PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33447346-3 2020 Phosphorylation of the proline-rich region, by kinases such as Erk2, has been suggested as an upstream activator. Proline 23-30 mitogen-activated protein kinase 1 Homo sapiens 63-67 31296381-5 2019 Structural and sequence comparison showed that hGas7-SH3 shares high similarity with Abl SH3 domain, which binds to a high-affinity proline-rich peptide P41 in a canonical SH3-ligand binding mode through two hydrophobic pockets and a specificity site in the RT-loop. Proline 132-139 mitogen-activated protein kinase 1 Homo sapiens 153-156 30282717-7 2019 In consistence, in vivo during infection, one proline-rich motif was enough for 11-kDa to significantly reduce phosphorylation of extracellular signal-regulated kinase (ERK). Proline 46-53 mitogen-activated protein kinase 1 Homo sapiens 130-167 30282717-7 2019 In consistence, in vivo during infection, one proline-rich motif was enough for 11-kDa to significantly reduce phosphorylation of extracellular signal-regulated kinase (ERK). Proline 46-53 mitogen-activated protein kinase 1 Homo sapiens 169-172 30282717-8 2019 Mutations of all three proline-rich motifs of 11-kDa abolished its capability to reduce ERK activity and, accordingly, decreased viral DNA replication. Proline 23-30 mitogen-activated protein kinase 1 Homo sapiens 88-91 20974802-4 2011 On the basis of a kinome-wide small interfering RNA (siRNA) screen and confirmative biochemical analysis, we show that several proline-directed mitogen-activated protein kinases (MAPKs), such as p38, ERK1/2, and JNK1 are sufficient and required for the phosphorylation of PPPS/TP motifs of LRP6. Proline 127-134 mitogen-activated protein kinase 1 Homo sapiens 195-198 26868487-6 2016 Immunoprecipitation with anti-ZEB1 antibodies followed by western analysis with a phospho-Threonine-Proline-specific antibody indicates that the ERK consensus site at Thr-867 is phosphorylated in ZEB1. Proline 100-107 mitogen-activated protein kinase 1 Homo sapiens 145-148 24509437-5 2014 Furthermore, a mass spectrometry-based in vitro kinase assay demonstrated that ERK2 specifically phosphorylated the Ser(16) residue in the Ser(16)-Pro(17) motif-containing substrate. Proline 147-150 mitogen-activated protein kinase 1 Homo sapiens 79-83 24049075-4 2013 Here we report that MED14, a core subunit of the Mediator, is a bona fide ERK substrate and identify serine 986 (S986) within a serine-proline rich region of MED14 as the major ERK phosphorylation site. Proline 135-142 mitogen-activated protein kinase 1 Homo sapiens 177-180 21762808-0 2011 Mechanism of host cell MAPK/ERK-2 incorporation into lentivirus particles: characterization of the interaction between MAPK/ERK-2 and proline-rich-domain containing capsid region of structural protein Gag. Proline 134-141 mitogen-activated protein kinase 1 Homo sapiens 124-129 21762808-8 2011 Utilizing virus-like particles directed by Gag, we have shown that the exchange of conserved proline residues within capsid of Gag(p55) resulted in impaired incorporation of MAPK/ERK-2. Proline 93-100 mitogen-activated protein kinase 1 Homo sapiens 179-184 16848763-3 2006 Further experiments showed that DAZAP1 was phosphorylated stoichiometrically in vitro by ERK2 (extracellular-signal-regulated protein kinase 2) at two Thr-Pro sequences (Thr269 and Thr315), and that both sites became phosphorylated in HEK-293 (human embryonic kidney 293) cells in response to PMA or EGF (epidermal growth factor), or RAW 264.7 macrophages in response to LPS. Proline 155-158 mitogen-activated protein kinase 1 Homo sapiens 95-142 17597065-4 2007 We found that substitution of residues 173-175 and particularly Pro(174) to