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PABPN1 encodes an abundant nuclear protein that binds with high affinity to nascent poly(A) tails. Additionally we are shipping Poly A Binding Protein Nuclear 1 Antibodies (33) and many more products for this protein.
Showing 6 out of 6 products:
we found a polyadenylation-dependent 3' end maturation pathway for the human telomerase RNA that relies on the nuclear poly(A)-binding protein PABPN1 and the poly(A)-specific RNase PARN (show PARN Proteins).
Many ribozymes were assayed and validated, including four ribozymes targeting the transcript of a disease-causing gene (a mutant version of PABPN1).
Studied if the stability of the RNP (show RNPC3 Proteins) domain of PABPN1 or domain swapping within the RNP (show RNPC3 Proteins) domain may add to fibril formation.
This function is mediated by the concerted actions of the nuclear poly(A) binding protein PABPN1, poly(A) polymerase (PAP (show PAPOLA Proteins)), and the nuclear exosome complex, a pathway we have named PABPN1 and PAP (show REG3A Proteins)-mediated RNA decay (PPD (show HPD Proteins))
These findings demonstrate a role for PABPN1 in rescuing several cytopathological features of TDP-43 (show TARDBP Proteins) proteinopathy by increasing the turnover of pathologic proteins.
PABPN1 inhibits expression of transcripts with pAs (show PASK Proteins) near the transcription start site (TSS (show RPL38 Proteins)), a property possibly related to its role in RNA degradation
this study provided a systematic phosphorylation analysis of the Fanconi anemia protein PALB2 (show PALB2 Proteins), and have revealed important roles of PALB2 (show PALB2 Proteins) Ser (show SIGLEC1 Proteins)-157 and Ser (show SIGLEC1 Proteins)-376 in driving cellular responses to genotoxic stress.
the first step of the cleavage and polyadenylation reaction, mRNA cleavage, is affected in muscles expressing alanine-expanded PABPN1. We propose that impaired cleavage is an early defect in Oculopharyngeal muscular dystrophy.
Data indicate that intron 6 of the poly(A)-binding protein nuclear 1 (PABPN1) gene is required for autoregulation.
The ability of PABPN1 to promote splicing requires its RNA binding and, to a lesser extent, poly(A)polymerase (PAP (show PAPOLA Proteins)) - stimulatory functions.
PABPN1 measures the length of the tail and is responsible for disrupting the CPSF (show CPSF2 Proteins)-poly(A) polymerase (show PAPOLA Proteins) interaction.
PABPN1 interacts with and is stabilized by heat shock protein 90 (show HSP90 Proteins).
These results suggest that PABPN1 levels regulate muscle cell aging and oculopharyngeal muscular dystrophy represents an accelerated muscle aging disorder.
tristetraprolin (show ZFP36 Proteins) inhibits poly(A) tail synthesis by interacting with poly(A)-binding protein nuclear 1 in the nucleus to regulate expression of AU-rich element-containing mRNA
PABPN1 plays an essential role in myoblast proliferation and differentiation, suggesting that it is required for muscle regeneration and maintenance in vivo.
PABPN1 has a role in myogenesis
Poly(A) Binding Protein binds to uridylated oligo(A) tails and determines the length of U-extensions added by URT1.
PAB2 was partially retargeted to the nucleolus in the presence of TuMV VPg-Pro. In addition, the membrane association of PAB2 during TuMV infection resulted from the internalization of the host protein in 6K-VPg-Pro-induced vesicles.
Thus, Hsc70-3 and PABP2 are potentially integral components of the replicase complex and could have important roles to play in the regulation of potyviral RdRp functions.
This gene encodes an abundant nuclear protein that binds with high affinity to nascent poly(A) tails. The protein is required for progressive and efficient polymerization of poly(A) tails at the 3' ends of eukaryotic transcripts and controls the size of the poly(A) tail to about 250 nt. At steady-state, this protein is localized in the nucleus whereas a different poly(A) binding protein is localized in the cytoplasm. This gene contains a GCG trinucleotide repeat at the 5' end of the coding region, and expansion of this repeat from the normal 6 copies to 8-13 copies leads to autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease. Related pseudogenes have been identified on chromosomes 19 and X. Read-through transcription also exists between this gene and the neighboring upstream BCL2-like 2 (BCL2L2) gene.
poly(A) binding protein 2
, poly(A) binding protein II
, polyadenylate-binding protein 2
, nuclear poly(A)-binding protein 1
, poly(A)-binding protein 2
, poly(A)-binding protein II
, polyadenylate-binding nuclear protein 1