PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3349036-0	1988	Growth hormone promoted tyrosyl phosphorylation of growth hormone receptors in murine 3T3-F442A fibroblasts and adipocytes.	cyclo(tyrosyl-tyrosyl)	24-31	growth hormone	Mus musculus	0-14	
2478547-1	1989	We have shown previously that growth hormone (GH) promotes the phosphorylation of its receptor on tyrosyl residues (Foster, C. M., Shafer, J.	cyclo(tyrosyl-tyrosyl)	98-105	growth hormone	Mus musculus	30-44	
2478547-1	1989	We have shown previously that growth hormone (GH) promotes the phosphorylation of its receptor on tyrosyl residues (Foster, C. M., Shafer, J.	cyclo(tyrosyl-tyrosyl)	98-105	growth hormone	Mus musculus	46-48	
3349036-0	1988	Growth hormone promoted tyrosyl phosphorylation of growth hormone receptors in murine 3T3-F442A fibroblasts and adipocytes.	cyclo(tyrosyl-tyrosyl)	24-31	growth hormone	Mus musculus	51-65	
9231797-0	1997	Growth hormone-induced tyrosyl phosphorylation and deoxyribonucleic acid binding activity of Stat5A and Stat5B.	cyclo(tyrosyl-tyrosyl)	23-30	growth hormone	Mus musculus	0-14	
9343427-7	1997	In 3T3-F442A cells, GH stimulates the interaction of SH2-Bbeta with tyrosyl-phosphorylated JAK2 both in vitro, as assessed by binding of JAK2 in cell lysates to glutathione S-transferase (GST)-SH2-Bbetac or GST-SH2-Bbeta fusion proteins, and in vivo, as assessed by coimmunoprecipitation of JAK2 with SH2-Bbeta.	cyclo(tyrosyl-tyrosyl)	68-75	growth hormone	Mus musculus	20-22	
9343427-8	1997	GH promoted a transient and dose-dependent tyrosyl phosphorylation of SH2-Bbeta in 3T3-F442A cells, further suggesting the involvement of SH2-Bbeta in GH signaling.	cyclo(tyrosyl-tyrosyl)	43-50	growth hormone	Mus musculus	0-2	
9343427-8	1997	GH promoted a transient and dose-dependent tyrosyl phosphorylation of SH2-Bbeta in 3T3-F442A cells, further suggesting the involvement of SH2-Bbeta in GH signaling.	cyclo(tyrosyl-tyrosyl)	43-50	growth hormone	Mus musculus	151-153	
12088868-1	2002	After receptor binding, growth hormone (GH) induces GH receptors (GHR) dimerization and JAK2 is activated after its association with a dimerized GHR, stimulating the tyrosyl phosphorylation of insulin receptor substrate-1 (IRS-1), IRS-2 and Shc proteins.	cyclo(tyrosyl-tyrosyl)	166-173	growth hormone	Mus musculus	24-38	
10757801-4	2000	In a glutathione S-transferase pull-down assay, wild-type SH2-Bbeta and SH2-Bbeta(R555E) with a defective SH2 domain bind to both tyrosyl-phosphorylated JAK2 from growth hormone (GH)-treated cells and non-tyrosyl-phosphorylated JAK2 from control cells, whereas the SH2 domain of SH2-Bbeta binds only to tyrosyl-phosphorylated JAK2 from GH-treated cells.	cyclo(tyrosyl-tyrosyl)	130-137	growth hormone	Mus musculus	163-177	
10757801-4	2000	In a glutathione S-transferase pull-down assay, wild-type SH2-Bbeta and SH2-Bbeta(R555E) with a defective SH2 domain bind to both tyrosyl-phosphorylated JAK2 from growth hormone (GH)-treated cells and non-tyrosyl-phosphorylated JAK2 from control cells, whereas the SH2 domain of SH2-Bbeta binds only to tyrosyl-phosphorylated JAK2 from GH-treated cells.	cyclo(tyrosyl-tyrosyl)	130-137	growth hormone	Mus musculus	179-181	
10757801-4	2000	In a glutathione S-transferase pull-down assay, wild-type SH2-Bbeta and SH2-Bbeta(R555E) with a defective SH2 domain bind to both tyrosyl-phosphorylated JAK2 from growth hormone (GH)-treated cells and non-tyrosyl-phosphorylated JAK2 from control cells, whereas the SH2 domain of SH2-Bbeta binds only to tyrosyl-phosphorylated JAK2 from GH-treated cells.	cyclo(tyrosyl-tyrosyl)	130-137	growth hormone	Mus musculus	336-338