PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2374612-6	1990	This reveals an evolutionarily conserved core which corresponds precisely to the 180-residue DNA binding/activation domain determined for yeast TFIID, a near absolute conservation of component structural motifs (direct repeats, central basic core/lysine repeat, and sigma homology), providing further support for their functional importance, and a unique N-terminal structure that suggests involvement in species-specific regulatory factor interactions.	Lysine	247-253	TATA-box binding protein	Homo sapiens	144-149	
7926734-6	1994	Three independently isolated derivatives of human TBP that permit yeast cell growth replace arginine 231 with lysine; the corresponding amino acid in yeast TBP (lysine 133) has been implicated in RNA polymerase III transcription.	Lysine	110-116	TATA-box binding protein	Homo sapiens	50-53	
9796820-5	1998	Molecular modelling studies indicate that this complex could be stabilized by electrostatic interactions involving the glutamate Glu287 and aspartates (Asp290, Asp294, Asp297 and Asp298) of L(281-301)TFIIA and lysine residues (Lys133, Lys138 and Lys145) and arginine residues (Arg137, Arg140) of H2(TBP) in agreement with mutagenesis experiments.	Lysine	210-216	TATA-box binding protein	Homo sapiens	299-302	
16337145-9	2006	Our study shows that ZNF76, a TBP-interacting transcriptional modulator, is regulated by both lysine modifications and alternative splicing.	Lysine	94-100	TATA-box binding protein	Homo sapiens	30-33	
34767799-9	2021	A specific arginine-to-lysine change in the highest affinity cyclic peptide reduced TAR binding by 10-fold, suggesting that TBP-derived cyclic peptides use an arginine-fork motif to recognize the TAR major-groove while differentiating the mode of binding from other TAR-targeting molecules.	Lysine	23-29	TATA-box binding protein	Homo sapiens	124-127	
24727527-2	2014	Results revealed that (a) a positively charged amino acid, lysine (K) or arginine (R), in TBP can anchor ferritin to negative zeta-potential substrates, (b) the adsorption force of K is stronger than R, and (c) local electrostatic interactions and flexibility of TBP directly affect adsorption.	Lysine	59-65	TATA-box binding protein	Homo sapiens	90-93	
24727527-2	2014	Results revealed that (a) a positively charged amino acid, lysine (K) or arginine (R), in TBP can anchor ferritin to negative zeta-potential substrates, (b) the adsorption force of K is stronger than R, and (c) local electrostatic interactions and flexibility of TBP directly affect adsorption.	Lysine	59-65	TATA-box binding protein	Homo sapiens	263-266	
15280358-9	2004	ZNF76 is sumoylated by PIAS1 at lysine 411, which is in the minimal TBP-interacting region.	Lysine	32-38	TATA-box binding protein	Homo sapiens	68-71	
12446790-4	2002	TFIIB with the G204D mutation [TFIIB(G204D)] was suppressed by hydrophobic substitutions at lysine 239 of TBP.	Lysine	92-98	TATA-box binding protein	Homo sapiens	106-109