PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23139211-10 2013 The latter altered interface residues or disrupted the phosphorylation-regulated Ser-Ser-X-Ser motifs within SMAD2 and SMAD3. Serine 81-84 SMAD family member 3 Homo sapiens 119-124 25267569-4 2014 The phosphoisoforms of Smad3 studied in this article included phosphorylation at C-terminal (pSmad3C)(Ser(423/425)) and phosphorylation at the linker region (pSmad3L)(Ser(213)). Serine 102-105 SMAD family member 3 Homo sapiens 23-28 25267569-4 2014 The phosphoisoforms of Smad3 studied in this article included phosphorylation at C-terminal (pSmad3C)(Ser(423/425)) and phosphorylation at the linker region (pSmad3L)(Ser(213)). Serine 167-170 SMAD family member 3 Homo sapiens 23-28 24080014-0 2013 Serine-204 in the linker region of Smad3 mediates the collagen-I response to TGF-beta in a cell phenotype-specific manner. Serine 0-6 SMAD family member 3 Homo sapiens 35-40 24080014-6 2013 Mutations replacing serine at S204 or S208 in the linker region decreased Smad3-mediated COL1A2 promoter activity, whereas mutating T179 enhanced basal COL1A2 promoter activity and did not prevent TGF-beta stimulation. Serine 20-26 SMAD family member 3 Homo sapiens 74-79 24080014-11 2013 Collectively, these data suggest that Serine-204 phosphorylation in the Smad3LR is a critical event by which ERK enhances Smad3-mediated COL1A2 promoter activity in mesenchymal cells. Serine 38-44 SMAD family member 3 Homo sapiens 72-77 24080014-11 2013 Collectively, these data suggest that Serine-204 phosphorylation in the Smad3LR is a critical event by which ERK enhances Smad3-mediated COL1A2 promoter activity in mesenchymal cells. Serine 38-44 SMAD family member 3 Homo sapiens 122-127 25205100-2 2014 In response to TGFbeta, the TGFbeta receptor phosphorylates serine residues at the Smad3 C-tail. Serine 60-66 SMAD family member 3 Homo sapiens 83-88 23139211-10 2013 The latter altered interface residues or disrupted the phosphorylation-regulated Ser-Ser-X-Ser motifs within SMAD2 and SMAD3. Serine 85-88 SMAD family member 3 Homo sapiens 119-124 23139211-10 2013 The latter altered interface residues or disrupted the phosphorylation-regulated Ser-Ser-X-Ser motifs within SMAD2 and SMAD3. Serine 85-88 SMAD family member 3 Homo sapiens 119-124 22819829-4 2012 This differential effect of tyrosine and serine phosphorylation mutants of Cav-2 correlated with TGF-beta-induced Smad3 phosphorylation and transcriptional activation of plasminogen activator inhibitor-1. Serine 41-47 SMAD family member 3 Homo sapiens 114-119 23077590-5 2012 We present evidence that riluzole increases Smad2 and Smad3 linker phosphorylation at the cluster of serines 245/250/255 and serine 204 respectively. Serine 101-107 SMAD family member 3 Homo sapiens 54-59 23077590-5 2012 We present evidence that riluzole increases Smad2 and Smad3 linker phosphorylation at the cluster of serines 245/250/255 and serine 204 respectively. Serine 101-108 SMAD family member 3 Homo sapiens 54-59 15247277-5 2004 Here we show that sphingosine 1-phosphate, independently of transforming growth factor beta secretion, induces a rapid phosphorylation of Smad3 on its C-terminal serine motif and induces its partnering with Smad4 and the translocation of the complex into the nucleus. Serine 162-168 SMAD family member 3 Homo sapiens 138-143 21665986-7 2011 Older men contained less active (Ser-425 phosphorylated) SMAD3 (p-SMAD3) protein than younger men at T3 and T4 (p < .05).Although it is well known that younger individuals possess a greater hypertrophic potential to resistance exercise, it appears that older individuals may paradoxically possess a more favorable resistance exercise response regarding myostatin pathway-related genes and a protein marker of pathway activity. Serine 33-36 SMAD family member 3 Homo sapiens 57-62 21665986-7 2011 Older men contained less active (Ser-425 phosphorylated) SMAD3 (p-SMAD3) protein than younger men at T3 and T4 (p < .05).Although it is well known that younger individuals possess a greater hypertrophic potential to resistance exercise, it appears that older individuals may paradoxically possess a more favorable resistance exercise response regarding myostatin pathway-related genes and a protein marker of pathway