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Validated All-in-One™ qPCR Primer for PABPC1(NM_002568.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
The poly(A)-binding protein (PABP), which is found complexed to the 3-prime poly(A) tail of eukaryotic mRNA, is required for poly(A) shortening and translation initiation. In humans, the PABPs comprise a small nuclear isoform and a conserved gene family that displays at least 3 functional proteins: PABP1 (PABPC1), inducible PABP (iPABP, or PABPC4; MIM 603407), and PABP3 (PABPC3; MIM 604680). In addition, there are at least 4 pseudogenes, PABPCP1 to PABPCP4.[supplied by OMIM].
Gene References into function
- Methylated in vivo by CARM1. Methylated region is mapped.
- Paip1 interacts with poly(A) binding protein through two independent binding motifs.
- PABP1 is a potential substrate in MAPKAP kinase 2-induced mRNA stabilization.
- targeted degradation of PABP contributes to translation inhibition in apoptotic cells
- PABP1 associates with paxillin in order to be efficiently transported from the nucleus to the cytoplasm; this event is necessary for cells to remodel their focal adhesions during cell migration.
- a novel signaling pathway involving MKK-2 and ERK1/2 may down-regulate the activity of PABP and eIF4E by controlling their phosphorylation and compensates for the effect of excess cellular PABP
- In esophageal cancer, reduced expression of PABPC1 was correlated with local tumor progression and poor prognosis after surgery.
- PABP interacts with HHV-8 K10/10.1 protein in infected primary effusion lymphoma (PEL) cell lines.
- poly(A)-binding protein 1 (PABP) as a novel BRCA1-interacting protein.
- Structural study of the A-rich repeats in the 5'-untranslated region of PABP.
- We have further characterized the interaction between PABP and IMP1 with the 3' end of the adenine-rich autoregulatory sequence
- the poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein
- Data show that TOB enhances mRNA deadenylation in vivo, and that interaction with PABPC1 is necessary for TOB's deadenylation-enhancing effect.
- Nonsense-mediated decay-sensitive mRNA can be stabilized by tethering the cytoplasmic poly(A) binding protein 1, PABPC1, at a premature termination codon-proximal position.
- RUBVgp2 capsid protein inhibits genetic translation by sequestration of poly(a)-binding protein
- The results further elucidate complex mechanisms where multiple inherent PABP conformations and protein and RNA interactions both serve to differentially regulate PABP cleavage by 3CD, 3C(pro) and 2A(pro).
- Findings suggest several levels of functional antagonism between TTP and PABP1 that have implications for regulation of unstable mRNAs like TNF.
- poly(A)-binding protein cleavage by poliovirus 3C proteinase inhibits viral internal ribosome entry site-mediated translation
- Basophilic inclusions from patients with adult-onset atypical motor neuron disease were distinctly labeled with the antibodies against poly(A)-binding protein 1, T cell intracellular antigen 1, and ribosomal protein S6.
- We show here that PABP-C1 evicted from eIF4G by NSP3 accumulates in the nucleus of rotavirus-infected cells.
- The authors demonstrate that inhibition of HIV expression by Sam68DeltaC is correlated with a loss of PABP1 binding with no attendant change in polyadenosine tail length of the affected RNAs.
