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Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing (By similarity). Additionally we are shipping LSM10 Proteins (4) and and many more products for this protein.
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FLASH plays two roles in 3' end processing of histone pre-mRNAs: It interacts with Lsm11 to form a docking platform for the polyadenylation factors, and it cooperates with SLBP to recruit U7 snRNP to histone pre-mRNA.
Lsm10 and Lsm11, which replace the Sm proteins D1 and D2 in the histone RNA processing U7 snRNPs, associate with pICln in vitro and in vivo without receiving sDMA modifications and with PRMT5 and SMN complexes
The overexpression of Lsm10 and Lsm11 increases the cellular levels of U7 snRNP but has no effect on histone pre-mRNA processing.
The subnuclear organization of histone gene regulatory proteins and 3' end processing factors (NPAT/LSM10) of normal somatic and embryonic stem cells is compromised in selected human cancer cell types.
Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein.
Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing (By similarity). Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed (By similarity). Required for cell cycle progression from G1 to S phases (By similarity). Binds specifically to U7 snRNA (By similarity). Binds specifically to U7 snRNA (By similarity). Binds to the downstream cleavage product (DCP) of histone pre-mRNA.
LSM10, U7 small nuclear RNA associated
, U7 snRNA-associated Sm-like protein LSm10
, U7 snRNP-specific Sm-like protein LSM10