Tdp2
entrez
56196
canonical
uniprot
Q9JJX7
canonical
ensembl
ENSMUSG00000035958
resolver
ensp
ENSMUSP00000035660
resolver
enst
ENSMUST00000038039
resolver
genesymbol
Tdp2
resolver
genesymbol_syn
Ttrap
resolver
uniprot
A2RTH9
resolver
uniprot_entry
TYDP2_MOUSE
resolver
uniprot_sec
A2RTH9
resolver
amino_acid_sequence
MASGSSSDAAEPAGPAGRAASAPEAAQAEEDRVKRRRLQCLGFALVGGCDPTMVPSVLRENDWQTQKALSAYFELPENDQGWPRQPPTSFKSEAYVDLTNEDANDTTILEASPSGTPLEDSSTISFITWNIDGLDGCNLPERARGVCSCLALYSPDVVFLQEVIPPYCAYLKKRAASYTIITGNEEGYFTAILLKKGRVKFKSQEIIPFPNTKMMRNLLCVNVSLGGNEFCLMTSHLESTREHSAERIRQLKTVLGKMQEAPDSTTVIFAGDTNLRDQEVIKCGGLPDNVFDAWEFLGKPKHCQYTWDTKANNNLRIPAAYKHRFDRIFFRAEEGHLIPQSLDLVGLEKLDCGRFPSDHWGLLCTLNVVL
uniprot
proteins
ec_number
3.1.4.-
uniprot
proteins
function
FUNCTION: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DNA double-strand breaks/DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation (PubMed:23104055, PubMed:24808172, PubMed:27060144, PubMed:27099339). Thereby, protects the transcription of many genes involved in neurological development and maintenance from the abortive activity of TOP2 (PubMed:22740648). Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DSBs due to DNA damage by radiation and free radicals. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Also has 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF-beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non-canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. Acts as a regulator of ribosome biogenesis following stress (By similarity). {ECO:0000250|UniProtKB:O95551, ECO:0000269|PubMed:22740648, ECO:0000269|PubMed:23104055, ECO:0000269|PubMed:24808172, ECO:0000269|PubMed:27060144, ECO:0000269|PubMed:27099339}.
uniprot
proteins
mass_dalton
41034
uniprot
proteins
mutagenesis
MUTAGEN 358; /note="D->N: Loss of magnesium binding."; /evidence="ECO:0000269|PubMed:27060144
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by TRAF6. {ECO:0000250|UniProtKB:O95551}.
uniprot
proteins
protein_family
CCR4/nocturin family
uniprot
proteins
pubmed
10764746
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
22740648
uniprot
proteins
pubmed
23104055
uniprot
proteins
pubmed
24658003
uniprot
proteins
pubmed
24808172
uniprot
proteins
pubmed
27060144
uniprot
proteins
pubmed
27099339
uniprot
proteins
sequence_length
370
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95551}. Nucleus, PML body {ECO:0000250|UniProtKB:O95551}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O95551}. Cytoplasm {ECO:0000250|UniProtKB:O95551}. Note=Localizes to nucleolar cavities following stress; localization to nucleolus is dependent on PML protein. {ECO:0000250|UniProtKB:O95551}.
uniprot
proteins