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Snurportin 1

snurportin1, SPN1, Spn1p, SNUPN
The nuclear import of the spliceosomal snRNPs U1, U2, U4 and U5, is dependent on the presence of a complex nuclear localization signal. The latter is composed of the 5'-2,2,7-terminal trimethylguanosine (m3G) cap structure of the U snRNA and the Sm core domain. The protein encoded by this gene interacts specifically with m3G-cap and functions as an snRNP-specific nuclear import receptor. Alternatively spliced transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: importin, CAN, CRM1, Spt6, V1a
Papers using snurportin1 antibodies
Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1
Supplier
Görlich Dirk et al., In The Journal of Cell Biology, 1997
... Snurportin 1 was cloned into the BamHI-XmaI sites of pQE30 (Qiagen), expressed with an NH ...
Papers on snurportin1
Combining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1-RanGTP-SPN1-Nup214 quaternary nuclear export complex.
New
Ficner et al., Göttingen, Germany. In Acta Crystallogr Sect F Struct Biol Commun, Jan 2016
Here, the crystallization and structure determination of a quaternary nuclear export complex consisting of the exportin CRM1, the small GTPase Ran in its GTP-bound form, the export cargo SPN1 and an FG repeat-containing fragment of the nuclear pore complex component nucleoporin Nup214 fused to maltose-binding protein is reported.
Genetic association of marbling score with intragenic nucleotide variants at selection signals of the bovine genome.
New
Lee et al., Seoul, South Korea. In Animal, Jan 2016
Genetic associations of MS were found (P<3.88×10-4) with six intragenic nucleotide variants on bovine autosomes 3 (cache domain containing 1, CACHD1), 5 (like-glycosyltransferase, LARGE), 16 (cell division cycle 42 binding protein kinase alpha, CDC42BPA) and 21 (snurportin 1, SNUPN; protein tyrosine phosphatase, non-receptor type 9, PTPN9; chondroitin sulfate proteoglycan 4, CSPG4).
The Abundant Histone Chaperones Spt6 and FACT Collaborate to Assemble, Inspect, and Maintain Chromatin Structure in Saccharomyces cerevisiae.
New
Formosa et al., Salt Lake City, United States. In Genetics, Nov 2015
Saccharomyces cerevisiae Spt6 protein is a conserved chromatin factor with several distinct functional domains, including a natively unstructured 30-residue N-terminal region that binds competitively with Spn1 or nucleosomes.
How to find the optimal partner--studies of snurportin 1 interactions with U snRNA 5' TMG-cap analogues containing modified 2-amino group of 7-methylguanosine.
New
Jankowska-Anyszka et al., Warsaw, Poland. In Bioorg Med Chem, Sep 2015
Snurportin 1 is an adaptor protein that mediates the active nuclear import of uridine-rich small nuclear RNAs (U snRNA) by the importin-β receptor pathway.
[Comparative observation of diffuse radiation in Qianyanzhou during the spring of 2012].
New
Li et al., In Ying Yong Sheng Tai Xue Bao, Mar 2015
Global radiation and diffuse radiation were measured from March to June of 2012 in Qianyanzhou Experimental Station of Red Soil and Hilly Land, Chinese Academy of Sciences by ising three types of pyranometers, including CMP11 attached with a shadow ring, SPN1 and RSR3, which were placed in parallel.
Necrotrophic effector-triggered susceptibility (NETS) underlies the barley-Pyrenophora teres f. teres interaction specific to chromosome 6H.
New
Friesen et al., Fargo, United States. In Mol Plant Pathol, Feb 2015
Using a barley recombinant inbred line (RIL) population developed from a cross between the sensitive/susceptible line Hector and the insensitive/resistant line NDB 112 (HN population), sensitivity to PttNE1, which we have named SPN1, mapped to a common resistance/susceptibility region on barley chromosome 6H.
Towards novel efficient and stable nuclear import signals: synthesis and properties of trimethylguanosine cap analogs modified within the 5',5'-triphosphate bridge.