activity. Serine 33-36 SMAD family member 3 Homo sapiens 64-71 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. Serine 93-96 SMAD family member 3 Homo sapiens 72-77 16528675-2 2006 TGF-beta signaling involves phosphorylation of Smad3 at serine residues 208 and 213 in the linker region and serine residues 423 and 425 in the C-terminal region. Serine 56-62 SMAD family member 3 Homo sapiens 47-52 19458083-0 2009 A negative feedback control of transforming growth factor-beta signaling by glycogen synthase kinase 3-mediated Smad3 linker phosphorylation at Ser-204. Serine 144-147 SMAD family member 3 Homo sapiens 112-117 19458083-4 2009 Here, we show that TGF-beta induces phosphorylation at three sites in the Smad3 linker region in addition to the two C-terminal residues, and glycogen synthase kinase 3 is responsible for phosphorylation at one of these sites, namely Ser-204. Serine 234-237 SMAD family member 3 Homo sapiens 74-79 19458083-5 2009 Alanine substitution at Ser-204 and/or the neighboring Ser-208, the priming site for glycogen synthase kinase 3 in vivo activity, strengthened the affinity of Smad3 to CREB-binding protein, suggesting that linker phosphorylation may be part of a negative feedback loop that modulates Smad3 transcriptional activity. Serine 24-27 SMAD family member 3 Homo sapiens 159-164 18032924-4 2007 Suppression of PLD activity or PLD expression resulted in increased phosphorylation of Smad2 and Smad3 on Ser 465/467-sites on Smads that get phosphorylated by the TGF-beta receptor and positively regulate TGF-beta signaling. Serine 106-109 SMAD family member 3 Homo sapiens 97-102 16156666-2 2005 We have mapped the ERK phosphorylation sites to Ser 207, Ser 203, and Thr 178 in Smad3. Serine 48-51 SMAD family member 3 Homo sapiens 81-86 16156666-2 2005 We have mapped the ERK phosphorylation sites to Ser 207, Ser 203, and Thr 178 in Smad3. Serine 57-60 SMAD family member 3 Homo sapiens 81-86 16156666-4 2005 Ser 207 is the best ERK site in Smad3. Serine 0-3 SMAD family member 3 Homo sapiens 32-37 14610066-11 2004 Activity of SBE-LUC, a Smad3/4-responsive construct, is stimulated by over-expression of Smad3 or Smad3D, in which the three C-terminal serine phospho-acceptor residues are mutated. Serine 136-142 SMAD family member 3 Homo sapiens 23-28 15210694-2 2004 TGFbeta binds to and activates serine/threonine kinase receptors that phosphorylate Smad2 and Smad3 intracellular signal transducers at two C-terminal serine residues. Serine 31-37 SMAD family member 3 Homo sapiens 94-99 14610066-11 2004 Activity of SBE-LUC, a Smad3/4-responsive construct, is stimulated by over-expression of Smad3 or Smad3D, in which the three C-terminal serine phospho-acceptor residues are mutated. Serine 136-142 SMAD family member 3 Homo sapiens 89-94 14610066-13 2004 However, TGF-beta1-induced total serine phosphorylation of Smad3 is decreased by LY294002, suggesting that Smad3 is phosphorylated by the PI3K pathway at serine residues other than the direct TGF-beta receptor I target site. Serine 33-39 SMAD family member 3 Homo sapiens 59-64 14610066-13 2004 However, TGF-beta1-induced total serine phosphorylation of Smad3 is decreased by LY294002, suggesting that Smad3 is phosphorylated by the PI3K pathway at serine residues other than the direct TGF-beta receptor I target site. Serine 33-39 SMAD family member 3 Homo sapiens 107-112 14610066-13 2004 However, TGF-beta1-induced total serine phosphorylation of Smad3 is decreased by LY294002, suggesting that Smad3 is phosphorylated by the PI3K pathway at serine residues other than the direct TGF-beta receptor I target site. Serine 154-160 SMAD family member 3 Homo sapiens 59-64 14610066-13 2004 However, TGF-beta1-induced total serine phosphorylation of Smad3 is decreased by LY294002, suggesting that Smad3 is phosphorylated by the PI3K pathway at serine residues other than the direct TGF-beta receptor I target site. Serine 154-160 SMAD family member 3 Homo sapiens 107-112 10504488-12 1999 A dominant negative mutant form of Smad3 lacking the C-terminal serine phosphoacceptor sites (Smad3A) inhibited TGF-beta1-induced luciferase activity. Serine 64-70 SMAD family member 3 Homo sapiens 35-40 12759229-9 2003 Overexpression of Smad3 or Smad3D, in which the three COOH-terminal