HCSGD entry for CPEB1
1. General information
| Official gene symbol | CPEB1 |
|---|---|
| Entrez ID | 64506 |
| Gene full name | cytoplasmic polyadenylation element binding protein 1 |
| Other gene symbols | CEBP CPE-BP1 CPEB |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
This gene isn't in PPI subnetwork.
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0000166 | Nucleotide binding | IEA | molecular_function |
| GO:0000900 | Translation repressor activity, nucleic acid binding | ISS | molecular_function |
| GO:0000932 | Cytoplasmic mRNA processing body | IEA | cellular_component |
| GO:0003676 | Nucleic acid binding | IEA | molecular_function |
| GO:0005634 | Nucleus | ISS | cellular_component |
| GO:0005737 | Cytoplasm | ISS | cellular_component |
| GO:0006397 | MRNA processing | IEA | biological_process |
| GO:0014069 | Postsynaptic density | IEA | cellular_component |
| GO:0030054 | Cell junction | IEA | cellular_component |
| GO:0030425 | Dendrite | IEA | cellular_component |
| GO:0032869 | Cellular response to insulin stimulus | IDA | biological_process |
| GO:0035925 | MRNA 3'-UTR AU-rich region binding | ISS | molecular_function |
| GO:0045211 | Postsynaptic membrane | IEA | cellular_component |
| GO:0046872 | Metal ion binding | IEA | molecular_function |
| GO:0071230 | Cellular response to amino acid stimulus | ISS | biological_process |
| GO:0071456 | Cellular response to hypoxia | IDA | biological_process |
| GO:2000766 | Negative regulation of cytoplasmic translation | IMP | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.0294073667 | 0.9700846662 | 0.3973587179 | 1.0000000000 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
| Data source | Up or down | Log fold change |
|---|---|---|
| GSE11954 | Up | 0.9212411569 |
| GSE13712_SHEAR | Up | 0.1232134745 |
| GSE13712_STATIC | Up | 0.0413398746 |
| GSE19018 | Up | 0.1644548145 |
| GSE19899_A1 | Up | 0.2723537497 |
| GSE19899_A2 | Down | -0.0436090682 |
| PubMed_21979375_A1 | Up | 0.3350193231 |
| PubMed_21979375_A2 | Down | -0.0741691645 |
| GSE35957 | Down | -0.4776537650 |
| GSE36640 | Down | -0.3035589227 |
| GSE54402 | Up | 0.5313437410 |
| GSE9593 | Up | 1.0124352951 |
| GSE43922 | Up | 0.1456011412 |
| GSE24585 | Down | -0.0650836357 |
| GSE37065 | Up | 0.3283524155 |
| GSE28863_A1 | Up | 0.1754294428 |
| GSE28863_A2 | Up | 0.6029696537 |
| GSE28863_A3 | Up | 0.1145627570 |
| GSE28863_A4 | Up | 0.0013464165 |
| GSE48662 | Up | 0.0488153288 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Not regulated by drugs
- MicroRNAs
- mirTarBase
No target information from mirTarBase
- mirTarBase
- mirRecord
No target information from mirRecord
- mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 10 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 26915047 | As this site is highly conserved between the CPEB family members, we suggest the existence of a splicing-based regulatory mechanism of CPEB function, and describe a robust phosphospecific antibody to study it in future |
| 25483308 | Cytoplasmic polyadenylation element binding (CPEB) proteins are translational regulators that are involved in the control of cellular senescence, synaptic plasticity, learning, and memory |
| 25483308 | In primary hippocampal cultures, the subcellular localization of CPEB2 in neurons and astrocytes resembled that of CPEB1 |
| 25483308 | Electrophoretic mobility shift assay and RNA coimmunoprecipitation revealed CPEB2 interaction with beta-catenin and Ca(2+) /calmodulin-dependent protein kinase II (both established CPEB1 targets), indicating an overlap in RNA binding specificity between CPEB1 and CPEB2 |
| 25483308 | In conclusion, our study identifies CPEB2 splice variants to be differentially expressed among individual cells and across cell types of the mouse hippocampus, and reveals overlapping binding specificity between CPEB2 and CPEB1 |
| 23788032 | CPEB1, a histone-modified hypomethylated gene, is regulated by miR-101 and involved in cell senescence in glioma |
| 23788032 | We certified that the mRNA translation-related gene cytoplasmic polyadenylation element-binding protein 1 (CPEB1) is hypomethylated and overexpressed in glioma cells and tissues |
| 23788032 | CPEB1 is also regulated directly by the tumor suppressor miR-101, a potential marker of glioma |
| 23788032 | We demonstrated that miR-101 downregulated the expression of CPEB1 through reversing the methylation status of the CPEB1 promoter by regulating the presence on the promoter of the methylation-related histones H3K4me2, H3K27me3, H3K9me3 and H4K20me3 |
| 23788032 | The epigenetic regulation of H3K27me3 on CPEB1 promoter is mediated by EZH2 and EED |
| 23788032 | Furthermore, the downregulation of CPEB1 induced senescence in a p53-dependent manner |
| 22253608 | The cytoplasmic polyadenylation element binding protein CPEB1 (CPEB) regulates germ cell development, synaptic plasticity, and cellular senescence |
| 22253608 | A microarray analysis of mRNAs regulated by CPEB unexpectedly showed that several encoded proteins are involved in insulin signaling |
| 22253608 | An investigation of Cpeb1 knockout mice revealed that the expression of two particular negative regulators of insulin action, PTEN and Stat3, were aberrantly increased |
| 22253608 | Indeed, when the Cpeb1 knockout mice were fed a high-fat diet, their livers became insulin-resistant |
| 22253608 | Analysis of HepG2 cells, a human liver cell line, depleted of CPEB demonstrated that this protein directly regulates the translation of PTEN and Stat3 mRNAs |
| 22253608 | Our results show that CPEB regulated translation is a key process involved in insulin signaling |
