PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
16901822-0	2006	Trimethylguanosine nucleoside inhibits cross-linking between Snurportin 1 and m3G-CAPPED U1 snRNA.	trimethylguanosine nucleoside	0-29	snurportin 1	Homo sapiens	61-73
18028944-1	2007	The nuclear import of assembled spliceosomal subunits, the uridine-rich small nuclear ribonucleoprotein particles (U snRNPs), is mediated by a nuclear import receptor adaptor couple of importin beta (Imp beta) and snurportin1 (SPN1).	Uridine	59-66	snurportin 1	Homo sapiens	214-225
18028944-1	2007	The nuclear import of assembled spliceosomal subunits, the uridine-rich small nuclear ribonucleoprotein particles (U snRNPs), is mediated by a nuclear import receptor adaptor couple of importin beta (Imp beta) and snurportin1 (SPN1).	Uridine	59-66	snurportin 1	Homo sapiens	227-231
18028944-3	2007	The crystal structure of Imp beta (127-876) in complex with the Imp beta-binding (IBB) domain of SPN1 (1-65) at 2.8-A resolution reveals that Imp beta adopts an open conformation, which is unique for a functional Imp beta/cargo complex, and rather surprisingly, it resembles the conformation of the Imp beta/RanGTP complex.	rangtp	308-314	snurportin 1	Homo sapiens	97-101
18028944-4	2007	As binding of RanGTP to Imp beta usually triggers the release of import complexes from the NPC, we propose that by already mimicking a conformation similar to Imp beta/RanGTP the independent dissociation of Imp beta/SPN1 from the nuclear basket is energetically aided.	rangtp	14-20	snurportin 1	Homo sapiens	216-220
18028944-4	2007	As binding of RanGTP to Imp beta usually triggers the release of import complexes from the NPC, we propose that by already mimicking a conformation similar to Imp beta/RanGTP the independent dissociation of Imp beta/SPN1 from the nuclear basket is energetically aided.	rangtp	168-174	snurportin 1	Homo sapiens	216-220
16901822-5	2006	In this report, we show how a synthesized trimethylguanosine nucleoside affects the binding of Snurportin 1 to m3G-capped U1 snRNA in a UV-cross-linking assay.	trimethylguanosine nucleoside	42-71	snurportin 1	Homo sapiens	95-107
16901822-6	2006	The data indicated that TMG nucleoside is an essential component required in the recognition by Snurportin 1, thus suggesting that interaction of Snurportin 1 with U1 snRNA is not strictly dependent on the presence of the whole cap structure, but rather on the presence of the TMG nucleoside structure.	tmg nucleoside	24-38	snurportin 1	Homo sapiens	96-108
16901822-6	2006	The data indicated that TMG nucleoside is an essential component required in the recognition by Snurportin 1, thus suggesting that interaction of Snurportin 1 with U1 snRNA is not strictly dependent on the presence of the whole cap structure, but rather on the presence of the TMG nucleoside structure.	tmg nucleoside	24-38	snurportin 1	Homo sapiens	146-158
16901822-6	2006	The data indicated that TMG nucleoside is an essential component required in the recognition by Snurportin 1, thus suggesting that interaction of Snurportin 1 with U1 snRNA is not strictly dependent on the presence of the whole cap structure, but rather on the presence of the TMG nucleoside structure.	tmg nucleoside	277-291	snurportin 1	Homo sapiens	96-108
16901822-6	2006	The data indicated that TMG nucleoside is an essential component required in the recognition by Snurportin 1, thus suggesting that interaction of Snurportin 1 with U1 snRNA is not strictly dependent on the presence of the whole cap structure, but rather on the presence of the TMG nucleoside structure.	tmg nucleoside	277-291	snurportin 1	Homo sapiens	146-158
16901822-7	2006	These results indicate that the free nucleoside TMG could be a candidate to be an inhibitor of the interaction between Snurportin 1 and U snRNAs.	nucleoside tmg	37-51	snurportin 1	Homo sapiens	119-131
