Target Name: CPEB1
NCBI ID: G64506
Review Report on CPEB1 Target / Biomarker Content of Review Report on CPEB1 Target / Biomarker
CPEB1
Other Name(s): CPE-binding protein 1 | CPEB1 variant 1 | h-CPEB | CPEB-1 | Cytoplasmic polyadenylation element binding protein 1, transcript variant 1 | Cytoplasmic polyadenylation element-binding protein 1 (isoform 1) | FLJ13203 | h-CEBP | hCPEB-1 | cytoplasmic polyadenylation element binding protein 1 | MGC34136 | CPE-BP1 | CPEB1_HUMAN | CPEB | MGC60106 | CEBP | Cytoplasmic polyadenylation element-binding protein 1

Identification and Characterization of CPEB1, A Potential Drug Target and Biomarker

CPEB1 (CPEB1-protein) is a protein that is expressed in various tissues throughout the body, including the brain, heart, and kidneys. It is a member of the CPEB family of proteins, which are known for their role in intracellular signaling. One of the unique features of CPEB1 is its ability to interact with the protein tyrosine phosphatase (PTP) gene, which is a key regulator of protein tyrosination and degradation. This interaction between CPEB1 and PTP has important implications for the regulation of cellular signaling pathways, and suggests that CPEB1 may be a potential drug target or biomarker.

The CPEB family of proteins was identified through the analysis of expressed sequence data from genomic libraries. These proteins share a conserved catalytic core and a common N-terminus, but differ in their length and sequence. CPEB1 is a 14-kDa protein that contains 115 amino acid residues. It has a distinct N-terminus that includes a 24 amino acid residue region that is involved in interactions with PTP. This region is known as the N-terminal hypervariable region (HVR) and is a feature that is unique to CPEB1.

CPEB1 is a potent inhibitor of PTP, a protein that plays a critical role in the regulation of intracellular signaling pathways. PTP is a highly conserved protein that is involved in the regulation of protein tyrosination and degradation, and is a key regulator of many cellular signaling pathways, including the T cell receptor (TCR) signaling pathway. CPEB1 has been shown to inhibit the tyrosination and phosphorylation of PTP, which is consistent with its role as an inhibitor of PTP.

The ability of CPEB1 to interact with PTP is important for its function in intracellular signaling pathways. CPEB1 has been shown to play a role in the regulation of cellular processes such as cell growth, apoptosis, and inflammation. For example, CPEB1 has been shown to be involved in the regulation of cell cycle progression, and has been shown to interact with the cyclin D1 protein. Additionally, CPEB1 has been shown to be involved in the regulation of apoptosis, and has been shown to interact with the protein Bcl-2.

CPEB1 has also been shown to play a role in the regulation of inflammation. CPEB1 has been shown to interact with the transcription factor NF-kappa-B, and has been shown to be involved in the regulation of inflammation. For example, CPEB1 has been shown to be involved in the regulation of the chemokine production pathway, and has been shown to interact with the protein STAT3.

CPEB1 is also a good candidate as a drug target, as it has been shown to have a unique structure and a unique function. CPEB1 is a small protein that is expressed in various tissues throughout the body, and its unique structure and function make it an attractive target for drug development. Additionally, CPEB1 has been shown to have a unique mechanism of inhibition of PTP, which may make it a more stable drug target than other proteins that are known to interact with PTP.

In conclusion, CPEB1 is a unique protein that is involved in the regulation of intracellular signaling pathways. Its ability to interact with PTP and its unique structure and function make it an attractive candidate for drug development. Further studies are needed to fully understand the role of CPEB1 in cellular signaling pathways and its potential as a drug target.

Protein Name: Cytoplasmic Polyadenylation Element Binding Protein 1

Functions: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism (PubMed:24990967). In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses (By similarity). Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation (By similarity). Induces the assembly of stress granules in the absence of stress. Required for cell cycle progression, specifically for prophase entry (PubMed:26398195)

The "CPEB1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about CPEB1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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CPEB1-AS1 | CPEB2 | CPEB2-DT | CPEB3 | CPEB4 | CPED1 | CPHL1P | CPLANE1 | CPLANE2 | CPLX1 | CPLX2 | CPLX3 | CPLX4 | CPM | CPN1 | CPN2 | CPNE1 | CPNE2 | CPNE3 | CPNE4 | CPNE5 | CPNE6 | CPNE7 | CPNE8 | CPNE9 | CPOX | CPPED1 | CPQ | CPS1 | CPS1-IT1 | CPSF1 | CPSF1P1 | CPSF2 | CPSF3 | CPSF4 | CPSF4L | CPSF6 | CPSF7 | CPT1A | CPT1B | CPT1C | CPT2 | CPTP | CPVL | CPVL-AS2 | CPXCR1 | CPXM1 | CPXM2 | CPZ | CR1 | CR1L | CR2 | CRABP1 | CRABP2 | CRACD | CRACDL | CRACR2A | CRACR2B | CRADD | CRADD-AS1 | CRAMP1 | CRAT | CRAT37 | CRB1 | CRB2 | CRB3 | CRBN | CRCP | CRCT1 | Creatine Kinase | CREB1 | CREB3 | CREB3L1 | CREB3L2 | CREB3L3 | CREB3L4 | CREB5 | CREBBP | CREBL2 | CREBRF | CREBZF | CREG1 | CREG2 | CRELD1 | CRELD2 | CREM | CRH | CRHBP | CRHR1 | CRHR2 | CRIM1 | CRIM1-DT | CRIP1 | CRIP1P1 | CRIP2 | CRIP3 | CRIPAK | CRIPT | CRISP1 | CRISP2