PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9312046-1	1997	Binding of macrophage colony stimulating factor (M-CSF) to its receptor (Fms) induces dimerization and activation of the tyrosine kinase domain of the receptor, resulting in autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins that relay growth and development signals.	Tyrosine	121-129	sperm hammerhead 2	Mus musculus	253-256	
9703981-3	1998	A G-to-A transition changing cysteine to tyrosine in the conserved actin binding domain is detected in sh-2 but absent in laboratory strains and wild mice belonging to different mouse subspecies and species.	Tyrosine	41-49	sperm hammerhead 2	Mus musculus	103-107	
7694287-3	1993	Here we demonstrate that purified recombinant SH2 and HSH3/SH2 domains of p56lck can mediate intermolecular interactions with a number of tyrosine-phosphorylated proteins present in lysates of NIH 3T3 cells transformed by a constitutively activated form of p56lck (p56lckF505).	Tyrosine	138-146	sperm hammerhead 2	Mus musculus	46-49	
7694287-3	1993	Here we demonstrate that purified recombinant SH2 and HSH3/SH2 domains of p56lck can mediate intermolecular interactions with a number of tyrosine-phosphorylated proteins present in lysates of NIH 3T3 cells transformed by a constitutively activated form of p56lck (p56lckF505).	Tyrosine	138-146	sperm hammerhead 2	Mus musculus	59-62	
7694287-5	1993	Using a synthetic phosphopeptide corresponding to the tyrosine-phosphorylated carboxyl terminus of p56lck (amino acids 494-509), purified recombinant Lck SH2 domain, and differentially phosphorylated forms of p56lck we provide evidence that the SH2 domain of p56lck can also mediate intramolecular interactions with the phosphorylated carboxyl terminus.	Tyrosine	54-62	sperm hammerhead 2	Mus musculus	245-248	
7694287-6	1993	Together these results suggest that the SH2 domain of p56lck has a dual function: (i) it can mediate intermolecular interactions with cellular proteins phosphorylated on tyrosine and thus might be involved in building up signaling complexes at the plasma membrane and (ii) it can bind to the tyrosine-phosphorylated carboxyl terminus of p56lck in an intramolecular fashion and thereby might be involved in the regulation of its intrinsic protein-tyrosine kinase activity.	Tyrosine	170-178	sperm hammerhead 2	Mus musculus	40-43	
7694287-6	1993	Together these results suggest that the SH2 domain of p56lck has a dual function: (i) it can mediate intermolecular interactions with cellular proteins phosphorylated on tyrosine and thus might be involved in building up signaling complexes at the plasma membrane and (ii) it can bind to the tyrosine-phosphorylated carboxyl terminus of p56lck in an intramolecular fashion and thereby might be involved in the regulation of its intrinsic protein-tyrosine kinase activity.	Tyrosine	292-300	sperm hammerhead 2	Mus musculus	40-43	
1570157-5	1992	The SH2 domain (but not the SH3 domain) was also required for full oncogenic transformation by Lck molecules activated through removal of tyrosine 505.	Tyrosine	138-146	sperm hammerhead 2	Mus musculus	4-7	
28092051-5	2017	We overexpress a tracer SH2 domain in cells and quantify the change in abundance of tyrosine phosphorylated sites using MS.	Tyrosine	84-92	sperm hammerhead 2	Mus musculus	24-27	
22525464-2	2012	In contrast to the sequence variability of the second SH3bm, tyrosine 89, within the SH2bm is a highly conserved residue among IAV strains.	Tyrosine	61-69	sperm hammerhead 2	Mus musculus	85-88	
12543778-5	2003	Addition of the Abl kinase inhibitor STI-571 to ABL SH2-transformed Rat-1 cells inhibited tyrosine phosphorylation of p145 ABL.	Tyrosine	90-98	sperm hammerhead 2	Mus musculus	52-55	
28290451-0	2017	Development of SH2 probes and pull-down assays to detect pathogen-induced, site-specific tyrosine phosphorylation of the TLR adaptor SCIMP.	Tyrosine	89-97	sperm hammerhead 2	Mus musculus	15-18	
10788787-3	2000	Tyrosine phosphorylation of Syk in cells expressing mSH2(N) Syk after H(2)O(2) treatment was higher than that in cells expressing wild-type Syk or mSH2(C) Syk.	Tyrosine	0-8	sperm hammerhead 2	Mus musculus	52-56	
10788787-3	2000	Tyrosine phosphorylation of Syk in cells expressing mSH2(N) Syk after H(2)O(2) treatment was higher than that in cells expressing wild-type Syk or mSH2(C) Syk.	Tyrosine	0-8	sperm hammerhead 2	Mus musculus	147-151	
10788787-4	2000	The tyrosine phosphorylation of wild-type Syk and mSH2(C) Syk, but not that of mSH2(N), was sensitive to PP2, a specific inhibitor of Src-family protein-tyrosine kinase.	Tyrosine	4-12	sperm hammerhead 2	Mus musculus	50-54	
10788787-5	2000	In oxidative stress, the C-terminal SH2 domain of Syk was demonstrated to be required for induction of tyrosine phosphorylation of cellular proteins, phospholipase C (PLC)-gamma2 phosphorylation, inositol 1,4, 5-triphosphate (IP(3)) generation, Ca(2)(+) release from intracellular stores, and c-Jun N-terminal kinase activation.	Tyrosine	103-111	sperm hammerhead 2	Mus musculus	36-39	
10788787-6	2000	In contrast, in mSH2(N) Syk-expressing cells, tyrosine phosphorylation of intracellular proteins including PLC-gamma2 was markedly induced in oxidative stress.	Tyrosine	46-54	sperm hammerhead 2	Mus musculus	16-20