TYDP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TYDP2_MOUSE
• UniProt AC: Q9JJX7
• Protein Name: Tyrosyl-DNA phosphodiesterase 2
• Gene Name: Tdp2
• Organism: Mus musculus (Mouse).
• Sequence Length: 370
• Subcellular Localization: Nucleus. Nucleus, PML body. Nucleus, nucleolus. Localizes to nucleolar cavities following stress; localization to nucleolus is dependent on PML protein..
• Protein Description: 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 (By similarity). 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. 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. Has also 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]
• Protein Sequence: MASGSSSDAAEPAGPAGRAASAPEAAQAEEDRVKRRRLQCLGFALVGGCDPTMVPSVLRENDWQTQKALSAYFELPENDQGWPRQPPTSFKSEAYVDLTNEDANDTTILEASPSGTPLEDSSTISFITWNIDGLDGCNLPERARGVCSCLALYSPDVVFLQEVIPPYCAYLKKRAASYTIITGNEEGYFTAILLKKGRVKFKSQEIIPFPNTKMMRNLLCVNVSLGGNEFCLMTSHLESTREHSAERIRQLKTVLGKMQEAPDSTTVIFAGDTNLRDQEVIKCGGLPDNVFDAWEFLGKPKHCQYTWDTKANNNLRIPAAYKHRFDRIFFRAEEGHLIPQSLDLVGLEKLDCGRFPSDHWGLLCTLNVVL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MASGSSSD -------CCCCCCCC	6.38	-
3	Phosphorylation	-----MASGSSSDAA -----CCCCCCCCCC	37.60	24759943
6	Phosphorylation	--MASGSSSDAAEPA --CCCCCCCCCCCCC	35.44	20139300
67	Ubiquitination	ENDWQTQKALSAYFE CCCHHHHHHHHHHCC	55.47	-
70	Phosphorylation	WQTQKALSAYFELPE HHHHHHHHHHCCCCC	26.28	26643407
99	Phosphorylation	SEAYVDLTNEDANDT CEEEEECCCCCCCCC	31.90	-
202	Ubiquitination	KKGRVKFKSQEIIPF ECCCEEECCCCEECC	45.58	22790023
252	Ubiquitination	AERIRQLKTVLGKMQ HHHHHHHHHHHHHHC	28.40	27667366
282	Ubiquitination	LRDQEVIKCGGLPDN CCCCCEEECCCCCCC	31.81	-
310	Ubiquitination	CQYTWDTKANNNLRI CEEEECCCCCCCEEC	46.79	22790023

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
99	T	Phosphorylation	Kinase	ACVR1B	Q61271	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TYDP2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TYDP2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of TYDP2_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.