PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17934522-2 2008 Csk-homologous kinase (CHK) can inhibit the kinase activity of certain Src kinase family members in vitro by phosphorylating the C-terminal tyrosine and by a non-catalytic mechanism. Tyrosine 140-148 megakaryocyte-associated tyrosine kinase Homo sapiens 0-21 21799000-10 2011 Analysis of specific tyrosines showed that mutation of tyrosines 428/452 in SHPS-1 to phenylalanine reduced SHPS-1 phosphorylation but allowed CTK binding. Tyrosine 55-64 megakaryocyte-associated tyrosine kinase Homo sapiens 143-146 21799000-11 2011 In contrast, the mutation of tyrosines 469/495 inhibited IGF-IR-mediated the phosphorylation of SHPS-1 and CTK binding, suggesting that IGF-IR phosphorylated Y469/495, allowing CTK binding, and that CTK subsequently phosphorylated Y428/452. Tyrosine 29-38 megakaryocyte-associated tyrosine kinase Homo sapiens 107-110 21799000-11 2011 In contrast, the mutation of tyrosines 469/495 inhibited IGF-IR-mediated the phosphorylation of SHPS-1 and CTK binding, suggesting that IGF-IR phosphorylated Y469/495, allowing CTK binding, and that CTK subsequently phosphorylated Y428/452. Tyrosine 29-38 megakaryocyte-associated tyrosine kinase Homo sapiens 177-180 21799000-11 2011 In contrast, the mutation of tyrosines 469/495 inhibited IGF-IR-mediated the phosphorylation of SHPS-1 and CTK binding, suggesting that IGF-IR phosphorylated Y469/495, allowing CTK binding, and that CTK subsequently phosphorylated Y428/452. Tyrosine 29-38 megakaryocyte-associated tyrosine kinase Homo sapiens 177-180 18783823-9 2008 Moreover, the kinase activity of SFK is negatively regulated by the phosphorylation of their carboxy (C)-terminal regulatory tyrosines by specific proteins called carboxyl-terminal Src kinase (Csk) and Csk homologous kinase (CHK). Tyrosine 125-134 megakaryocyte-associated tyrosine kinase Homo sapiens 202-223 18783823-9 2008 Moreover, the kinase activity of SFK is negatively regulated by the phosphorylation of their carboxy (C)-terminal regulatory tyrosines by specific proteins called carboxyl-terminal Src kinase (Csk) and Csk homologous kinase (CHK). Tyrosine 125-134 megakaryocyte-associated tyrosine kinase Homo sapiens 225-228 17934522-2 2008 Csk-homologous kinase (CHK) can inhibit the kinase activity of certain Src kinase family members in vitro by phosphorylating the C-terminal tyrosine and by a non-catalytic mechanism. Tyrosine 140-148 megakaryocyte-associated tyrosine kinase Homo sapiens 23-26 16959780-2 2006 To prevent constitutive SFK activation, the catalytic activity of SFKs in normal mammalian cells is suppressed mainly by two inhibitors called C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK), which inactivate SFKs by phosphorylating a consensus tyrosine near the C terminus of SFKs (Y(T)). Tyrosine 257-265 megakaryocyte-associated tyrosine kinase Homo sapiens 175-196 16959780-2 2006 To prevent constitutive SFK activation, the catalytic activity of SFKs in normal mammalian cells is suppressed mainly by two inhibitors called C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK), which inactivate SFKs by phosphorylating a consensus tyrosine near the C terminus of SFKs (Y(T)). Tyrosine 257-265 megakaryocyte-associated tyrosine kinase Homo sapiens 198-201 16707123-0 2006 Involvement of the N-terminal unique domain of Chk tyrosine kinase in Chk-induced tyrosine phosphorylation in the nucleus. Tyrosine 51-59 megakaryocyte-associated tyrosine kinase Homo sapiens 47-50 16707123-0 2006 Involvement of the N-terminal unique domain of Chk tyrosine kinase in Chk-induced tyrosine phosphorylation in the nucleus. Tyrosine 51-59 megakaryocyte-associated tyrosine kinase Homo sapiens 70-73 16707123-3 2006 In