Jemielity et al., Warsaw, Poland. In Org Biomol Chem, 2015
The import is mediated by recognition of the TMG cap by the snRNA transporting protein, snurportin1.
Sphaerochaeta multiformis sp. nov., an anaerobic, psychrophilic bacterium isolated from subseafloor sediment, and emended description of the genus Sphaerochaeta.
Imachi et al., Yokosuka, Japan. In Int J Syst Evol Microbiol, 2014
16S rRNA gene-based phylogenetic analysis showed that strain MO-SPC2(T) was affiliated with the genus Sphaerochaeta within the phylum Spirochaetes, and its closest relatives were Sphaerochaeta pleomorpha Grapes(T) (88.4 % sequence identity), Sphaerochaeta globosa Buddy(T) (86.7 %) and Sphaerochaeta coccoides SPN1(T) (85.4 %).
Septin ring assembly is regulated by Spt20, a structural subunit of the SAGA complex.
Lu et al., Shanghai, China. In J Cell Sci, 2014
In fission yeast (Schizosaccharomyces pombe), Spn1-Spn4 are assembled into a primary septin ring at the division site, and the subsequent recruitment of Mid2 to the structure results in a stable septin ring.
Tolerance of a phage element by Streptococcus pneumoniae leads to a fitness defect during colonization.
Weiser et al., Philadelphia, United States. In J Bacteriol, 2014
Here, we examined a clinical isolate that carries a novel prophage element, designated Spn1, which was detected in both integrated and episomal forms.
Chemical synthesis of U1 snRNA derivatives.
Sekine et al., Yokohama, Japan. In Org Lett, 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.
Identification and characterization of Drosophila Snurportin reveals a role for the import receptor Moleskin/importin-7 in snRNP biogenesis.
Matera et al., Chapel Hill, United States. In Mol Biol Cell, 2013
Snurportin1 (SPN1), the import adaptor, binds to trimethylguanosine (TMG) caps on spliceosomal small nuclear RNAs.
[Cnb1 involved in cytokinesis in Schizosaccharomyces pombe].
Lv et al., Shanghai, China. In Yi Chuan, 2013
Septins include Spn1, Spn2, Spn3, and Spn4.
The transcription factor Spn1 regulates gene expression via a highly conserved novel structural motif.
GeneRIF
Stargell et al., Fort Collins, United States. In J Mol Biol, 2010
Study reports the crystal structure of the conserved central domain of Saccharomyces cerevisiae Spn1; the central domain is composed of 8 alpha-helices in a right-handed superhelical arrangement and exhibits structural similarity to domain I of TFIIS.
Molecular determinants of snurportin 1 ligand affinity and structural response upon binding.
GeneRIF
Grubmüller et al., Göttingen, Germany. In Biophys J, 2009
the binding of dimethylated RNA-caps to snurportin 1
Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP.
Impact
GeneRIF
Ficner et al., Göttingen, Germany. In Science, 2009
study presents the crystal structure of the SPN1.CRM1.RanGTP export complex at 2.5 angstrom resolution (where SPN1 is snurportin1 and RanGTP is guanosine 5' triphosphate-bound Ran
Structural basis for leucine-rich nuclear export signal recognition by CRM1.
Impact
Chook et al., Dallas, United States. In Nature, 2009
Here we present the 2.9 A structure of CRM1 bound to snurportin 1 (SNUPN).
Spn1 regulates the recruitment of Spt6 and the Swi/Snf complex during transcriptional activation by RNA polymerase II.
GeneRIF
Stargell et al., Fort Collins, United States. In Mol Cell Biol, 2008
These findings link Spn1 functions to the transition from an inactive to an actively transcribing RNAPII complex at a postrecruitment-regulated promoter.
Cross-talk between snurportin1 subdomains.
GeneRIF
Matera et al., Cleveland, United States. In Mol Biol Cell, 2005
There is an interaction between the N- and C-terminal domains of SPN, suggesting an autoregulatory function similar to that of importin-alpha.
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