PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28241136-2	2017	Central to all 53BP1 activities is its recruitment to double-strand breaks via the interaction of the tandem Tudor domain with dimethylated lysine 20 of histone H4 (H4K20me2).	Lysine	140-146	BP1	Homo sapiens	17-20	
23172354-3	2013	At pH 6.5 a monocoordinated complex [Fe(II)(BP1)] was formed instead (K(f) = 2.1 x 10(5) M(-1)) due to electrostatic repulsion between the polyanionic dendrimer branches, as confirmed by the behavior of three analogues where glutamates were partially or completely replaced by neutral glutamines or positive lysines.	Lysine	308-315	BP1	Homo sapiens	44-47	
16166626-6	2005	In human cells, H3 Lys 79 methylation by hDOT1L likely mediates recruitment of the signaling protein 53BP1 via its paired tudor domains to double-strand breaks (DSBs).	Lysine	19-22	BP1	Homo sapiens	103-106	
23760478-0	2013	53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.	Lysine	48-51	BP1	Homo sapiens	2-5	
23760478-6	2013	53BP1 binds to nucleosomes minimally as a dimer using its previously characterized methyl-lysine-binding Tudor domain and a carboxy-terminal extension, termed the ubiquitination-dependent recruitment (UDR) motif, which interacts with the epitope formed by H2AK15ub and its surrounding residues on the H2A tail.	Lysine	90-96	BP1	Homo sapiens	2-5