this study, we explored the role of the N-terminal unique domain of Chk in nuclear localization and Chk-induced tyrosine phosphorylation in the nucleus. Tyrosine 115-123 megakaryocyte-associated tyrosine kinase Homo sapiens 103-106 16707123-5 2006 The presence of the N-terminal domain of Chk led to a fourfold increase in cell population exhibiting Chk-induced tyrosine phosphorylation in the nucleus. Tyrosine 114-122 megakaryocyte-associated tyrosine kinase Homo sapiens 41-44 16707123-5 2006 The presence of the N-terminal domain of Chk led to a fourfold increase in cell population exhibiting Chk-induced tyrosine phosphorylation in the nucleus. Tyrosine 114-122 megakaryocyte-associated tyrosine kinase Homo sapiens 102-105 16707123-6 2006 Expression of Chk but not kinase-deficient Chk induced tyrosine phosphorylation of a variety of proteins ranging from 23 kDa to approximately 200 kDa, especially in Triton X-100-insoluble fraction that included chromatin and the nuclear matrix. Tyrosine 55-63 megakaryocyte-associated tyrosine kinase Homo sapiens 14-17 16707123-7 2006 Intriguingly, in situ subnuclear fractionations revealed that Chk induced tyrosine phosphorylation of proteins that were associated with the nuclear matrix. Tyrosine 74-82 megakaryocyte-associated tyrosine kinase Homo sapiens 62-65 16707123-9 2006 Thus, our findings indicate that the importance of the N-terminal domain to Chk-induced tyrosine phosphorylation in the nucleus, implicating that these nuclear tyrosine-phosphorylated proteins may contribute to inhibition of cell proliferation. Tyrosine 88-96 megakaryocyte-associated tyrosine kinase Homo sapiens 76-79 16707123-9 2006 Thus, our findings indicate that the importance of the N-terminal domain to Chk-induced tyrosine phosphorylation in the nucleus, implicating that these nuclear tyrosine-phosphorylated proteins may contribute to inhibition of cell proliferation. Tyrosine 160-168 megakaryocyte-associated tyrosine kinase Homo sapiens 76-79 12122014-4 2002 The interaction between the CHK SH2 domain and Tyr(P)(1248) of the ErbB-2 receptor has been shown to be specific and critical for CHK function. Tyrosine 47-50 megakaryocyte-associated tyrosine kinase Homo sapiens 28-31 12686554-2 2003 PTKs in the Csk family, Csk and Chk, are rare exceptions for lacking Tyr residues in this loop. Tyrosine 69-72 megakaryocyte-associated tyrosine kinase Homo sapiens 32-35 16243715-3 2005 CSK and CHK inactivate SFKs by specifically phosphorylating a consensus tyrosine (called Y(T)) near their C-termini. Tyrosine 72-80 megakaryocyte-associated tyrosine kinase Homo sapiens 8-11 12444928-3 2003 Tyr-568 has previously been identified as the binding site of the Src family of tyrosine kinases, the Csk-homologous kinase CHK, and the protein tyrosine phosphatase SHP-2. Tyrosine 0-3 megakaryocyte-associated tyrosine kinase Homo sapiens 124-127 12122014-4 2002 The interaction between the CHK SH2 domain and Tyr(P)(1248) of the ErbB-2 receptor has been shown to be specific and critical for CHK function. Tyrosine 47-50 megakaryocyte-associated tyrosine kinase Homo sapiens 130-133 12063569-4 2002 Stimulation of human T47D breast cancer cells with HRG induced the tyrosine phosphorylation of RAFTK and its association with CHK in vitro and in vivo. Tyrosine 67-75 megakaryocyte-associated tyrosine kinase Homo sapiens 126-129 12063569-8 2002 Furthermore, CHK inhibited the tyrosine phosphorylation of the focal adhesion-associated protein, paxillin, and inhibited HRG-induced T47D breast cancer cell migration. Tyrosine 31-39 megakaryocyte-associated tyrosine kinase Homo sapiens 13-16 9461599-2 1998 The Csk homologous kinase (CHK) is a recently identified tyrosine kinase which, like Csk, phosphorylates the