PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22922962-1 2012 OBJECTIVE: To investigate the role of Pyk2, a proline-rich nonreceptor tyrosine kinase, in G protein-coupled receptor agonist, thrombin-induced human aortic smooth muscle cell growth and migration, and injury-induced vascular wall remodeling. Proline 46-53 protein tyrosine kinase 2 beta Homo sapiens 38-42 27605668-10 2016 The signaling does not require a functional SH2 domain or the tyrosine residues commonly phosphorylated in Shc1 but is mediated by the interaction between a short segment of the central domain of Shc1 and the proline-rich region of Pyk2. Proline 209-216 protein tyrosine kinase 2 beta Homo sapiens 232-236 11461120-6 2001 In addition stimulation with MIP-1alpha induces tyrosine phosphorylation of the proline-rich tyrosine kinase Pyk-2. Proline 80-87 protein tyrosine kinase 2 beta Homo sapiens 109-114 17906699-3 2008 We report here that proline-rich tyrosine kinase Pyk2 is highly expressed in SCLC cells and provides a functional link between neuropeptide-induced increases in [Ca2+](i) and tumor cell proliferation. Proline 20-27 protein tyrosine kinase 2 beta Homo sapiens 49-53 12576483-6 2003 The proline-rich regions in the C-terminal half of Pyk2 bind to the SH3 domain of PSD-95 and SAP102. Proline 4-11 protein tyrosine kinase 2 beta Homo sapiens 51-55 17283076-6 2007 Pulldown analysis with glutathione S-transferase-fused proline-rich regions of PTP-PEST revealed coprecipitation of WASP, PYK2, c-Src, and PSTPIP proteins with the N-terminal region (amino acids 294-497) of PTP-PEST. Proline 55-62 protein tyrosine kinase 2 beta Homo sapiens 122-126 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 protein tyrosine kinase 2 beta Homo sapiens 109-113 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 protein tyrosine kinase 2 beta Homo sapiens 109-113 12893833-4 2003 PRAP contains a coiled-coil domain, a pleckstrin homology domain, and a SH3 domain; the SH3 domain binds to the proline-rich domain of Pyk2/RAFTK. Proline 112-119 protein tyrosine kinase 2 beta Homo sapiens 135-139 12893833-4 2003 PRAP contains a coiled-coil domain, a pleckstrin homology domain, and a SH3 domain; the SH3 domain binds to the proline-rich domain of Pyk2/RAFTK. Proline 112-119 protein tyrosine kinase 2 beta Homo sapiens 140-145 12771146-4 2003 Pyk2-ASAP1 interaction was confirmed in pull-down as well as in co-immunoprecipitation experiments, and contact sites were mapped to the proline-rich regions of Pyk2 and the SH3 domain of ASAP1. Proline 137-144 protein tyrosine kinase 2 beta Homo sapiens 0-4 12771146-4 2003 Pyk2-ASAP1 interaction was confirmed in pull-down as well as in co-immunoprecipitation experiments, and contact sites were mapped to the proline-rich regions of Pyk2 and the SH3 domain of ASAP1. Proline 137-144 protein tyrosine kinase 2 beta Homo sapiens 161-165 12730223-0 2003 Fibronectin fragment activation of proline-rich tyrosine kinase PYK2 mediates integrin signals regulating collagenase-3 expression by human chondrocytes through a protein kinase C-dependent pathway. Proline 35-42 protein tyrosine kinase 2 beta Homo sapiens 64-68 12529254-5 2003 Other results suggest that rP2X(7)-R-mediated ERK1/2 phosphorylation was linked to the phosphorylation of the proline-rich/Ca(2+)-activated tyrosine kinase Pyk2, c-Src, phosphatidylinositol 3"-kinase, and protein kinase Cdelta activities and was dependent on the presence of extracellular Ca(2+). Proline 110-117 protein tyrosine kinase 2 beta Homo sapiens 156-160 11262415-0 2001 Down-regulation by antisense oligonucleotides