PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
16888326-8	2006	Finally, we show a genetic interaction between LTV1 and YRB2, a gene that encodes a Ran-GTP-, Crm1-binding protein that facilitates the small subunit export.	Guanosine Triphosphate	88-91	Yrb2p	Saccharomyces cerevisiae S288C	56-60
25437554-3	2014	Efficient export of NES-cargoes requires Yrb2p (yeast RanBP3), a primarily nuclear protein containing nucleoporin-like phenylalanine-glycine (FG) repeats and a low-affinity Gsp1p-binding domain (RanBD).	phenylalanine-glycine	119-140	Yrb2p	Saccharomyces cerevisiae S288C	41-46
16143306-1	2005	A Gtr1p GTPase, the GDP mutant of which suppresses both temperature-sensitive mutants of Saccharomyces cerevisiae RanGEF/Prp20p and RanGAP/Rna1p, was presently found to interact with Yrb2p, the S. cerevisiae homologue of mammalian Ran-binding protein 3.	Guanosine Diphosphate	20-23	Yrb2p	Saccharomyces cerevisiae S288C	183-188
9395535-9	1997	Yrb2p binding to Gsp1p (yeast Ran) as well as to a novel 150-kDa GTP-binding protein is also detected.	Guanosine Triphosphate	65-68	Yrb2p	Saccharomyces cerevisiae S288C	0-5
9395535-10	1997	The Ran binding domain of Yrb2p is essential for function and for its association with Prp20p and the GTP-binding proteins.	Guanosine Triphosphate	102-105	Yrb2p	Saccharomyces cerevisiae S288C	26-31
9121474-7	1997	Similar to Yrb1p, Yrb2p bound to GTP-Gsp1p but not to GDP-Gsp1p and enhanced the GTPase-activating activity of Rna1p.	Guanosine Triphosphate	33-36	Yrb2p	Saccharomyces cerevisiae S288C	18-23
25437554-4	2014	Here, we show that Yrb2p strikingly accelerates the association of Gsp1p-GTP and NES to Xpo1p.	Guanosine Triphosphate	73-76	Yrb2p	Saccharomyces cerevisiae S288C	19-24
25437554-5	2014	We have solved the crystal structure of the Xpo1p-Yrb2p-Gsp1p-GTP complex, a key assembly intermediate that can bind cargo rapidly.	Guanosine Triphosphate	62-65	Yrb2p	Saccharomyces cerevisiae S288C	50-55
25437554-6	2014	Although the NES-binding cleft of Xpo1p is closed in this intermediate, our data suggest that preloading of Gsp1p-GTP onto Xpo1p by Yrb2p, conformational flexibility of Xpo1p, and the low affinity of RanBD enable active displacement of Yrb2p RanBD by NES to occur effectively.	gsp1p-gtp	108-117	Yrb2p	Saccharomyces cerevisiae S288C	132-137
25437554-6	2014	Although the NES-binding cleft of Xpo1p is closed in this intermediate, our data suggest that preloading of Gsp1p-GTP onto Xpo1p by Yrb2p, conformational flexibility of Xpo1p, and the low affinity of RanBD enable active displacement of Yrb2p RanBD by NES to occur effectively.	gsp1p-gtp	108-117	Yrb2p	Saccharomyces cerevisiae S288C	236-241