C-terminal tyrosine of Src kinases, resulting in inactivation of these enzymes. Tyrosine 57-65 megakaryocyte-associated tyrosine kinase Homo sapiens 4-25 10364466-1 1999 The Csk Homologous Kinase (CHK) has been shown to have an enzymatic activity similar to the tyrosine kinase Csk in that it down-regulates Src family kinase activity by causing phosphorylation of the Src C-terminal tyrosine residue. Tyrosine 92-100 megakaryocyte-associated tyrosine kinase Homo sapiens 4-25 10364466-1 1999 The Csk Homologous Kinase (CHK) has been shown to have an enzymatic activity similar to the tyrosine kinase Csk in that it down-regulates Src family kinase activity by causing phosphorylation of the Src C-terminal tyrosine residue. Tyrosine 92-100 megakaryocyte-associated tyrosine kinase Homo sapiens 27-30 10364466-4 1999 Studies using immobilized c-Kit phosphopeptides show that Lyn is able to specifically associate with the tyrosine-phosphorylated juxtamembrane 568Y*VY*IDPT sequence of c-Kit which has previously been shown to associate with CHK. Tyrosine 105-113 megakaryocyte-associated tyrosine kinase Homo sapiens 224-227 10364466-6 1999 Examination of total tyrosine phosphorylation by Western blotting showed that over-expression of CHK resulted in a reduction in the levels of tyrosine phosphorylations in the range of 50-60 kDa, but had no apparent effect on c-Kit autophosphorylation. Tyrosine 21-29 megakaryocyte-associated tyrosine kinase Homo sapiens 97-100 10364466-6 1999 Examination of total tyrosine phosphorylation by Western blotting showed that over-expression of CHK resulted in a reduction in the levels of tyrosine phosphorylations in the range of 50-60 kDa, but had no apparent effect on c-Kit autophosphorylation. Tyrosine 142-150 megakaryocyte-associated tyrosine kinase Homo sapiens 97-100 10080957-0 1999 The Csk homologous kinase, Chk, binds tyrosine phosphorylated paxillin in human blastic T cells. Tyrosine 38-46 megakaryocyte-associated tyrosine kinase Homo sapiens 4-25 10080957-0 1999 The Csk homologous kinase, Chk, binds tyrosine phosphorylated paxillin in human blastic T cells. Tyrosine 38-46 megakaryocyte-associated tyrosine kinase Homo sapiens 27-30 10080957-5 1999 Interestingly, Chk specifically bound tyrosine phosphorylated paxillin. Tyrosine 38-46 megakaryocyte-associated tyrosine kinase Homo sapiens 15-18 10080957-7 1999 Using GST fusion proteins, we determined that the Chk SH2 domain, not the SH3 domain, bound tyrosine phosphorylated paxillin. Tyrosine 92-100 megakaryocyte-associated tyrosine kinase Homo sapiens 50-53 10080957-9 1999 Using Far Western analysis, we revealed that the Chk SH2 domain directly associates with tyrosine phosphorylated paxillin. Tyrosine 89-97 megakaryocyte-associated tyrosine kinase Homo sapiens 49-52 10080957-11 1999 These studies provide important insight into the role of Chk in tyrosine mediated signaling, as well as T cell physiology. Tyrosine 64-72 megakaryocyte-associated tyrosine kinase Homo sapiens 57-60 11309195-8 2001 Chk overexpression induced a decrease in autophosphorylation of Lyn and concomitant changes in levels of tyrosine phosphorylation of proteins associated with both fractions. Tyrosine 105-113 megakaryocyte-associated tyrosine kinase Homo sapiens 0-3 11309195-9 2001 These results indicate that Chk, Lyn and the tyrosine-phosphorylated proteins localize to mitotic chromosomes and spindles, suggesting that Chk-dependent tyrosine phosphorylation, presumably through Lyn, may be involved in chromosome dynamics. Tyrosine 45-53 megakaryocyte-associated tyrosine kinase Homo sapiens 140-143 11309195-9 2001 These results indicate that Chk, Lyn and the tyrosine-phosphorylated proteins localize to mitotic chromosomes and spindles, suggesting