PubMed:1846781 JSONTXT

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":14,"end":30},"obj":"protein"},{"id":"T2","span":{"begin":60,"end":65},"obj":"protein"},{"id":"T3","span":{"begin":178,"end":183},"obj":"protein"},{"id":"T4","span":{"begin":287,"end":313},"obj":"protein"},{"id":"T5","span":{"begin":315,"end":320},"obj":"protein"},{"id":"T6","span":{"begin":433,"end":438},"obj":"protein"},{"id":"T7","span":{"begin":492,"end":508},"obj":"protein"},{"id":"T8","span":{"begin":562,"end":567},"obj":"protein"},{"id":"T9","span":{"begin":637,"end":641},"obj":"protein"},{"id":"T10","span":{"begin":697,"end":702},"obj":"protein"},{"id":"T11","span":{"begin":724,"end":729},"obj":"protein"},{"id":"T12","span":{"begin":913,"end":918},"obj":"protein"},{"id":"T13","span":{"begin":953,"end":958},"obj":"protein"},{"id":"T14","span":{"begin":1092,"end":1108},"obj":"protein"}],"text":"Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity.\nIn resting human epithelial and fibroblastic cells, c-Jun is phosphorylated on serine and threonine at five sites, three of which are phosphorylated in vitro by glycogen synthase kinase 3 (GSK-3). These three sites are nested within a single tryptic peptide located just upstream of the basic region of the c-Jun DNA-binding domain (residues 227-252). Activation of protein kinase C results in rapid, site-specific dephosphorylation of c-Jun at one or more of these three sites and is coincident with increased AP-1-binding activity. Phosphorylation of recombinant human c-Jun proteins in vitro by GSK-3 decreases their DNA-binding activity. Mutation of serine 243 to phenylalanine blocks phosphorylation of all three sites in vivo and increases the inherent trans-activation ability of c-Jun at least 10-fold. We propose that c-Jun is present in resting cells in a latent, phosphorylated form that can be activated by site-specific dephosphorylation in response to protein kinase C activation."}

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":14,"end":30},"obj":"protein"},{"id":"T2","span":{"begin":60,"end":65},"obj":"protein"},{"id":"T3","span":{"begin":178,"end":183},"obj":"protein"},{"id":"T4","span":{"begin":287,"end":313},"obj":"protein"},{"id":"T5","span":{"begin":315,"end":320},"obj":"protein"},{"id":"T6","span":{"begin":433,"end":438},"obj":"protein"},{"id":"T7","span":{"begin":492,"end":508},"obj":"protein"},{"id":"T8","span":{"begin":562,"end":567},"obj":"protein"},{"id":"T9","span":{"begin":637,"end":641},"obj":"protein"},{"id":"T10","span":{"begin":697,"end":702},"obj":"protein"},{"id":"T11","span":{"begin":724,"end":729},"obj":"protein"},{"id":"T12","span":{"begin":913,"end":918},"obj":"protein"},{"id":"T13","span":{"begin":953,"end":958},"obj":"protein"},{"id":"T14","span":{"begin":1092,"end":1108},"obj":"protein"}],"text":"Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity.\nIn resting human epithelial and fibroblastic cells, c-Jun is phosphorylated on serine and threonine at five sites, three of which are phosphorylated in vitro by glycogen synthase kinase 3 (GSK-3). These three sites are nested within a single tryptic peptide located just upstream of the basic region of the c-Jun DNA-binding domain (residues 227-252). Activation of protein kinase C results in rapid, site-specific dephosphorylation of c-Jun at one or more of these three sites and is coincident with increased AP-1-binding activity. Phosphorylation of recombinant human c-Jun proteins in vitro by GSK-3 decreases their DNA-binding activity. Mutation of serine 243 to phenylalanine blocks phosphorylation of all three sites in vivo and increases the inherent trans-activation ability of c-Jun at least 10-fold. We propose that c-Jun is present in resting cells in a latent, phosphorylated form that can be activated by site-specific dephosphorylation in response to protein kinase C activation."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":137,"end":142},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":691,"end":696},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"}],"text":"Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity.\nIn resting human epithelial and fibroblastic cells, c-Jun is phosphorylated on serine and threonine at five sites, three of which are phosphorylated in vitro by glycogen synthase kinase 3 (GSK-3). These three sites are nested within a single tryptic peptide located just upstream of the basic region of the c-Jun DNA-binding domain (residues 227-252). Activation of protein kinase C results in rapid, site-specific dephosphorylation of c-Jun at one or more of these three sites and is coincident with increased AP-1-binding activity. Phosphorylation of recombinant human c-Jun proteins in vitro by GSK-3 decreases their DNA-binding activity. Mutation of serine 243 to phenylalanine blocks phosphorylation of all three sites in vivo and increases the inherent trans-activation ability of c-Jun at least 10-fold. We propose that c-Jun is present in resting cells in a latent, phosphorylated form that can be activated by site-specific dephosphorylation in response to protein kinase C activation."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":158,"end":170},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000057"}],"text":"Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity.\nIn resting human epithelial and fibroblastic cells, c-Jun is phosphorylated on serine and threonine at five sites, three of which are phosphorylated in vitro by glycogen synthase kinase 3 (GSK-3). These three sites are nested within a single tryptic peptide located just upstream of the basic region of the c-Jun DNA-binding domain (residues 227-252). Activation of protein kinase C results in rapid, site-specific dephosphorylation of c-Jun at one or more of these three sites and is coincident with increased AP-1-binding activity. Phosphorylation of recombinant human c-Jun proteins in vitro by GSK-3 decreases their DNA-binding activity. Mutation of serine 243 to phenylalanine blocks phosphorylation of all three sites in vivo and increases the inherent trans-activation ability of c-Jun at least 10-fold. We propose that c-Jun is present in resting cells in a latent, phosphorylated form that can be activated by site-specific dephosphorylation in response to protein kinase C activation."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":158,"end":170},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000057"}],"text":"Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity.\nIn resting human epithelial and fibroblastic cells, c-Jun is phosphorylated on serine and threonine at five sites, three of which are phosphorylated in vitro by glycogen synthase kinase 3 (GSK-3). These three sites are nested within a single tryptic peptide located just upstream of the basic region of the c-Jun DNA-binding domain (residues 227-252). Activation of protein kinase C results in rapid, site-specific dephosphorylation of c-Jun at one or more of these three sites and is coincident with increased AP-1-binding activity. Phosphorylation of recombinant human c-Jun proteins in vitro by GSK-3 decreases their DNA-binding activity. Mutation of serine 243 to phenylalanine blocks phosphorylation of all three sites in vivo and increases the inherent trans-activation ability of c-Jun at least 10-fold. We propose that c-Jun is present in resting cells in a latent, phosphorylated form that can be activated by site-specific dephosphorylation in response to protein kinase C activation."}