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Validated All-in-One™ qPCR Primer for PCBP1(NM_006196.4) Search again
Powered by BiozBy 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.
Summary
This intronless gene is thought to have been generated by retrotransposition of a fully processed PCBP-2 mRNA. This gene and PCBP-2 have paralogues (PCBP3 and PCBP4) which are thought to have arisen as a result of duplication events of entire genes. The protein encoded by this gene appears to be multifunctional. It along with PCBP-2 and hnRNPK corresponds to the major cellular poly(rC)-binding protein. It contains three K-homologous (KH) domains which may be involved in RNA binding. This encoded protein together with PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promote poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human Papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA.
Gene References into function
- The binding of HuR, CP1, and CP2 to AR mRNA suggests a role for each of these proteins in the post-transcriptional regulation of AR expression in cancer cells.
- PCBP1, a highly homologous isoform of PCBP2, binds to poliovirus stem-loop I with an affinity similar to that of PCBP2
- The 3'-untranslated region of p21WAF1 mRNA is a composite cis-acting sequence bound by RNA-binding proteins from breast cancer cells, including this one.
- HADHB trifunctional enzyme, human renin, and poly(C)-binding protein are novel renin mRNA-binding proteins that target a cis-element in the 3'-UTR of renin mRNA and regulate renin production
- deletion of NLS I from alphaCP1 blocks its nuclear accumulation, whereas NLS I and NLS II must both be inactivated to block nuclear accumulation of alphaCP2
- The interactions of PTB-1 and PCBP1 with their cognate binding sites on the Bag-1 IRES disrupt many of the RNA-RNA interactions, and this creates a largely unstructured region of approximately 40 nucleotides that could permit ribosome binding.
- Kaposi's sarcoma-associated herpesvirus ORF57 binds to PCBP1 as a functional partner for posttranscriptional regulation and is involved in the regulation of the expression of both cellular and viral genes through IRESs.
- hnRNPE1 is a positive effector of collagen synthesis acting at the post-transcriptional level by interaction with the 3'-untranslated regions (3'-UTRs) of COL1A1, 1A2 mRNAs.
- PCBPs act as a transcription factor and positively regulate mu opioid receptor gene expression in NMB cells
- Thus, we did not find evidence for uniquely interacting partner proteins using this approach, but did identify four new lamin A/C interactive partners
- These results are consistent with a model where hnRNP E1 recruited to A2RE RNA granules by binding to hnRNP A2 inhibits translation of A2RE RNA during granule transport.
- To define the mechanism of STAT3C suppression of transcript. and/or translational activity of NF-kappaB we found that a alphaCP-1 interacted with STAT3C. alphaCP-1 is a K-homol. domain-containing RNA-binding prot with specific for C-rich pyrimidine tract
- Signal-dependent and coordinated regulation of transcription, splicing, and translation resides in a single coregulator, PCBP1.
- Specific binding of heterogenous nuclear ribonucleoprotein E1 (hnRNP E1) and U1 small nuclear ribonucleoprotein (snRNP) in the pre-spliceosomal complex was associated with silencing of pseudoexon splicing.
- PCBP1 can function as a cytosolic iron chaperone in the delivery of iron to ferritin
- The detailed transcripts and translatants targeted by PCBP1 at a global level.