| Tag | Content |
|---|
| CPLM ID | CPLM-013278 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tyrosyl-DNA phosphodiesterase 1 |
Protein Synonyms/Alias | Tyr-DNA phosphodiesterase 1 |
Gene Name | Tdp1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 75 | TDSVLPHKKQKMDSP | acetylation | [1] | | 232 | ILLVHGDKREAKADL | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. Has low 3'exonuclease activity and can remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate (By similarity). |
Sequence Annotation | REGION 401 404 Interaction with DNA (By similarity).
ACT_SITE 264 264 Nucleophile (By similarity).
ACT_SITE 494 494 Proton donor (By similarity).
BINDING 266 266 Substrate (By similarity).
BINDING 496 496 Substrate (By similarity).
MOD_RES 61 61 Phosphoserine (By similarity).
MOD_RES 148 148 Phosphothreonine (By similarity).
MOD_RES 149 149 Phosphoserine (By similarity). |
Keyword | Complete proteome; Cytoplasm; DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease; Nucleus; Phosphoprotein; Reference proteome; Repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 609 AA |
Protein Sequence | MSQESSYGKW TISSSDDSED EKPKPVKPST SSGPQAGQGV SKEPTYTCSE ARKAAHKRQI 60
SPVKFNNTDS VLPHKKQKMD SPEGLGWCLS SSDDEQQPDV TQQEQPKGVP PQEKKYAPSA 120
NVTTAQKVED RSPPDSHRAQ RADEEYETSG EGQDIWDMLD KENPFQFYLT RVSGIKAKYN 180
SKALHIKDIL SPLFGTLVSS AQFNYCFDVN WLIKQYPPEF RKKPILLVHG DKREAKADLH 240
AQAKPYANIS LCQAKLDIAF GTHHTKMMLL LYEEGLRVVI HTSNLIREDW HQKTQGIWLS 300
PLYPRIYQGN HTSGESSTHF KADLTSYLMA YNAPPLQEWI DIIQEHDLSE TNVYLIGSTP 360
GRFQGSHKDN WGHFRLRKLL QAHAPSAPRG ECWPVVGQFS SIGSLGPDES KWLCSEFKES 420
LLAVREEGRT PGRSAVPLHL IYPSVENVRT SLEGYPAGGS LPYGIQTAEK QRWLHPYFHK 480
WSAETSGRSN AMPHIKTYMR PSPDFSKLAW FLVTSANLSK AAWGALEKNG AQLMIRSYEL 540
GVLFLPSAFG LDTFKVKQKF FSSSSEPMAS FPVPYDLPPE LYGSKDRPWI WNIPYVKAPD 600
THGNMWVPS 609 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0017005; F:3'-tyrosyl-DNA phosphodiesterase activity; ISS:UniProtKB. GO:0003690; F:double-stranded DNA binding; IEA:Compara. GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. GO:0003697; F:single-stranded DNA binding; IEA:Compara. GO:0006302; P:double-strand break repair; IEA:Compara. GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. GO:0000012; P:single strand break repair; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |