PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10471274-0	1999	Conformational states of the nuclear GTP-binding protein Ran and its complexes with the exchange factor RCC1 and the effector protein RanBP1.	Guanosine Triphosphate	37-40	RAN binding protein 1	Homo sapiens	134-140	
10471274-7	1999	In complex with the Ran-binding protein RanBP1, one of the Ran.GTP conformations (state 2) is stabilized.	Guanosine Triphosphate	63-66	RAN binding protein 1	Homo sapiens	40-46	
9315840-5	1997	Affinities of RanBP1 for Ran in the GTP-bound state were in the nanomolar range, while Ran.GDP bound RanBP1 with a dissociation constant around 10 microM.	Guanosine Triphosphate	36-39	RAN binding protein 1	Homo sapiens	14-20	
10397757-1	1999	Mammalian Ran-binding protein-1 (RanBP1) and its fission yeast homologue, sbp1p, are cytosolic proteins that interact with the GTP-charged form of Ran GTPase through a conserved Ran-binding domain (RBD).	Guanosine Triphosphate	127-130	RAN binding protein 1	Homo sapiens	33-39	
10347184-4	1999	Third, and most surprisingly, RanBP1/RanGTP/Crm1 can be disassembled without GTP hydrolysis by the nucleotide exchange factor RanGEF.	Guanosine Triphosphate	40-43	RAN binding protein 1	Homo sapiens	30-36	
9398678-6	1997	In contrast to wild-type Ran, T42A-Ran.GTP binds very weakly or not detectably to three proposed Ran effectors, Ran-binding protein 1 (RanBP1), Ran-binding protein 2 (RanBP2, a nucleoporin), and karyopherin beta (a component of the nuclear protein import pathway), and is not stimulated to hydrolyze bound GTP by Ran GTPase-activating protein, RanGAP1.	Guanosine Triphosphate	39-42	RAN binding protein 1	Homo sapiens	135-141	
9428644-4	1997	The transiently released RanGTP x RanBP1 complex is then induced by RanGAP to hydrolyse GTP, preventing the receptor to rebind RanGTP.	Guanosine Triphosphate	28-31	RAN binding protein 1	Homo sapiens	34-40	
8995296-2	1997	RanBP1 is a cytosolic Ran-binding protein that inhibits RCC1-stimulated release of GTP from Ran.	Guanosine Triphosphate	83-86	RAN binding protein 1	Homo sapiens	0-6	
8995296-11	1997	These results demonstrate that RanBP1 and karyopherin beta interact with distinct sites of Ran and suggest that RanBP1 plays an essential role in nuclear transport by permitting RanGAP-mediated hydrolysis of GTP on Ran complexed to karyopherin beta.	Guanosine Triphosphate	208-211	RAN binding protein 1	Homo sapiens	112-118	
8995296-11	1997	These results demonstrate that RanBP1 and karyopherin beta interact with distinct sites of Ran and suggest that RanBP1 plays an essential role in nuclear transport by permitting RanGAP-mediated hydrolysis of GTP on Ran complexed to karyopherin beta.	Guanosine Triphosphate	208-211	RAN binding protein 1	Homo sapiens	31-37	
10995230-6	2000	We show that RanBP1 and the four RanBDis from RanBP2 have comparable affinities for Ran.GTP (10(8)-10(9) M(-1)).	Guanosine Triphosphate	88-91	RAN binding protein 1	Homo sapiens	13-19	
7882974-8	1995	RanBP1 is the first member of a new class of proteins regulating the binding and hydrolysis of GTP by Ras-related proteins.	Guanosine Triphosphate	95-98	RAN binding protein 1	Homo sapiens	0-6	
32594833-7	2020	Together, our findings reveal an important mitotic role for RanBP1 in human somatic cells, controlling the spatial distribution and magnitude of mitotic Ran-GTP production and thereby ensuring the accurate execution of Ran-dependent mitotic events.	Guanosine Triphosphate	157-160	RAN binding protein 1	Homo sapiens	60-66	
31163384-5	2019	Specifically, SGK1 affects paclitaxel sensitivity in RKO colon carcinoma cells by modulating the specificity protein 1 (SP1)-dependent expression of Ran-specific GTPase-activating protein (RANBP1), a member of the GTP-binding nuclear protein Ran (RAN) network that is required for the organization and function of the mitotic spindle.	Guanosine Triphosphate	162-165	RAN binding protein 1	Homo sapiens	189-195	
28358001-8	2017	Experiments using RANGTP conformational antibodies confirmed that SGK1, through RANBP1, decreases the level of the GTP-bound state of RAN.	Guanosine Triphosphate	21-24	RAN binding protein 1	Homo sapiens	80-86	
10995230-10	2000	In addition, we show that the RanBDis of RanBP2 are full equivalents of RanBP1 in that they also costimulate RanGAP-catalyzed GTP hydrolysis in Ran and relieve the GTPase block in a Ran.GTP.transportin complex.	Guanosine Triphosphate	126-129	RAN binding protein 1	Homo sapiens	72-78	
10779340-3	2000	We now show that RanBP1 accumulates in nuclei of cells treated with the export inhibitor, leptomycin B, and collapse of the nucleocytoplasmic Ran:GTP gradient leads to equilibration of RanBP1 across the nuclear envelope.	Guanosine Triphosphate	146-149	RAN binding protein 1	Homo sapiens	17-23	
10779340-3	2000	We now show that RanBP1 accumulates in nuclei of cells treated with the export inhibitor, leptomycin B, and collapse of the nucleocytoplasmic Ran:GTP gradient leads to equilibration of RanBP1 across the nuclear envelope.	Guanosine Triphosphate	146-149	RAN binding protein 1	Homo sapiens	185-191	
10779340-6	2000	In permeabilized cells, nuclear accumulation of GST-RanBP1(1-161) requires nuclear Ran:GTP but is not inhibited by a dominant interfering G19V mutant of Ran.	Guanosine Triphosphate	87-90	RAN binding protein 1	Homo sapiens	52-58	
10779340-10	2000	These data indicate that RanBP1 translocates through the pores by an active, nonclassical mechanism and requires Ran:GTP for nuclear accumulation.	Guanosine Triphosphate	117-120	RAN binding protein 1	Homo sapiens	25-31	
10779340-11	2000	Shuttling of RanBP1 may function to clear nuclear pores of Ran:GTP, to prevent premature release of import cargo from transport receptors.	Guanosine Triphosphate	63-66	RAN binding protein 1	Homo sapiens	13-19