PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19221419-0	2009	Phosphorylation of a tyrosine in the amyloid-beta protein precursor intracellular domain inhibits Fe65 binding and signaling.	Tyrosine	21-29	amyloid beta precursor protein binding family B member 1	Homo sapiens	98-102	
24086696-10	2013	This is consistent with the negative impact of tyrosine phosphorylation on Fe65 binding to AICD.	Tyrosine	47-55	amyloid beta precursor protein binding family B member 1	Homo sapiens	75-79	
24044023-5	2013	The Tip60 mutation Y327F abolished tyrosine phosphorylation, reduced the inhibition of Tip60 HAT activity, and caused G0-G1 arrest and association with FE65.	Tyrosine	35-43	amyloid beta precursor protein binding family B member 1	Homo sapiens	152-156	
24044023-0	2013	Phosphorylation of Tip60 Tyrosine 327 by Abl Kinase Inhibits HAT Activity through Association with FE65.	Tyrosine	25-33	amyloid beta precursor protein binding family B member 1	Homo sapiens	99-103	
19221419-3	2009	Here we report that phosphorylation of Tyr-682 inhibits the interactions between AbetaPP and Fe65, which is the main regulatory mechanism controlling Fe65 nuclear signaling.	Tyrosine	39-42	amyloid beta precursor protein binding family B member 1	Homo sapiens	93-97	
19221419-3	2009	Here we report that phosphorylation of Tyr-682 inhibits the interactions between AbetaPP and Fe65, which is the main regulatory mechanism controlling Fe65 nuclear signaling.	Tyrosine	39-42	amyloid beta precursor protein binding family B member 1	Homo sapiens	150-154	
19221419-4	2009	Furthermore, we show that tyrosine phosphorylation of AbetaPP also inhibits interaction of the two other Fe65 family members, Fe65L1 and Fe65L2.	Tyrosine	26-34	amyloid beta precursor protein binding family B member 1	Homo sapiens	105-109	
19221419-6	2009	Our results indicate that phosphorylation of the cytoplasmic tail of AbetaPP on Tyr-682 represents a second mechanism, alternative to AbetaPP processing by secretases, that regulates AbetaPP/Fe65 downstream signaling pathways.	Tyrosine	80-83	amyloid beta precursor protein binding family B member 1	Homo sapiens	191-195	
18922798-5	2008	Phosphorylation of FE65 tyrosine 547 within the PTB2 domain has been shown to enhance FE65-APP-mediated transcription but not to influence binding to APP.	Tyrosine	24-32	amyloid beta precursor protein binding family B member 1	Homo sapiens	19-23	
18922798-5	2008	Phosphorylation of FE65 tyrosine 547 within the PTB2 domain has been shown to enhance FE65-APP-mediated transcription but not to influence binding to APP.	Tyrosine	24-32	amyloid beta precursor protein binding family B member 1	Homo sapiens	86-90	
18922798-9	2008	Thus, Dexras1 functions as a suppressor of FE65-APP-mediated transcription, and FE65 tyrosine 547 phosphorylation enhances FE65-APP-mediated transcription, at least in part, by modulating the interaction between FE65 and Dexras1.	Tyrosine	85-93	amyloid beta precursor protein binding family B member 1	Homo sapiens	80-84	
18922798-9	2008	Thus, Dexras1 functions as a suppressor of FE65-APP-mediated transcription, and FE65 tyrosine 547 phosphorylation enhances FE65-APP-mediated transcription, at least in part, by modulating the interaction between FE65 and Dexras1.	Tyrosine	85-93	amyloid beta precursor protein binding family B member 1	Homo sapiens	80-84	
18922798-9	2008	Thus, Dexras1 functions as a suppressor of FE65-APP-mediated transcription, and FE65 tyrosine 547 phosphorylation enhances FE65-APP-mediated transcription, at least in part, by modulating the interaction between FE65 and Dexras1.	Tyrosine	85-93	amyloid beta precursor protein binding family B member 1	Homo sapiens	80-84	
18547980-4	2008	In addition, we detected co-localization of GSK 3beta and Fe65 by confocal microscopy, and this co-localization was disrupted by mutation of the putative WW domain binding motif of GSK 3beta.Finally, in transient transfection assays interaction of GSK 3 beta (wt) with Fe65 induced substantial cell apoptosis, whereas interaction with the GSK 3beta AALA mutant ((371)AALA(374)) did not, and we noted that phosphorylation of the Tyr 216 residue of the GSK 3beta AALA mutant was significantly reduced compared to that of GSK 3beta wild type.	Tyrosine	428-431	amyloid beta precursor protein binding family B member 1	Homo sapiens	58-62	
18547980-5	2008	Thus, our observations indicate that GSK 3beta binds to Fe65 through its (371)PPLA(374) motif and that this interaction regulates apoptosis and phosphorylation of Tyr 216 of GSK 3beta.	Tyrosine	163-166	amyloid beta precursor protein binding family B member 1	Homo sapiens	56-60	
15031292-6	2004	Here, we show that active c-Abl stimulates APP/Fe65-mediated gene transcription and that this effect is mediated by phosphorylation of Fe65 on tyrosine 547 within its second PTB domain.	Tyrosine	143-151	amyloid beta precursor protein binding family B member 1	Homo sapiens	135-139