Target Name: EGFEM1P
NCBI ID: G93556
Review Report on EGFEM1P Target / Biomarker Content of Review Report on EGFEM1P Target / Biomarker
EGFEM1P
Other Name(s): EGF like and EMI domain containing 1, pseudogene | NCRNA00259 | C3orf50

EGFEM1P: A Potential Drug Target and Biomarker

The endoplasmic reticulum (ER) is a protein synthesis and quality control center for the cell that retrieves and modifies proteins before they are released for further processing or degradation. One of the key proteins that are targeted by drugs in the field of nuclear medicine is EGFEM1P (EGF-like and EMI domain containing 1), also known as P191G2. This protein is a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

Structure and Function

EGFEM1P is a 21-kDa protein that is expressed in most tissues of the body, including the brain, heart, liver, and muscle. It is localized to the ER and has a nuclear localization signal in the cytoplasm. EGFEM1P has a unique structure that includes an N-terminal transmembrane domain, a coiled-coil domain, and a C-terminal extracellular domain with a glycophosphorylated cysteine 鈥嬧?媟esidue.

The EGFEM1P gene is located on chromosome 18q21 and has four exons. The protein is made up of 151 amino acids, with a calculated pI of 11.99. EGFEM1P has a molecular weight of 19.1 kDa and a calculatedMr of 21 kDa.

Expression and localization

EGFEM1P is highly expressed in most tissues of the body, including the brain, heart, liver, and muscle. It is expressed at levels of up to 10% of total cell protein in each of these tissues. The protein is mainly localized to the ER and has a nuclear localization signal in the cytoplasm.

EGFEM1P has been shown to localize to the endoplasmic reticulum (ER) and the nuclear envelope (NE) in various cell types. The ER is a protein synthesis and quality control center that retrieves and modifies proteins before they are released for further processing or degradation. The NE is the double membrane structure that surrounds the ER and is involved in the regulation of gene expression.

The nuclear localization signal in the cytoplasm is thought to play a role in the nuclear import of EGFEM1P. This signal is present in the cytoplasm and is recognized by nuclear import factors, which transport the protein into the nucleus. The nuclear import of EGFEM1P is also thought to be regulated by the transmembrane protein, TRIM-30.

EGFEM1P functions

EGFEM1P has been shown to play a role in various cellular processes, including cell signaling, cell adhesion, and neurotransmission.

EGFEM1P is a component of the Shc-associated protein complex (SAPC), which is a network of proteins that play a role in cell signaling and cell adhesion. The SAPC includes EGFEM1P, which interacts with the protein known as Shc, also known as S /TIM-3.

EGFEM1P is also involved in neurotransmission, specifically in the regulation of neurotransmitter release from dendrites of neurons. EGFEM1P has been shown to interact with the neurotransmitter acetylcholine (ACh) and modulate its release.

EGFEM1P has also been shown to play a role in cell proliferation and survival. EGFEM1P has been shown to be involved in the regulation of cell cycle progression, cell growth, and apoptosis.

Drug targeting

EGFEM1P is a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

In

Protein Name: EGF Like And EMI Domain Containing 1, Pseudogene

The "EGFEM1P 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 EGFEM1P 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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