alanines reduces the EGF-induced ERK2 phosphorylation, without modifying its in vitro phosphorylation by MEK1. Proline 64-67 mitogen-activated protein kinase 1 Homo sapiens 109-113 19361221-5 2009 Here we have modeled the interaction of ERK with a target peptide and analyzed the specificity toward Ser/Thr-Pro motifs. Proline 110-113 mitogen-activated protein kinase 1 Homo sapiens 40-43 19361221-7 2009 Our results suggest that (1) the proline residue has a role in both specificity and phospho transfer efficiency, (2) the reaction occurs in one step, with ERK2 Asp(147) acting as the catalytic base, (3) a conserved Lys in the kinase superfamily that is usually mutated to check kinase activity strongly stabilizes the transition state, and (4) the reaction mechanism is similar with either one or two Mg(2+) ions in the active site. Proline 33-40 mitogen-activated protein kinase 1 Homo sapiens 155-159 17928366-5 2008 MEK1-mediated ERK2 nuclear translocation and proliferation were shown to depend on phosphorylation of S298 and T292 sites in the MEK1 proline-rich domain. Proline 134-141 mitogen-activated protein kinase 1 Homo sapiens 14-18 16024771-10 2005 A putative DEF (docking for ERK FXFP) domain located in the proline-rich region of CdGAP is required for efficient binding and phosphorylation by ERK1/2. Proline 60-67 mitogen-activated protein kinase 1 Homo sapiens 28-31 16456541-4 2006 IEX-1 binds to B56 subunits and pERK independently, enhances B56 phosphorylation by ERK at a conserved Ser/Pro site in this complex and triggers dissociation from the catalytic subunit. Proline 107-110 mitogen-activated protein kinase 1 Homo sapiens 33-36 15664191-4 2005 Five of the identified sites are proline-directed targets of activated ERK, and phosphorylation of all six sites requires MEK signaling, indicating a negative feedback mechanism. Proline 33-40 mitogen-activated protein kinase 1 Homo sapiens 71-74 15826939-3 2005 When compared with Pro(33)-negative platelets, Pro(33)-positive platelets demonstrated significantly greater serine/threonine phosphorylation of extracellular signal-regulated kinase (ERK2) and myosin light chain (MLC) but not cytoplasmic phospholipase A2 upon thrombin-induced aggregation. Proline 47-50 mitogen-activated protein kinase 1 Homo sapiens 184-188 15023352-3 2004 ERK2 catalyses the transfer of the gamma-phosphate of adenosine triphosphate to serine or threonine residues found in Ser-Pro or Thr-Pro motifs on proteins. Proline 122-125 mitogen-activated protein kinase 1 Homo sapiens 0-4 15023352-3 2004 ERK2 catalyses the transfer of the gamma-phosphate of adenosine triphosphate to serine or threonine residues found in Ser-Pro or Thr-Pro motifs on proteins. Proline 133-136 mitogen-activated protein kinase 1 Homo sapiens 0-4 14757063-3 2004 We present here a complete thermodynamic analysis of the binding energetics of the p41 proline-rich decapeptide (APSYSPPPPP) to the SH3 domain of the c-Abl oncogene. Proline 87-94 mitogen-activated protein kinase 1 Homo sapiens 83-86 14993270-3 2004 It was previously shown that Rac-p21-activated kinase (PAK) signaling regulated the physical association of MEK1 with ERK2 through phosphorylation sites in the proline-rich sequence (PRS) of MEK1. Proline 160-167 mitogen-activated protein kinase 1 Homo sapiens 118-122 14757063-6 2004 The origin of the binding energetics for proline-rich ligands to the Abl-SH3 domain is further investigated by a comparative calorimetric analysis of a set of p41-related ligands. Proline 41-48 mitogen-activated protein kinase 1 Homo sapiens 159-162 11604401-2 2001 The MKK C-terminal region contains a proline-rich region that reportedly functions in regulating interactions with the Raf-1 