; DNA_polXtrans. DR PANTHER; PTHR11276:SF6; DNA_polXtrans; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF01909; NTP_transf_2; 1. DR PRINTS; PR00869; DNAPOLX. DR PRINTS; PR00871; DNAPOLXTDT. DR SMART; SM00292; BRCT; 1. DR SMART; SM00483; POLXc; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00522; DNA_POLYMERASE_X; 1. KW 3D-structure; Magnesium; Metal-binding; Nucleotidyltransferase; KW Nucleus; Terminal addition; Transferase. FT CHAIN 1 509 DNA nucleotidylexotransferase. FT /FTId=PRO_0000218791. FT DOMAIN 27 124 BRCT. FT REGION 336 345 Involved in ssDNA binding (By FT similarity). FT METAL 253 253 Sodium (via carbonyl oxygen) (By FT similarity). FT METAL 255 255 Sodium (via carbonyl oxygen) (By FT similarity). FT METAL 343 343 Magnesium (By similarity). FT METAL 345 345 Magnesium (By similarity). FT METAL 433 433 Magnesium (By similarity). FT CONFLICT 452 452 S -> SP (in Ref. 2). FT CONFLICT 454 454 Missing (in Ref. 1 and 4). FT STRAND 23 25 FT STRAND 36 40 FT TURN 42 44 FT HELIX 46 58 FT STRAND 73 78 FT HELIX 81 90 FT STRAND 100 103 FT HELIX 104 112 FT STRAND 120 124 SQ SEQUENCE 509 AA; 58437 MW; 4F33A95A983B7287 CRC64; MDPPRASHLS PRKKRPRQTG ALMASSPQDI KFQDLVVFIL EKKMGTTRRA FLMELARRKG FRVENELSDS VTHIVAENNS GSDVLEWLQA QKVQVSSQPE LLDVSWLIEC IGAGKPVEMT GKHQLVVRRD YSDSTNPGPP KTPPIAVQKI SQYACQRRTT LNNCNQIFTD AFDILAENCE FRENEDSCVT FMRAASVLKS LPFTIISMKD TEGIPCLGSK VKGIIEEIIE DGESSEVKAV LNDERYQSFK LFTSVFGVGL KTSEKWFRMG FRTLSKVRSD KSLKFTRMQK AGFLYYEDLV SCVTRAEAEA VSVLVKEAVW AFLPDAFVTM TGGFRRGKKM GHDVDFLITS PGSTEDEEQL LQKVMNLWEK KGLLLYYDLV ESTFEKLRLP SRKVDALDHF QKCFLIFKLP RQRVDSDQSS WQEGKTWKAI RVDLVLCPYE RRAFALLGWT GSRQFERDLR RYATHERKMI LDNHALYDKT KRIFLKAESE EEIFAHLGLD YIEPWERNA //