PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15845350-2	2005	The initially described phosphorylation sites of Src include an activating phosphotyrosine 416 that results from autophosphorylation, and an inhibiting phosphotyrosine 527 that results from phosphorylation by C-terminal Src kinase (Csk) and Csk homologous kinase.	Phosphotyrosine	152-167	C-terminal Src kinase	Homo sapiens	209-230	
18056706-2	2008	PAG has a role in negative regulation of Src family kinases in T-cells by recruitment of Csk (C-terminal Src kinase) to the membrane via binding to PAG phosphotyrosine 317.	Phosphotyrosine	152-167	C-terminal Src kinase	Homo sapiens	89-92	
18056706-2	2008	PAG has a role in negative regulation of Src family kinases in T-cells by recruitment of Csk (C-terminal Src kinase) to the membrane via binding to PAG phosphotyrosine 317.	Phosphotyrosine	152-167	C-terminal Src kinase	Homo sapiens	94-115	
8995444-5	1997	Like p50csk, Chk reduced the elevated phosphotyrosine levels and the augmented activity of Src family kinases in Csk-deficient fibroblasts.	Phosphotyrosine	38-53	C-terminal Src kinase	Homo sapiens	5-11	
9221755-2	1997	Because the tyrosine kinase Csk is a potential negative regulator of lymphocyte activation, we examined the effects of BCR and FcgammaRIIB1 engagement on the binding of Csk to phosphotyrosine-containing proteins.	Phosphotyrosine	176-191	C-terminal Src kinase	Homo sapiens	169-172	
10803607-9	2000	In c-Src kinase reactions, polarization decreased with time as reaction products displaced the fluorescein-labeled phosphopeptide from the anti-phosphotyrosine antibodies.	Phosphotyrosine	144-159	C-terminal Src kinase	Homo sapiens	3-15	
9618476-4	1998	The semisynthetic tail-phosphorylated Csk showed evidence of an intramolecular phosphotyrosine-Src homology 2 interaction and an unexpected increase in catalytic phosphoryl transfer efficiency toward a physiologically relevant substrate compared with the non-tail-phosphorylated control.	Phosphotyrosine	79-94	C-terminal Src kinase	Homo sapiens	38-41	
9425036-12	1998	The failure of the Lck phosphorylation product (phosphotyrosine-505) to significantly inhibit Csk phosphorylation of Lck is consistent with a catalytic model involving multidomain structural interactions between substrate and enzyme.	Phosphotyrosine	48-63	C-terminal Src kinase	Homo sapiens	94-97	
24632723-7	2014	Our results collectively indicate that SHP-2 alters Src kinase activity by interfering with the complex formation between CSK and phosphotyrosine caveolin-1 in the presence of H2O2, thus functions as a positive regulator in Src signaling under oxidative stress in brain astrocytes.	Phosphotyrosine	130-145	C-terminal Src kinase	Homo sapiens	122-125	
7524477-7	1994	Repression of Fyn activity by Csk reduced binding of Fyn to phosphopeptides to undetectable levels, supporting the model that predicts an intramolecular interaction of the Fyn SH2 domain with a C-terminal phosphotyrosine residue.	Phosphotyrosine	205-220	C-terminal Src kinase	Homo sapiens	30-33	
7683128-3	1993	Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity.	Phosphotyrosine	28-43	C-terminal Src kinase	Homo sapiens	128-140	
7529872-4	1995	Immunofluorescence for the induced p50csk was localized in the cytoplasm and distinctly in focal adhesions, in which the amount of phosphotyrosine containing proteins was also increased.	Phosphotyrosine	131-146	C-terminal Src kinase	Homo sapiens	35-41	
28768887-6	2017	Biochemical analyses of premetazoan pTyr signalling components have further revealed the premetazoan origin of many key features of metazoan pTyr signalling, and the metazoan establishment of others, including the Csk-mediated negative regulation of the activity of Src, a conserved tyrosine kinase in the Holozoa.	Phosphotyrosine	36-40	C-terminal Src kinase	Homo sapiens	214-217