that Chk-dependent tyrosine phosphorylation, presumably through Lyn, may be involved in chromosome dynamics. Tyrosine 154-162 megakaryocyte-associated tyrosine kinase Homo sapiens 28-31 11309195-9 2001 These results indicate that Chk, Lyn and the tyrosine-phosphorylated proteins localize to mitotic chromosomes and spindles, suggesting that Chk-dependent tyrosine phosphorylation, presumably through Lyn, may be involved in chromosome dynamics. Tyrosine 154-162 megakaryocyte-associated tyrosine kinase Homo sapiens 140-143 9461599-2 1998 The Csk homologous kinase (CHK) is a recently identified tyrosine kinase which, like Csk, phosphorylates the C-terminal tyrosine of Src kinases, resulting in inactivation of these enzymes. Tyrosine 57-65 megakaryocyte-associated tyrosine kinase Homo sapiens 27-30 8999872-7 1997 CHK-SH2 and CHK-SH3-SH2, but not CHK-SH3 or CHK-NH2-SH3, precipitated the tyrosine-phosphorylated ErbB-2 upon stimulation with heregulin. Tyrosine 74-82 megakaryocyte-associated tyrosine kinase Homo sapiens 0-3 8999872-7 1997 CHK-SH2 and CHK-SH3-SH2, but not CHK-SH3 or CHK-NH2-SH3, precipitated the tyrosine-phosphorylated ErbB-2 upon stimulation with heregulin. Tyrosine 74-82 megakaryocyte-associated tyrosine kinase Homo sapiens 12-15 8999872-7 1997 CHK-SH2 and CHK-SH3-SH2, but not CHK-SH3 or CHK-NH2-SH3, precipitated the tyrosine-phosphorylated ErbB-2 upon stimulation with heregulin. Tyrosine 74-82 megakaryocyte-associated tyrosine kinase Homo sapiens 12-15 8999872-7 1997 CHK-SH2 and CHK-SH3-SH2, but not CHK-SH3 or CHK-NH2-SH3, precipitated the tyrosine-phosphorylated ErbB-2 upon stimulation with heregulin. Tyrosine 74-82 megakaryocyte-associated tyrosine kinase Homo sapiens 12-15 8999872-9 1997 In vivo association of the tyrosine-phosphorylated ErbB-2 with CHK was observed in co-immunoprecipitation studies with anti-CHK antibodies. Tyrosine 27-35 megakaryocyte-associated tyrosine kinase Homo sapiens 63-66 8999872-9 1997 In vivo association of the tyrosine-phosphorylated ErbB-2 with CHK was observed in co-immunoprecipitation studies with anti-CHK antibodies. Tyrosine 27-35 megakaryocyte-associated tyrosine kinase Homo sapiens 124-127 7530249-10 1995 Functional studies indicated that MATK can phosphorylate the carboxyl-terminal conserved tyrosine of the Src protein. Tyrosine 89-97 megakaryocyte-associated tyrosine kinase Homo sapiens 34-38 28784162-0 2017 Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine. Tyrosine 146-154 megakaryocyte-associated tyrosine kinase Homo sapiens 0-21 28784162-0 2017 Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine. Tyrosine 146-154 megakaryocyte-associated tyrosine kinase Homo sapiens 23-26 8288563-5 1994 Sequence comparisons also indicate that matk contains src homology region 2 and 3 domains but lacks the NH2-terminal myristylation signal, the negative regulatory tyrosine (Tyr-527), and the autophosphorylation site (Tyr-416) corresponding to those found in src. Tyrosine 163-171 megakaryocyte-associated tyrosine kinase Homo sapiens 40-44 8288563-5 1994 Sequence comparisons also indicate that matk contains src homology region 2 and 3 domains but lacks the NH2-terminal myristylation signal, the negative regulatory tyrosine (Tyr-527), and the autophosphorylation site (Tyr-416) corresponding to those found in src. Tyrosine 173-176 megakaryocyte-associated tyrosine kinase Homo sapiens 40-44 8288563-5 1994 Sequence comparisons also indicate that matk contains src homology region 2 and 3 domains but lacks the NH2-terminal myristylation signal, the negative regulatory tyrosine (Tyr-527), and the autophosphorylation site (Tyr-416) corresponding to those found in src. Tyrosine 217-220 megakaryocyte-associated tyrosine kinase Homo sapiens 40-44