| 21536657 | CPEB control of NF-kappaB nuclear localization and interleukin-6 production mediates cellular senescence |
| 21536657 | CPEB is a sequence-specific translational regulatory RNA binding protein that mediates cellular senescence in primary mouse and human cells |
| 21536657 | CPEB knockout mouse embryo fibroblasts (MEFs) bypass senescence and synthesize large amounts of interleukin-6 (IL-6) and many other cytokines, which is not the case with either wild-type MEFs immortalized by prolonged culture or p53-deficient MEFs |
| 21536657 | CPEB regulates the production of IL-6 at both the translational and transcriptional levels; in CPEB-depleted cells, aberrant IL-6 transcription is mediated by improper NF-kappaB p65 phosphorylation and nuclear localization |
| 21536657 | IL-6-promoted entry into senescence requires p53; CPEB knockout MEFs, however, synthesize only approximately 50% of the p53 of wild-type MEFs, which is insufficient to respond to IL-6 |
| 21536657 | Thus, CPEB deficiency not only increases IL-6 production but also renders the cell incapable of a senescence-promoting response |
| 21478871 | CPEB and two poly(A) polymerases control miR-122 stability and p53 mRNA translation |
| 21478871 | The cytoplasmic polyadenylation element binding protein (CPEB) promotes polyadenylation by nucleating a group of factors including defective in germline development 2 (Gld2), a non-canonical poly(A) polymerase, on specific messenger RNA (mRNA) 3' untranslated regions (UTRs) |
| 21478871 | Because CPEB regulation of p53 mRNA polyadenylation/translation is necessary for cellular senescence in primary human diploid fibroblasts, we surmised that Gld2 would be the enzyme responsible for poly(A) addition |
| 21478871 | Here we show that depletion of Gld2 surprisingly promotes rather than inhibits p53 mRNA polyadenylation/translation, induces premature senescence and enhances the stability of CPEB mRNA |
| 20040591 | The nuclear experience of CPEB: implications for RNA processing and translational control |
| 20040591 | CPEB is a sequence-specific RNA binding protein that promotes polyadenylation-induced translation in early development, during cell cycle progression and cellular senescence, and following neuronal synapse stimulation |
| 20040591 | Here, we report that CPEB shuttles between the nucleus and cytoplasm and that its export occurs via the CRM1-dependent pathway |
| 20040591 | CPEB also interacts with Maskin in the nucleus as well as with CPE-containing mRNAs |
| 20040591 | Moreover, CPEB directly or indirectly mediates the alternative splicing of at least one pre-mRNA in mouse embryo fibroblasts as well as certain mouse tissues |
| 20040591 | We propose that CPEB, together with Maskin, binds mRNA in the nucleus to ensure tight translational repression upon export to the cytoplasm |
| 20040591 | In addition, we propose that nuclear CPEB regulates specific pre-mRNA alternative splicing |
| 19141477 | CPEB regulation of human cellular senescence, energy metabolism, and p53 mRNA translation |
| 19141477 | Cytoplasmic polyadenylation element-binding protein (CPEB) stimulates polyadenylation and translation in germ cells and neurons |
| 19141477 | Knockdown of CPEB causes skin and lung cells to bypass the M1 crisis stage of senescence; reintroduction of CPEB into the knockdown cells restores a senescence-like phenotype |
| 19141477 | Surprisingly, knockdown of exogenous CPEB that induced a senescence-like phenotype results in the resumption of cell growth |
| 19141477 | Together, these results suggest that CPEB controls senescence and bioenergetics in human cells at least in part by modulating p53 mRNA polyadenylation-induced translation |
| 17481902 | CPEB: a life in translation |
| 17481902 | This cytoplasmic polyadenylation element (CPE) is the binding platform for CPE-binding protein (CPEB), which promotes polyadenylation-induced translation |
| 17481902 | Since then, the biochemistry and biology of CPEB has grown rather substantially: mechanistically, CPEB nucleates a complex of factors that regulates poly(A) elongation through, of all things, a deadenylating enzyme; biologically, CPEB mediates many processes including germ-cell development, cell division and cellular senescence, and synaptic plasticity and learning and memory |
| 17481902 | These observations underscore the growing complexities of CPEB involvement in cell function |
| 17015432 | Control of cellular senescence by CPEB |
| 17015432 | Cytoplasmic polyadenylation element-binding protein (CPEB) is a sequence-specific RNA-binding protein that promotes polyadenylation-induced translation |
| 17015432 | While a CPEB knockout (KO) mouse is sterile but overtly normal, embryo fibroblasts derived from this mouse (MEFs) do not enter senescence in culture as do wild-type MEFs, but instead are immortal |
| 17015432 | Exogenous CPEB restores senescence in the KO MEFs and also induces precocious senescence in wild-type MEFs |
| 17015432 | CPEB cannot stimulate senescence in MEFs lacking the tumor suppressors p53, p19ARF, or p16(INK4A); however, the mRNAs encoding these proteins are unlikely targets of CPEB since their expression is the same in wild-type and KO MEFs |
| 17015432 | Conversely, Ras cannot induce senescence in MEFs lacking CPEB, suggesting that it may lie upstream of CPEB |
| 17015432 | One target of CPEB regulation is myc mRNA, whose unregulated translation in the KO MEFs may cause them to bypass senescence |
| 17015432 | Thus, CPEB appears to act as a translational repressor protein to control myc translation and resulting cellular senescence |
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