PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7925472-3 1994 Two distinct proline-directed kinase families phosphorylate Ser25 and Ser38 of Op18 with overlapping but distinct site preference. Proline 13-20 stathmin 1 Homo sapiens 79-83 8325880-4 1993 In conjunction with in vitro phosphorylation experiments, using purified wild-type and mutant Op18 proteins in combination with a series of kinases, these results have identified two distinct proline-directed kinase families that phosphorylate Op18 with overlapping but distinct site preference. Proline 192-199 stathmin 1 Homo sapiens 94-98 8325880-4 1993 In conjunction with in vitro phosphorylation experiments, using purified wild-type and mutant Op18 proteins in combination with a series of kinases, these results have identified two distinct proline-directed kinase families that phosphorylate Op18 with overlapping but distinct site preference. Proline 192-199 stathmin 1 Homo sapiens 244-248 24589734-3 2014 Previously, we characterized mechanisms underlying JNK phosphorylation of STMN at proline-flanked serine residues (Ser25 and Ser38) that are conserved across STMN-like proteins. Proline 82-89 stathmin 1 Homo sapiens 74-78 24589734-3 2014 Previously, we characterized mechanisms underlying JNK phosphorylation of STMN at proline-flanked serine residues (Ser25 and Ser38) that are conserved across STMN-like proteins. Proline 82-89 stathmin 1 Homo sapiens 158-162 22577147-4 2012 Although the two proteins have been proposed to display the four conserved phosphorylation sites originally identified in stathmin 1, we show here that they possess distinct phosphorylation sites within their specific proline-rich domains (PRDs) that are differentially regulated by phosphorylation by proline-directed kinases involved in the control of neuronal differentiation. Proline 218-225 stathmin 1 Homo sapiens 122-132 22577147-4 2012 Although the two proteins have been proposed to display the four conserved phosphorylation sites originally identified in stathmin 1, we show here that they possess distinct phosphorylation sites within their specific proline-rich domains (PRDs) that are differentially regulated by phosphorylation by proline-directed kinases involved in the control of neuronal differentiation. Proline 302-309 stathmin 1 Homo sapiens 122-132