PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24742684-0	2014	Cell surface translocation of annexin A2 facilitates glutamate-induced extracellular proteolysis.	Glutamic Acid	53-62	annexin A2	Homo sapiens	30-40	
24742684-5	2014	We showed that glutamate translocated both endogenous and AnxA2-GFP to the cell surface in a process dependent on the activity of the NMDA receptor.	Glutamic Acid	15-24	annexin A2	Homo sapiens	58-63	
24742684-6	2014	Glutamate-induced translocation of AnxA2 is dependent on the phosphorylation of tyrosine 23 at the N terminus, and mutation of tyrosine 23 to a non-phosphomimetic variant inhibits the translocation process.	Glutamic Acid	0-9	annexin A2	Homo sapiens	35-40	
24742684-8	2014	These results suggest an involvement of AnxA2 in potentiating glutamate-induced cell death processes.	Glutamic Acid	62-71	annexin A2	Homo sapiens	40-45	
9836589-3	1998	In this report, we have compared the ability of the isolated p36 and p11 subunits to stimulate t-PA-dependent [Glu]plasminogen activation.	Glutamic Acid	111-114	annexin A2	Homo sapiens	61-64	
18412141-5	2008	By site-specific substitution of glutamic acid in the place of serine 11 and 25 in the N-terminus, we show that serine 25 phosphorylation of annexin A2 was associated with the nuclear entry of annexin A2, DNA synthesis and cell proliferation, whereas serine 11 has no obvious influence.	Glutamic Acid	33-46	annexin A2	Homo sapiens	141-151	
12962548-0	2003	Nuclear annexin II negatively regulates growth of LNCaP cells and substitution of ser 11 and 25 to glu prevents nucleo-cytoplasmic shuttling of annexin II.	Glutamic Acid	99-102	annexin A2	Homo sapiens	144-154	
12962548-12	2003	By site-specific substitution of glutamic acid in the place of serines 11 and 25 in the N-terminus, we show that simultaneous phosphorylation of both serines 11 and 25, but not either one alone, prevents nuclear localization of annexin II.	Glutamic Acid	33-46	annexin A2	Homo sapiens	228-238	
8063741-12	1994	Kinetic analyses revealed that Ann-II conferred an approximately 60-fold increase in catalytic efficiency upon t-PA-dependent activation of either Glu-PLG or Lys-PLG.	Glutamic Acid	147-150	annexin A2	Homo sapiens	31-37	
8063741-9	1994	At fixed plasminogen concentrations, preincubation with purified native Ann-II was associated with an approximately 21-fold increase in the rate of Glu-PLG activation and an approximately 14-fold increase in activation of Lys-PLG.	Glutamic Acid	148-151	annexin A2	Homo sapiens	72-78