PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15907489-0	2005	Roles for lysine residues of the MH2 domain of Smad3 in transforming growth factor-beta signaling.	Lysine	10-16	SMAD family member 3	Homo sapiens	47-52	
16862174-4	2007	A major acetylation site of Smad3 by p300/CBP is Lys-378 in the MH2 domain (Smad3C) known to be critical for the regulation of transcriptional activity.	Lysine	49-52	SMAD family member 3	Homo sapiens	28-33	
17074756-7	2006	Mutation of Lys(19) also reduced the p300-mediated acetylation of Smad3.	Lysine	12-15	SMAD family member 3	Homo sapiens	66-71	
17074756-10	2006	Acetylation of Lys(19) also enhanced the DNA binding activity of Smad3.	Lysine	15-18	SMAD family member 3	Homo sapiens	65-70	
15907489-4	2005	In this study, we examined the roles for four lysine residues (Lys-333, Lys-341, Lys-378, and Lys-409) in the Smad3 MH2 domain.	Lysine	46-52	SMAD family member 3	Homo sapiens	110-115	
15907489-9	2005	Thus, the lysine residues of Smad3 MH2 domain play important roles in the transcriptional regulation of TGF-beta signals through TbetaR-I.	Lysine	10-16	SMAD family member 3	Homo sapiens	29-34	
10846168-4	2000	This basic motif (Lys(40-)Lys-Leu-Lys-Lys(44)), conserved among all the pathway-specific Smad proteins, is required for Smad 3 nuclear import in response to ligand.	Lysine	18-21	SMAD family member 3	Homo sapiens	120-126	
10846168-4	2000	This basic motif (Lys(40-)Lys-Leu-Lys-Lys(44)), conserved among all the pathway-specific Smad proteins, is required for Smad 3 nuclear import in response to ligand.	Lysine	26-29	SMAD family member 3	Homo sapiens	120-126	
10846168-4	2000	This basic motif (Lys(40-)Lys-Leu-Lys-Lys(44)), conserved among all the pathway-specific Smad proteins, is required for Smad 3 nuclear import in response to ligand.	Lysine	26-29	SMAD family member 3	Homo sapiens	120-126	
10846168-4	2000	This basic motif (Lys(40-)Lys-Leu-Lys-Lys(44)), conserved among all the pathway-specific Smad proteins, is required for Smad 3 nuclear import in response to ligand.	Lysine	26-29	SMAD family member 3	Homo sapiens	120-126	
10884415-3	2000	An NLS-like basic motif (Lys(40)-Lys-Leu-Lys-Lys(44)), conserved among all pathway-specific Smad proteins, not only is responsible for constitutive nuclear localization of the isolated Smad 3 MH1 domain but also is crucial for Smad 3 nuclear import in response to ligand.	Lysine	25-28	SMAD family member 3	Homo sapiens	185-191	
10884415-3	2000	An NLS-like basic motif (Lys(40)-Lys-Leu-Lys-Lys(44)), conserved among all pathway-specific Smad proteins, not only is responsible for constitutive nuclear localization of the isolated Smad 3 MH1 domain but also is crucial for Smad 3 nuclear import in response to ligand.	Lysine	25-28	SMAD family member 3	Homo sapiens	227-233	
10884415-3	2000	An NLS-like basic motif (Lys(40)-Lys-Leu-Lys-Lys(44)), conserved among all pathway-specific Smad proteins, not only is responsible for constitutive nuclear localization of the isolated Smad 3 MH1 domain but also is crucial for Smad 3 nuclear import in response to ligand.	Lysine	33-36	SMAD family member 3	Homo sapiens	185-191	
10884415-3	2000	An NLS-like basic motif (Lys(40)-Lys-Leu-Lys-Lys(44)), conserved among all pathway-specific Smad proteins, not only is responsible for constitutive nuclear localization of the isolated Smad 3 MH1 domain but also is crucial for Smad 3 nuclear import in response to ligand.	Lysine	33-36	SMAD family member 3	Homo sapiens	227-233	
10884415-3	2000	An NLS-like basic motif (Lys(40)-Lys-Leu-Lys-Lys(44)), conserved among all pathway-specific Smad proteins, not only is responsible for constitutive nuclear localization of the isolated Smad 3 MH1 domain but also is crucial for Smad 3 nuclear import in response to ligand.	Lysine	33-36	SMAD family member 3	Homo sapiens	185-191	
10884415-3	2000	An NLS-like basic motif (Lys(40)-Lys-Leu-Lys-Lys(44)), conserved among all pathway-specific Smad proteins, not only is responsible for constitutive nuclear localization of the isolated Smad 3 MH1 domain but also is crucial for Smad 3 nuclear import in response to ligand.	Lysine	33-36	SMAD family member 3	Homo sapiens	227-233	
10884415-3	2000	An NLS-like basic motif (Lys(40)-Lys-Leu-Lys-Lys(44)), conserved among all pathway-specific Smad proteins, not only is responsible for constitutive nuclear localization of the isolated Smad 3 MH1 domain but also is crucial for Smad 3 nuclear import in response to ligand.	Lysine	33-36	SMAD family member 3	Homo sapiens	185-191	
10884415-3	2000	An NLS-like basic motif (Lys(40)-Lys-Leu-Lys-Lys(44)), conserved among all pathway-specific Smad proteins, not only is responsible for constitutive nuclear localization of the isolated Smad 3 MH1 domain but also is crucial for Smad 3 nuclear import in response to ligand.	Lysine	33-36	SMAD family member 3	Homo sapiens	227-233	
10531318-5	1999	Deletion of the MH1 domain as well as mutations of four lysine residues in the MH1 domain abrogated the inhibitory activity of Smad3, but did not compromise the self-stimulatory function.	Lysine	56-62	SMAD family member 3	Homo sapiens	127-132	
34908107-7	2022	siRNAs for MAB21L4 did not inhibit the binding of Smad3 to their target genomic regions but down-regulated the acetylation of histone H3 lys 27 (H3K27ac), an active mark, near the Smad3 binding regions.	Lysine	137-140	SMAD family member 3	Homo sapiens	180-185	
34347311-9	2021	The Ac-SDpsiKP analogue (whereby the peptide bond between the aspartate and lysine is reduced) peptide inhibited TGF-beta/ small mother against decapentaplegic (Smad)-3 signalling and collagen deposition.	Lysine	76-82	SMAD family member 3	Homo sapiens	123-168