Variant position: 307 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 362 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human LGKPKHCQYTWDTQMNSNLG ITAACKLRFDRIFFRAAAEEG
Mouse LGKPKHCQYTWDTKANNNLR IPAAYKHRFDRIFFRA--EEG
Rat LGKPKHCRYTWDTKANDNLR IPAACKHRFDRIFFRA--EEG
Bovine LGKPKHCQYTWDTQMNSNLG IAANCKLRFDRIFFRAAAEGG
Chicken LGKPQHCRYTWDTSSNTNLR IESKCKLRFDRLYFRPAAEGG
Xenopus laevis LGKPEHCRYTWDTKLNNNLR ACYTSRLRFDRILYRASMEGS
Xenopus tropicalis LGKPEHCRYTWDTKVNKNLR APYICRLRFDRIFFRASQEGS
Zebrafish LGKQEHCRYTWDTKANSNKT VPYVSRCRFDRIFLRSAKTAP
Caenorhabditis elegans AGSDNKTKFTWDTFKNDNKQ GFHGAKMRFDRLYW-----SG
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 362 Tyrosyl-DNA phosphodiesterase 2
297 – 297 Interaction with 5' end of substrate DNA
315 – 315 Interaction with 5' end of substrate DNA
305 – 305 L -> AFW. Decreased phosphodiesterase activity.
316 – 316 D -> N. Strongly decreased phosphodiesterase activity.
TDP2 protects transcription from abortive topoisomerase activity and is required for normal neural function.
Gomez-Herreros F.; Schuurs-Hoeijmakers J.H.; McCormack M.; Greally M.T.; Rulten S.; Romero-Granados R.; Counihan T.J.; Chaila E.; Conroy J.; Ennis S.; Delanty N.; Cortes-Ledesma F.; de Brouwer A.P.; Cavalleri G.L.; El-Khamisy S.F.; de Vries B.B.; Caldecott K.W.;
Nat. Genet. 46:516-521(2014)
Cited for: FUNCTION; TISSUE SPECIFICITY; INVOLVEMENT IN SCAR23; VARIANT VAL-307;
Reversal of DNA damage induced Topoisomerase 2 DNA-protein crosslinks by Tdp2.
Schellenberg M.J.; Perera L.; Strom C.N.; Waters C.A.; Monian B.; Appel C.D.; Vilas C.K.; Williams J.G.; Ramsden D.A.; Williams R.S.;
Nucleic Acids Res. 44:3829-3844(2016)
Cited for: X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 108-362 IN COMPLEX WITH DNA; FUNCTION; CATALYTIC ACTIVITY; COFACTOR; ACTIVE SITE; CHARACTERIZATION OF VARIANT VAL-307; MUTAGENESIS OF TYR-178; ARG-206; ASP-262; LEU-305; ASP-316; ASP-350 AND HIS-351;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.