PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11685249-2	2001	The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain.	Serine	99-102	C-terminal Src kinase	Homo sapiens	30-33	
9224730-5	1997	Csk phosphorylation in vitro by PKA is on a serine residue(s) and can reach a stoichiometry of approximately 0.6 mol phosphate per mole of enzyme.	Serine	44-50	C-terminal Src kinase	Homo sapiens	0-3	
12600271-0	2003	Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain.	Serine	64-70	C-terminal Src kinase	Homo sapiens	14-35	
12600271-0	2003	Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain.	Serine	64-70	C-terminal Src kinase	Homo sapiens	37-40	
12600271-0	2003	Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain.	Serine	64-70	C-terminal Src kinase	Homo sapiens	90-93	
12600271-2	2003	Although isolated Csk kinase domain was phosphorylated at Ser(364) by PKA to the same stoichiometry as wild-type Csk, significant activation of the isolated Csk kinase domain by PKA was observed only in the presence of the purified Src homology 3 domain (SH3 domain).	Serine	58-61	C-terminal Src kinase	Homo sapiens	18-21	
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.	Serine	30-36	C-terminal Src kinase	Homo sapiens	256-259