15920472-8	2005	The specificity of the m3G-cap recognition by snurportin1 was evaluated by fluorescence spectroscopy, demonstrating the importance of a highly solvent exposed tryptophan for the discrimination of m7G-capped RNAs.	Tryptophan	159-169	snurportin 1	Homo sapiens	46-57
16030253-2	2005	After formation of an Sm-core and a trimethylguanosine (TMG) cap, the RNPs are transported into the nucleus via the import adaptor snurportin1 (SPN) and the import receptor importin-beta.	tmg	56-59	snurportin 1	Homo sapiens	131-142
16030253-2	2005	After formation of an Sm-core and a trimethylguanosine (TMG) cap, the RNPs are transported into the nucleus via the import adaptor snurportin1 (SPN) and the import receptor importin-beta.	tmg	56-59	snurportin 1	Homo sapiens	144-147
16030253-4	2005	Mutation of a single arginine residue within the importin-beta binding domain (IBB) disrupted the interaction with importin-beta, but preserved the ability of SPN to bind Xpo1 or TMG caps.	Arginine	21-29	snurportin 1	Homo sapiens	159-162
16030253-9	2005	SPN also relocalizes to Cajal bodies upon treatment with leptomycin B.	leptomycin B	57-69	snurportin 1	Homo sapiens	0-3
15920472-9	2005	The critical role of this tryptophan and as well of a tryptophan continuing the RNA base stack was confirmed by nuclear import assays and cap-binding activity tests using several snurportin1 mutants.	Tryptophan	26-36	snurportin 1	Homo sapiens	179-190
15920472-9	2005	The critical role of this tryptophan and as well of a tryptophan continuing the RNA base stack was confirmed by nuclear import assays and cap-binding activity tests using several snurportin1 mutants.	Tryptophan	54-64	snurportin 1	Homo sapiens	179-190
23885126-2	2013	Snurportin1 (SPN1), the import adaptor, binds to trimethylguanosine (TMG) caps on spliceosomal small nuclear RNAs.	trimethylguanosine	49-67	snurportin 1	Homo sapiens	0-11
11815630-3	2002	Here, we show that recombinant snurportin1 and importin-beta (impbeta) are not only necessary, but also sufficient for U1 snRNP transport to the nuclei of digitonin-permeabilized HeLa cells.	Digitonin	155-164	snurportin 1	Homo sapiens	31-42
26118337-1	2015	Snurportin 1 is an adaptor protein that mediates the active nuclear import of uridine-rich small nuclear RNAs (U snRNA) by the importin-beta receptor pathway.	Uridine	78-85	snurportin 1	Homo sapiens	0-12
15333938-1	2004	The nuclear import of spliceosomal UsnRNPs is mediated by the transport adaptor snurportin 1 (SPN1), which specifically recognizes the 2,2,7-trimethylguanosine (m(3)G) cap at the 5" end of UsnRNAs.	N(2),N(2),7-trimethylguanosine	135-159	snurportin 1	Homo sapiens	80-92
15333938-1	2004	The nuclear import of spliceosomal UsnRNPs is mediated by the transport adaptor snurportin 1 (SPN1), which specifically recognizes the 2,2,7-trimethylguanosine (m(3)G) cap at the 5" end of UsnRNAs.	N(2),N(2),7-trimethylguanosine	135-159	snurportin 1	Homo sapiens	94-98
12095920-10	2002	Cell fractionation studies showed that SPN binds preferentially to cytoplasmic SMN complexes.	(S)-(+)-Mandelic acid	79-82	snurportin 1	Homo sapiens	39-42
23952175-4	2013	Moreover, it was found that the binding affinity of the modified U1 snRNA with an ethylene glycol linkage to snurportin 1 (nuclear import adaptor) was as high as that of the unmodified RNA.	Ethylene Glycol	82-97	snurportin 1	Homo sapiens	109-121
23885126-2	2013	Snurportin1 (SPN1), the import adaptor, binds to trimethylguanosine (TMG) caps on spliceosomal small nuclear RNAs.	tmg	69-72	snurportin 1	Homo sapiens	0-11
23885126-4	2013	We identify CG42303/snup as the Drosophila orthologue of human snurportin1 (SNUPN).	cg42303	12-19	snurportin 1	Homo sapiens	63-74
23885126-4	2013	We identify CG42303/snup as the Drosophila orthologue of human snurportin1 (SNUPN).	cg42303	12-19	snurportin 1	Homo sapiens	76-81