Target Name: ELL2
NCBI ID: G22936
Review Report on ELL2 Target / Biomarker Content of Review Report on ELL2 Target / Biomarker
ELL2
Other Name(s): MRCCAT1 | metastatic renal cell carcinoma-associated transcript 1 | elongation factor RNA for polymerase II 2 | ELL-related RNA polymerase II, elongation factor | RNA polymerase II elongation factor ELL2 | elongation factor, RNA polymerase II, 2 | Elongation factor for RNA polymerase II 2 | ELL2_HUMAN | elongation factor for RNA polymerase II 2

LLL2: A Metal-Responsive CAMP-Activated Protein as A Potential Drug Target and Biomarker for Various Diseases

ELL2 (MRCAT1), a protein that belongs to the metal responsive cAMP-activated protein (MRP) family, has been identified as a potential drug target and biomarker for various diseases, including cancer, neurodegenerative diseases, and metabolic disorders. Its unique function as a cAMP-activated protein, which can be regulated by metal ions, makes it an attractive target for small molecules that can modulate its activity. In this article, we will discuss the current research on ELL2 and its potential as a drug target, as well as its potential as a biomarker for various diseases.

The MRP family is a family of transcription factors that play a crucial role in the regulation of gene expression. These proteins are characterized by the presence of a metal-responsive cAMP-activated domain, which is responsible for their unique transcription activity. The first member of the MRP family was identified in the 1970s, and since then, many more members have been identified, each with unique functions and mechanisms of action.

LL2 is a member of the MRP family and is a protein that can be regulated by metal ions. It is composed of 21 amino acid residues and has a calculated molecular weight of 19.4 kDa. LLL2 is highly conserved and has a single known function, which is to regulate gene expression in various cell types, including muscle, nerve, and heart cells.

Functional assays have shown that LLL2 can be regulated by metal ions, such as EGTA, a protein that is commonly found in cell signaling pathways. When EGTA binds to LLL2, it causes a conformational change that results in a shift of its activity center. This conformational change allows LLL2 to interact with specific DNA sequences and modulate gene expression.

LL2 has been shown to play a role in various cellular processes, including cell signaling, DNA replication, and metabolism. It has been shown to interact with various protein partners, including transcription factors, DNA-binding proteins, and metabolic enzymes.

As a drug target, LLL2 is an attractive target due to its unique function as a cAMP-activated protein. The cAMP-activated protein pathway is a well-established signaling pathway that plays a crucial role in various cellular processes, including cell signaling, DNA replication, and metabolism. Therefore, modulating the activity of LLL2 by small molecules could have a significant impact on cellular processes and potentially lead to the development of new treatments for various diseases.

In addition to its potential as a drug target, LLL2 has also been shown to be a potential biomarker for various diseases. The detection and quantification of gene expression is an important step in the analysis of diseases, and LLL2 has been shown to be a useful biomarker for several diseases, including cancer, neurodegenerative diseases, and metabolic disorders.

In cancer, LLL2 has been shown to play a role in various cellular processes, including cell signaling, DNA replication, and apoptosis. Several studies have shown that LLL2 is involved in the regulation of cell proliferation, and that its activity can be modulated by various therapeutic agents. Therefore, LLL2 may be a useful target for cancer therapies that aim to inhibit cell proliferation or promote cell apoptosis.

In neurodegenerative diseases, LLL2 has been shown to play a role in the regulation of cellular processes, including cell signaling and neurotransmission. Several studies have shown that LLL2 is involved in the regulation of neurotransmitter release from neurons, and that its activity can be modulated by various therapeutic agents. Therefore, LLL2 may be a useful target for neurodegenerative diseases therapies that aim to modulate neurotransmission.

In metabolic disorders, LLL2 has been shown to play a role in

Protein Name: Elongation Factor For RNA Polymerase II 2

Functions: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane-specific to secretory IgH mRNA expression

The "ELL2 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 ELL2 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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ELL2P1 | ELL3 | ELMO1 | ELMO2 | ELMO3 | ELMOD1 | ELMOD2 | ELMOD3 | ELN | ELOA | ELOA-AS1 | ELOA2 | ELOA3BP | ELOA3DP | ELOA3P | ELOB | ELOC | ELOF1 | Elongation Factor 1 Complex | Elongation of very long chain fatty acids protein | Elongin (SIII) complex | ELOVL1 | ELOVL2 | ELOVL2-AS1 | ELOVL3 | ELOVL4 | ELOVL5 | ELOVL6 | ELOVL7 | ELP1 | ELP2 | ELP3 | ELP4 | ELP5 | ELP6 | ELSPBP1 | EMB | EMBP1 | EMC1 | EMC1-AS1 | EMC10 | EMC2 | EMC3 | EMC3-AS1 | EMC4 | EMC6 | EMC7 | EMC8 | EMC9 | EMCN | EMD | EME1 | EME2 | EMG1 | EMID1 | EMILIN1 | EMILIN2 | EML1 | EML2 | EML2-AS1 | EML3 | EML4 | EML4-AS1 | EML5 | EML6 | EMP1 | EMP2 | EMP2P1 | EMP3 | EMSLR | EMSY | EMX1 | EMX2 | EMX2OS | EN1 | EN2 | ENAH | ENAM | ENC1 | ENDOD1 | ENDOG | Endogenous Retrovirus group K Env polyprotein (ERVK) | Endogenous retrovirus group K member 25 Pol protein-like, transcript variant X1 | EndoGlyx-1 | Endoplasmic reticulum collagen prolyl 3-hydroxylation complex | Endothelin receptor | Endothelin-Converting Enzymes (ECE) | Endothiapepsin | ENDOU | ENDOV | ENG | ENGASE | ENHO | ENKD1 | ENKUR | ENO1 | ENO1-AS1 | ENO1P1 | ENO1P4 | ENO2