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NCBP2 is not required for cell viability and poly(A) RNA export.
A novel alternative splice variant of CBP20, termed CBP20S, has an in-frame deletion, leading to the translation of a protein lacking most of the RNA recognition motif (RRM).
crystal structure at 2.1 A resolution of CBP20 and CBP80 (show NCBP1 Proteins) bound to an m(7)GpppG cap analogue
Structural basis of m7GpppG binding to the nuclear cap-binding protein (show EIF4E Proteins) complex.
We show that NELF (show NELF Proteins) interacts with the nuclear cap binding complex (CBC), a heterodimeric, multifunctional factor that plays important roles in several mRNA processing steps, and the two factors together participate in the 3' end processing of histone mRNAs
a new MIF4G domain-containing protein (show MIF4GD Proteins), CTIF (CBP80/20-dependent translation initiation factor (show KIAA0427 Proteins)) that interacts directly with CBP80 (show NCBP1 Proteins) and is part of the CBP80 (show NCBP1 Proteins)/20-dependent translation initiation complex
determined how importin-beta (show KPNB1 Proteins) binds to the cap-binding complex (CBC) through its CBP20 subunit
we proposed that ethylene regulated phosphorylation of CBP20 is involved in the root growth and one pathway is through the regulation of miR319b and its target MYB33 in roots
Data suggest that CBP20 and CBP80 (ABH1) have synergistic roles during the salt stress response.
SERRATE, CAP BINDING PROTEIN20 (CBP20), and CBP80 (show NCBP1 Proteins) are regulators of lincRNA expression and biogenesis. RT-PCR experiments confirmed these three proteins are also needed for splicing of a small group of intron-containing lincRNAs.
Some hitherto undescribed changes were found in the tissue structure and epidermal morphology of cbp20 mutant
The cbp80(abh1) and cbp20/80 mutants had many more changes in alternative splicing in common than did cbp20 and cbp20/80 suggesting that CBP80 (show NCBP1 Proteins) plays a more significant role in alternative splicing than CBP20.
CBP20 and CBP80 function in miRNA biogenesis by binding to pri-miRNA transcripts, and are stabilized by ABA by a post-translational mechanism.
The N-terminal part of AtCBP20 is crucial for the formation of a complex with AtCBP80.
The product of this gene is a component of the nuclear cap-binding protein complex (CBC), which binds to the monomethylated 5' cap of nascent pre-mRNA in the nucleoplasm. The encoded protein has an RNP domain commonly found in RNA binding proteins, and contains the cap-binding activity. The CBC promotes pre-mRNA splicing, 3'-end processing, RNA nuclear export, and nonsense-mediated mRNA decay. Multiple transcript variants encoding different isoforms have been found for this gene.
, 20 kDa nuclear cap-binding protein
, NCBP 20 kDa subunit
, nuclear cap binding protein subunit 2, 20kDa
, nuclear cap-binding protein subunit 2
, nuclear cap binding protein subunit 2, 20kD
, NCBP interacting protein 1
, NCBP-interacting protein 1
, cell proliferation-inducing gene 55 protein