kinase and ERK activity. Proline 37-44 mitogen-activated protein kinase 1 Homo sapiens 136-139 11818515-7 2002 The phospho-Ser/Thr-Pro content (characteristic of ERK1/2 substrates) of Triton-insoluble proteins (75 and 80 kDa) increased during capacitation and also appeared to be regulated by O(2)(-)* and the ERK pathway. Proline 20-23 mitogen-activated protein kinase 1 Homo sapiens 51-54 12966092-11 2003 Interestingly, PPARalpha and gamma agonists caused rapid activation of proline-rich tyrosine kinase or Pyk2; Pyk2 as well as p38 phosphorylation was reduced by intracellular Ca2+ chelation without an observable effect on EGFR and Erk activation, suggesting a possible role for Pyk2 as an upstream activator of p38. Proline 71-78 mitogen-activated protein kinase 1 Homo sapiens 230-233 12966092-11 2003 Interestingly, PPARalpha and gamma agonists caused rapid activation of proline-rich tyrosine kinase or Pyk2; Pyk2 as well as p38 phosphorylation was reduced by intracellular Ca2+ chelation without an observable effect on EGFR and Erk activation, suggesting a possible role for Pyk2 as an upstream activator of p38. Proline 71-78 mitogen-activated protein kinase 1 Homo sapiens 310-313 9677429-0 1998 The MEK1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases ERK1 and ERK2 in mammalian cells. Proline 9-16 mitogen-activated protein kinase 1 Homo sapiens 116-120 10737616-8 2000 The MAP kinases may not be strictly proline specific: p38 phosphorylated the nonproline sites Ser185, Thr245, Ser305, and Ser356, whereas ERK2 was the most strict. Proline 36-43 mitogen-activated protein kinase 1 Homo sapiens 54-57 10922375-7 2000 It is apparent that mechanisms controlling events downstream of the proline-directed MAPKs involve specific MAPK docking sites within the carboxyl termini of the MAPKAPKs that determine the cascade in which the MAPKAPK functions. Proline 68-75 mitogen-activated protein kinase 1 Homo sapiens 85-89 10922466-3 2000 The proline-directed p42 mitogen-activated protein kinase (ERK2) was used to phosphorylate the serine side chain in Pro-Arg-Ser-Pro-Phe-4-nitroanilide under conditions where different amounts of cis prolyl isomer of the substrate were present. Proline 4-11 mitogen-activated protein kinase 1 Homo sapiens 59-63 9202310-3 1997 A number of protein kinases can phosphorylate tau in vitro; those that require or accept prolines include GSK3 and members of the mitogen-activated protein (MAP) kinase family, ERK1, ERK2, and SAP kinase-beta/JNK. Proline 89-97 mitogen-activated protein kinase 1 Homo sapiens 183-187 9006942-7 1997 Activation of the proline-directed kinases Erk1/2, JNKs, and p38 was neither necessary nor sufficient for stress-induced PTP-1B phosphorylation. Proline 18-25 mitogen-activated protein kinase 1 Homo sapiens 61-64 1939237-12 1991 We propose that the primary sequence of substrates for ERK1 and ERK2 protein kinases can be generalized as -Pro-Xaan-Ser/Thr-Pro- (where Xaa is a neutral or basic amino acid and n = 1 or 2). Proline 108-111 mitogen-activated protein kinase 1 Homo sapiens 64-68 8668214-4 1996 The results showed that AML1 is phosphorylated in vivo on two serine residues within the proline-, serine-, and threonine-rich region, with dependence on the activation of extracellular signal-regulated kinase (ERK) and with interleukin-3 stimulation in a hematopoietic cell line. Proline 89-96 mitogen-activated protein kinase 1 Homo sapiens 211-214 7709430-2 1995 Until recently, ERK1 and ERK2 were the only cloned and well-characterized mammalian MAPKs; diverse ligand-stimulated, proline-directed protein phosphorylation events were attributed to these kinases. Proline 118-125 mitogen-activated protein kinase 1 Homo sapiens 25-29