establishes a role for the proline-rich tyrosine kinase PYK2 in angiotensin ii-induced signaling in vascular smooth muscle. Proline 73-80 protein tyrosine kinase 2 beta Homo sapiens 102-106 11238453-4 2001 PYK2 interacts with PSGAP Src homology 3 domain via the carboxyl-terminal proline-rich sequence. Proline 74-81 protein tyrosine kinase 2 beta Homo sapiens 0-4 10749687-12 2000 With the use of glutathione S-transferase fusion proteins containing Shc-SH2, Grb2-SH2, and Grb2 N-terminal and C-terminal SH3 domains, it was implied that the proline-rich region of Pyk2 (and FAK) binds to the N-terminal SH3 domain of Grb2 and that the phosphotyrosine residue of Shc binds to the SH2 domain of Grb2. Proline 160-167 protein tyrosine kinase 2 beta Homo sapiens 183-187 9545257-3 1998 The monocyte CADTK was 5 kDa smaller than protein from epithelial cells; isolation and sequencing of the monocyte CADTK cDNA revealed a predicted 42-amino acid deletion between the two proline-rich domains of the enzyme. Proline 185-192 protein tyrosine kinase 2 beta Homo sapiens 13-18 10601992-1 1999 The proline-, glutamic acid-, serine- and threonine-enriched protein tyrosine phosphatase PEP, which is expressed primarily in hematopoietic cells, was recently discovered to be physically associated with the 50-kDa cytosolic protein tyrosine kinase (PTK) Csk, an important suppressor of Src family PTK, including Lck and Fyn in T cells. Proline 4-11 protein tyrosine kinase 2 beta Homo sapiens 251-254 10601992-1 1999 The proline-, glutamic acid-, serine- and threonine-enriched protein tyrosine phosphatase PEP, which is expressed primarily in hematopoietic cells, was recently discovered to be physically associated with the 50-kDa cytosolic protein tyrosine kinase (PTK) Csk, an important suppressor of Src family PTK, including Lck and Fyn in T cells. Proline 4-11 protein tyrosine kinase 2 beta Homo sapiens 299-302 9545257-3 1998 The monocyte CADTK was 5 kDa smaller than protein from epithelial cells; isolation and sequencing of the monocyte CADTK cDNA revealed a predicted 42-amino acid deletion between the two proline-rich domains of the enzyme. Proline 185-192 protein tyrosine kinase 2 beta Homo sapiens 114-119 9568986-2 1998 Replacement of proline by alanine (ATK) in the PTK motif abolished transmission almost completely both from plants and from membranes. Proline 15-22 protein tyrosine kinase 2 beta Homo sapiens 47-50 9099734-7 1997 Using in vitro binding assays, RAFTK and paxillin were shown to bind directly through the C-terminal proline-rich domain. Proline 101-108 protein tyrosine kinase 2 beta Homo sapiens 31-36 9310476-8 1997 RAFTK coimmunoprecipitated with the cytoskeletal protein paxillin through its C-terminal proline-rich domain in TrHBMEC. Proline 89-96 protein tyrosine kinase 2 beta Homo sapiens 0-5 7499242-6 1995 In addition, like pp125FAK, RAFTK contains a kinase domain flanked by large N-terminal (426 residues) and C-terminal (331 residues) domains, and the C-terminal region contains a predicted proline-rich stretch of residues. Proline 188-195 protein tyrosine kinase 2 beta Homo sapiens 28-33 9091579-6 1997 RAFTK also co-immunoprecipitates with the SH2 domain of Lck and with the cytoskeletal protein paxillin through its COOH-terminal proline-rich domain. Proline 129-136 protein tyrosine kinase 2 beta Homo sapiens 0-5 8995252-3 1997 The structure of RAFTK is similar to p125FAK in that it lacks a transmembrane region, does not contain Src homology 2 or 3 domains, and has a proline-rich region in its C terminus. Proline 142-149 protein tyrosine kinase 2 beta Homo sapiens 17-22