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Human SNUPN Protein expressed in Escherichia coli (E. coli) - ABIN667159
Huber, Cronshagen, Kadokura, Marshallsay, Wada, Sekine, Lührmann: Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure. in The EMBO journal 1998
Results show that marker rs218966 in gene PHF14 and rs9836027 in MAP4 (show MAP4 Proteins) significantly associated with hypertension; additionally, rare variants in SNUPN significantly associated with systolic blood pressure.
analysis of interactions between CRM1 and the nuclear pore protein Tpr and snurportin
SPN (show SPN Proteins) construct lacking the importin beta (show KPNB1 Proteins) binding domain (IBB) localizes primarily to the nucleus rather than to the cytoplasm.
There is an interaction between the N- and C-terminal domains of SPN (show SPN Proteins), suggesting an autoregulatory function similar to that of importin-alpha (show KPNA4 Proteins).
study presents the crystal structure of the SPN1 (show SSPN Proteins).CRM1 (show XPO1 Proteins).RanGTP export complex at 2.5 angstrom resolution (where SPN1 (show SSPN Proteins) is snurportin1 and RanGTP is guanosine 5' triphosphate-bound Ran
the binding of dimethylated RNA-caps (show CAPS Proteins) to snurportin 1
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.
RNA, U transporter 1
, snurportin 1
, RNA U transporter 1