Target Name: RNF168
NCBI ID: G165918
Review Report on RNF168 Target / Biomarker Content of Review Report on RNF168 Target / Biomarker
RNF168
Other Name(s): Ring finger protein 168 | RN168_HUMAN | RIDL | ring finger protein 168 | RING finger protein 168 | E3 ubiquitin-protein ligase RNF168 | ring finger protein 168, E3 ubiquitin protein ligase | RING-type E3 ubiquitin transferase RNF168 | hRNF168

RNF168: A Drug Target / Disease Biomarker

RNA-Fucosin (RF168) is a drug target and biomarker that is derived from the RNA-protein complex that is present in the endoplasmic reticulum (ER) of all cells. It is a 22 kDa protein that is composed of two subunits, RF1 and RF2. RF1 is a 19 kDa protein that consists of a cytoplasmic domain, a transmembrane domain, and a C-terminal domain that contains a fucose molecule, while RF2 is a 2 kDa protein that consists of a cytoplasmic domain and a transmembrane domain.

The RNA-protein complex that is present in the ER is involved in the regulation of various cellular processes, including protein synthesis, DNA replication, and cell signaling. It is thought to play a role in the regulation of cellular processes that are dependent on the endoplasmic reticulum, such as the biosynthesis of proteins that are involved in cell signaling pathways.

One of the functions of RF168 is its ability to interact with other proteins that are present in the ER. This interaction with other proteins is thought to be important for the regulation of cellular processes that are dependent on the ER. For example, RF168 has been shown to interact with the protein known as TRIM22, which is involved in the regulation of DNA replication. This interaction between RF168 and TRIM22 is thought to be important for the regulation of the DNA replication process.

Another function of RF168 is its ability to modulate the activity of other proteins that are present in the ER. This modulation of protein activity is thought to be important for the regulation of cellular processes that are dependent on the ER. For example, RF168 has been shown to inhibit the activity of the protein known as p16INK4a, which is involved in cell signaling pathways. This inhibition of p16INK4a activity is thought to be important for the regulation of cellular processes that are dependent on the ER.

RF168 is also thought to play a role in the regulation of cellular processes that are dependent on the endoplasmic reticulum. This includes the regulation of protein synthesis, DNA replication, and cell signaling. It is also thought to be involved in the regulation of cellular processes that are dependent on the ER, such as the regulation of the transport of proteins into the ER.

In conclusion, RNA-Fucosin (RF168) is a drug target and biomarker that is derived from the RNA-protein complex that is present in the endoplasmic reticulum of all cells. It is a 22 kDa protein that is composed of two subunits, RF1 and RF2. RF1 is a 19 kDa protein that consists of a cytoplasmic domain, a transmembrane domain, and a C-terminal domain that contains a fucose molecule, while RF2 is a 2 kDa protein that consists of a cytoplasmic domain and a transmembrane domain. The interaction between RF168 and other proteins that are present in the ER is thought to be important for the regulation of various cellular processes, including protein synthesis, DNA replication, and cell signaling. Further research is needed to fully understand the role of RF168 in cellular processes.

Protein Name: Ring Finger Protein 168

Functions: E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively)

The "RNF168 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 RNF168 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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