PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19218245-3	2009	Here we show that in addition to the C-tail, three (S/T)-P sites in the Smad3 linker region, Ser(208), Ser(204), and Thr(179) are phosphorylated in response to TGF-beta.	Threonine	117-120	SMAD family member 3	Homo sapiens	72-77	
19115199-7	2009	Transforming growth factor (TGF)-beta1 specifically phosphorylates beta1 integrin (threonine 788-789) via Smad-2 and Smad-3, causing a conformational change of the extracellular component with an inside-out mechanism.	Threonine	83-92	SMAD family member 3	Homo sapiens	117-123	
32733385-5	2020	These ligands signal through serine/threonine receptor complexes to activate downstream signaling mediators, Smad2 and Smad3.	Threonine	36-45	SMAD family member 3	Homo sapiens	119-124	
16156666-2	2005	We have mapped the ERK phosphorylation sites to Ser 207, Ser 203, and Thr 178 in Smad3.	Threonine	70-73	SMAD family member 3	Homo sapiens	81-86	
30251686-5	2018	Among the four sites in the Smad3 linker region, threonine-179 (T179) appears to be unique as it serves as the binding site for multiple WW-domain-containing proteins upon phosphorylation, suggesting that this phosphorylation is a key for Smad3 to engage other pathways.	Threonine	49-58	SMAD family member 3	Homo sapiens	28-33	
30589983-3	2019	The Smad3 linker region contains serine/threonine phosphorylation sites and can be phosphorylated by intracellular kinases, such as the MAPK family, cyclin-dependent kinase (CDK) family and glycogen synthase kinase-3beta (GSK-3beta).	Threonine	40-49	SMAD family member 3	Homo sapiens	4-9	
30589983-5	2019	However, recent discoveries of Smad3-interacting molecules that preferentially bind phosphorylated Smad3 linker serine/threonine residues have shown a multitude of signal transductions that either enhance or suppress TGF-beta responses associated with Smad3 turnover or cancer progression.	Threonine	119-128	SMAD family member 3	Homo sapiens	31-36	
30589983-5	2019	However, recent discoveries of Smad3-interacting molecules that preferentially bind phosphorylated Smad3 linker serine/threonine residues have shown a multitude of signal transductions that either enhance or suppress TGF-beta responses associated with Smad3 turnover or cancer progression.	Threonine	119-128	SMAD family member 3	Homo sapiens	99-104	
30589983-5	2019	However, recent discoveries of Smad3-interacting molecules that preferentially bind phosphorylated Smad3 linker serine/threonine residues have shown a multitude of signal transductions that either enhance or suppress TGF-beta responses associated with Smad3 turnover or cancer progression.	Threonine	119-128	SMAD family member 3	Homo sapiens	99-104	
30251686-5	2018	Among the four sites in the Smad3 linker region, threonine-179 (T179) appears to be unique as it serves as the binding site for multiple WW-domain-containing proteins upon phosphorylation, suggesting that this phosphorylation is a key for Smad3 to engage other pathways.	Threonine	49-58	SMAD family member 3	Homo sapiens	239-244	
29524413-0	2018	Heme oxygenase-1/carbon monoxide axis suppresses transforming growth factor-beta1-induced growth inhibition by increasing ERK1/2-mediated phosphorylation of Smad3 at Thr-179 in human hepatocellular carcinoma cell lines.	Threonine	166-169	SMAD family member 3	Homo sapiens	157-162	
29524413-6	2018	Additional experiments revealed that HO-1/CO axis selectively induces phosphorylation of Smad3 at Thr-179 residue in the linker region through activation of extracellular signal-activated kinase (ERK) 1/2.	Threonine	98-101	SMAD family member 3	Homo sapiens	89-94	
29524413-8	2018	These findings for the first time demonstrate that HO-1/CO axis confer resistance of HCC cells to TGF-beta growth inhibitory signal by increasing Smad3 phosphorylation at Thr-179 via ERK1/2 pathway.	Threonine	171-174	SMAD family member 3	Homo sapiens	146-151