serine phosphoacceptor residues have been mutated, increased activity of the SBE-LUC construct, containing four DNA binding sites for Smad3 and Smad4. Serine 68-74 SMAD family member 3 Homo sapiens 18-23 12759229-9 2003 Overexpression of Smad3 or Smad3D, in which the three COOH-terminal serine phosphoacceptor residues have been mutated, increased activity of the SBE-LUC construct, containing four DNA binding sites for Smad3 and Smad4. Serine 68-74 SMAD family member 3 Homo sapiens 27-32 12700666-4 2003 TGF-beta signaling involves TGF-beta type I receptor-mediated phosphorylation of serine residues within the conserved SSXS motif at the C-terminus of Smad2 and Smad3. Serine 81-87 SMAD family member 3 Homo sapiens 160-165 33676893-5 2021 Specifically, we discovered that NLK associates with Smad3 and phosphorylates the designated serine residues located in the linker region of Smad2 and Smad3, which inhibits phosphorylation at the C-terminus, thereby decreasing the duration of TGF-beta signaling. Serine 93-99 SMAD family member 3 Homo sapiens 53-58 9380693-5 1997 Either attachment of an epitope tag to the C terminus or replacement of these three serine residues with alanine abolishes TGF-beta-induced Smad3 phosphorylation; these proteins act in a dominant-negative fashion to block the antiproliferative effect of TGF-beta in mink lung epithelial cells. Serine 84-90 SMAD family member 3 Homo sapiens 140-145 34003249-11 2021 TGF-beta1 increased cellular phosphoSSXS-Smad3 serines 423 and 425, with and without high D-glucose. Serine 47-54 SMAD family member 3 Homo sapiens 41-46 34003249-13 2021 Smad3 serine 204 phosphorylation was significantly raised by a combination of high D-glucose+TGF-beta1; this was significantly reduced by SGLT2 and MEK inhibition. Serine 6-12 SMAD family member 3 Homo sapiens 0-5 9380693-6 1997 A Smad3 protein in which the three C-terminal serines have been replaced by aspartic acids is also a dominant inhibitor of TGF-beta signaling, but can activate plasminogen activator inhibitor 1 (PAI-1) transcription in a ligand-independent fashion when its nuclear localization is forced by transient overexpression. Serine 46-53 SMAD family member 3 Homo sapiens 2-7 9380693-7 1997 Phosphorylation of the three C-terminal serine residues of Smad3 by an activated TGF-beta receptor complex is an essential step in signal transduction by TGF-beta for both inhibition of cell proliferation and activation of the PAI-1 promoter. Serine 40-46 SMAD family member 3 Homo sapiens 59-64 33676893-5 2021 Specifically, we discovered that NLK associates with Smad3 and phosphorylates the designated serine residues located in the linker region of Smad2 and Smad3, which inhibits phosphorylation at the C-terminus, thereby decreasing the duration of TGF-beta signaling. Serine 93-99 SMAD family member 3 Homo sapiens 151-156 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). Serine 33-39 SMAD family member 3 Homo sapiens 4-9 32733385-5 2020 These ligands signal through serine/threonine receptor complexes to activate downstream signaling mediators, Smad2 and Smad3. Serine 29-35 SMAD family member 3 Homo sapiens 119-124 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. Serine 112-118 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. Serine 112-118 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. Serine 112-118 SMAD family member 3 Homo sapiens 99-104 28032440-10 2017 Furthermore, the phosphorylation of Smad3 in its linker area (Thr179, Ser 204/208/213) was inhibited by magnolol. Serine 70-73 SMAD family member 3 Homo sapiens 36-41 26919443-6 2016 Observations revealed that E2F5 overexpression was accompanied by significantly higher phosphorylation of SMAD3 at Ser-208 in the linker region (pSMAD3L) and p38 in tumor tissue. Serine 115-118 SMAD family member 3 Homo sapiens 106-111 26919443-7 2016 A striking difference in SMAD3 phosphorylation, marked by preponderance of pSMAD3L and pSMAD3C (Ser-423 and 425) in tumor and benign tissues, respectively was noted. Serine 96-99 SMAD family member 3 Homo sapiens 25-30 26269751-11 2015 The phosphorylation of smad3 linker region at serine 204, 208 and 213 was enhanced in gastric cancer cells after TGF-beta treatment. Serine 46-52 SMAD family member 3 Homo sapiens 23-28