PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16289966-3	2006	We successively identified p95 as the nucleolin and the first signal transduction pathway specifically triggered by CD21 activation, i.e.: pp60Src activation, tyrosine phosphorylation of p95 nucleolin, its interaction with SH2 domains of p85 subunit and PI 3-kinase activation, followed by AKT-GSK-3 activations.	Tyrosine	159-167	nucleolin	Homo sapiens	38-47	
25092868-3	2014	Syk binds robustly to nucleolin and phosphorylates it on tyrosine, enhancing its ability to bind the Bcl-x(L) mRNA.	Tyrosine	57-65	nucleolin	Homo sapiens	22-31	
23161541-3	2013	Interestingly, cell surface NCL localization was detected only in cells expressing alpha(v)beta(3) and depended on the phosphorylation of beta(3) at Tyr(773) through receptor protein-tyrosine phosphatase beta/zeta (RPTPbeta/zeta) and c-Src activation.	Tyrosine	149-152	nucleolin	Homo sapiens	28-31	
23161541-6	2013	Collectively, these data suggest that both expression and beta(3) integrin phosphorylation at Tyr(773) determine the cell surface localization of NCL downstream of the RPTPbeta/zeta/c-Src signaling cascade and can be used as a biomarker for the use of cell surface NCL antagonists as anticancer agents.	Tyrosine	94-97	nucleolin	Homo sapiens	146-149	
18504038-5	2008	We have also found P-selectin binding to Colo-320 cells induces tyrosine phosphorylation specifically of cell-surface nucleolin and formation of a signaling complex containing cell-surface nucleolin, PI3-K and p38 MAPK.	Tyrosine	64-72	nucleolin	Homo sapiens	118-127	
16289966-3	2006	We successively identified p95 as the nucleolin and the first signal transduction pathway specifically triggered by CD21 activation, i.e.: pp60Src activation, tyrosine phosphorylation of p95 nucleolin, its interaction with SH2 domains of p85 subunit and PI 3-kinase activation, followed by AKT-GSK-3 activations.	Tyrosine	159-167	nucleolin	Homo sapiens	191-200	
12938232-1	2003	We previously demonstrated that CR2 activation on human B lymphocyte surface specifically triggered tyrosine phosphorylation of the 95-kDa nucleolin, this leading to its binding on SH2 domains of p85 sub-unit of PI 3-kinase and to activation of this enzyme.	Tyrosine	100-108	nucleolin	Homo sapiens	139-148	
12938232-4	2003	Upstream, we demonstrated that pp60src, a tyrosine kinase of the src family, was involved in tyrosine phosphorylation of nucleolin, while syk tyrosine kinase was not.	Tyrosine	42-50	nucleolin	Homo sapiens	121-130	
11207269-0	2001	Activation of the EBV/C3d receptor (CR2, CD21) on human B lymphocyte surface triggers tyrosine phosphorylation of the 95-kDa nucleolin and its interaction with phosphatidylinositol 3 kinase.	Tyrosine	86-94	nucleolin	Homo sapiens	125-134	
11207269-4	2001	Then, the isolated 95-kDa tyrosine phosphorylated band was submitted to amino acid analysis by mass spectrometry; the two different isolated peptides were characterized by amino acid sequences 100% identical with two different domains of nucleolin, localized between aa 411--420 and 611--624.	Tyrosine	26-34	nucleolin	Homo sapiens	238-247	
11207269-6	2001	Functional studies demonstrated that CR2 activation induced, within a brief span of 2 min, tyrosine phosphorylation of nucleolin and its interaction with Src homology 2 domains of the p85 subunit of PI 3 kinase and of 3BP2 and Grb2, but not with Src homology 2 domains of Fyn and Gap.	Tyrosine	91-99	nucleolin	Homo sapiens	119-128	
11207269-8	2001	Furthermore, tyrosine phosphorylation of nucleolin was also induced in normal B lymphocytes by CR2 activation but neither by CD19 nor BCR activation.	Tyrosine	13-21	nucleolin	Homo sapiens	41-50	
11207269-9	2001	These data support that tyrosine phosphorylation of nucleolin and its interaction with PI 3 kinase p85 subunit constitute one of the earlier steps in the specific intracellular signaling pathway of CR2.	Tyrosine	24-32	nucleolin	Homo sapiens	52-61