PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31226791-10	2019	The resultant analog sequence Ac-Leu-Thr-Phe-Aib-Glu-Tyr-Trp-Gln-Leu-Cba-Aib-Ser-Ala-Ala-NH2 exhibited high-affinity target binding (Mdm2 Kd = 43 nM) and significant alpha-helicity in circular dichroism studies.	Tyrosine	53-56	MDM2 proto-oncogene	Homo sapiens	133-137	
17938582-4	2007	The structure reveals that although the principle features of the Mdm2-p53 interaction are preserved in the Mdmx-p53 complex, the Mdmx hydrophobic cleft on which the p53 peptide binds is significantly altered: a part of the cleft is blocked by sidechains of Met and Tyr of the p53-binding pocket of Mdmx.	Tyrosine	266-269	MDM2 proto-oncogene	Homo sapiens	66-70	
29088763-11	2017	Furthermore, we found that overexpression of CENP-K stimulated the tyrosine phosphorylation of the AKT and MDM2 proteins, but inhibited tyrosine phosphorylation of the TP53 protein.	Tyrosine	67-75	MDM2 proto-oncogene	Homo sapiens	107-111	
27481281-7	2013	It was found that the pi-pi stacking between Tyr 51 of MDM2 and ligands is the critical event in MDM2-p53 dissociation.	Tyrosine	45-48	MDM2 proto-oncogene	Homo sapiens	55-59	
27481281-7	2013	It was found that the pi-pi stacking between Tyr 51 of MDM2 and ligands is the critical event in MDM2-p53 dissociation.	Tyrosine	45-48	MDM2 proto-oncogene	Homo sapiens	97-101	
19153082-6	2009	The x-ray structures revealed surprising conformational changes of the binding cleft of HdmX, including an "open conformation" of Tyr(99) and unexpected "cross-talk" between the Trp and Leu pockets.	Tyrosine	130-133	MDM2 proto-oncogene	Homo sapiens	88-92	
19075013-9	2009	One of these phosphorylations, on tyrosine 99, inhibited Hdmx interaction with p53.	Tyrosine	34-42	MDM2 proto-oncogene	Homo sapiens	57-61	
18707164-3	2008	The specific residues of MDM2 that have dominant binding interactions with p53 are specifically identified to be (51)Lys, (54)Leu, (62)Met, (67)Tyr, (72)Gln, (94)Lys, (96)His, and (100)Tyr.	Tyrosine	144-147	MDM2 proto-oncogene	Homo sapiens	25-29	
18707164-3	2008	The specific residues of MDM2 that have dominant binding interactions with p53 are specifically identified to be (51)Lys, (54)Leu, (62)Met, (67)Tyr, (72)Gln, (94)Lys, (96)His, and (100)Tyr.	Tyrosine	185-188	MDM2 proto-oncogene	Homo sapiens	25-29	
16702947-0	2006	c-Abl phosphorylates Hdm2 at tyrosine 276 in response to DNA damage and regulates interaction with ARF.	Tyrosine	29-37	MDM2 proto-oncogene	Homo sapiens	21-25	
16702947-3	2006	As part of this mechanism ATM itself, and the ATM-activated protein tyrosine kinase, c-Abl, inhibit Hdm2 function through phosphorylation of serine 395 and tyrosine 394 (Y394), respectively.	Tyrosine	68-76	MDM2 proto-oncogene	Homo sapiens	100-104	
16702947-4	2006	In the present study, we have identified a novel target of c-Abl in the Hdm2 protein, tyrosine 276 (Y276).	Tyrosine	86-94	MDM2 proto-oncogene	Homo sapiens	72-76	
12110584-0	2002	Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation.	Tyrosine	0-8	MDM2 proto-oncogene	Homo sapiens	28-32	
15985438-0	2005	Secretase-dependent tyrosine phosphorylation of Mdm2 by the ErbB-4 intracellular domain fragment.	Tyrosine	20-28	MDM2 proto-oncogene	Homo sapiens	48-52	
15985438-1	2005	Heregulin activation of the endogenous receptor tyrosine kinase ErbB-4 in ZR-75-1 breast cancer cells provokes tyrosine phosphorylation of Hdm2 in a manner that is sensitive to inhibition of alpha- or gamma-secretase activity, indicating that liberation of the tyrosine kinase intracellular domain (ICD) fragment is required.	Tyrosine	48-56	MDM2 proto-oncogene	Homo sapiens	139-143	
15985438-3	2005	Expression of the ErbB-4 ICD fragment leads to its constitutive association with Mdm2 and tyrosine phosphorylation of Mdm2, a protein that is predominantly localized in the nucleus and that regulates p53 levels.	Tyrosine	90-98	MDM2 proto-oncogene	Homo sapiens	118-122	
9836595-12	1998	However, distance measurement from fluorescence energy transfer indicated that the Tyr 489 residue was only approximately 14 A away from the first metal center, suggesting that the hdm2 protein exists in a compact form, at least in the presence of metal ion.	Tyrosine	83-86	MDM2 proto-oncogene	Homo sapiens	181-185