Target Name: RUVBL1
NCBI ID: G8607
Review Report on RUVBL1 Target / Biomarker Content of Review Report on RUVBL1 Target / Biomarker
RUVBL1
Other Name(s): TIP49A | RuvB like AAA ATPase 1 | RuvB (E coli homolog)-like 1 | NMP238 | PONTIN | epididymis secretory sperm binding protein | ECP54 | RUVB1_HUMAN | TATA binding protein interacting protein 49 kDa | 54 kDa erythrocyte cytosolic protein | RuvB like AAA ATPase 1, transcript variant 1 | TIP60-associated protein 54-alpha | nuclear matrix protein 238 | RuvB-like AAA ATPase | RuvB-like 1 | 49 kDa TBP-interacting protein | Pontin52 | RuvB-like 1 (isoform 1) | RVB1 | TIP49a | TAP54-alpha | Pontin 52 | INO80 complex subunit H | TIP49 | Nuclear matrix protein 238 | ECP-54 | TIH1 | pontin 52 | INO80H | RUVBL1 variant 1 | 49 kDa TATA box-binding protein-interacting protein | NMP 238

Unlocking The Potential of RUVBL1: A G-Coupled Protein with A Unique N-Terminal Region

RUVBL1 (TIP49A) is a protein that is expressed in various tissues throughout the body, including the brain, heart, liver, and kidneys. It is a member of the superfamily of G-coupled proteins, which are a type of transmembrane protein that consists of a catalytic active site and a transmembrane region. RUVBL1 is characterized by its unique N-terminal region, which consists of a short amino acid sequence that is unique among G-coupled proteins.

One of the unique features of RUVBL1 is its ability to form a complex with other proteins, particularly with the protein TIP49A. This complex plays a role in the regulation of a variety of cellular processes, including cell signaling, DNA replication, and metabolism. The The interaction between RUVBL1 and TIP49A is regulated by a variety of factors, including changes in the concentration of the protein in the cell, the presence of certain drugs, and the activity of different signaling pathways.

In addition to its role in cellular signaling, RUVBL1 is also of interest as a potential drug target. The ability of RUVBL1 to form a complex with TIP49A makes it a potential target for small molecules that can modulate the activity of this protein. One of the primary targets for RUVBL1 is the protein p21, which is a hallmark of the T-cell receptor signaling pathway. p21 is a transduction molecule, which can be modified by phosphorylation after activation, and then participate in the cell cycle, DNA replication and other processes. The interaction between RUVBL1 and p21 can affect cell signaling pathways by regulating the phosphorylation status of p21.

Another potential target for RUVBL1 is the protein p53, which is a well-known tumor suppressor protein. P53 is a transcription factor that is responsible for regulating the expression of many genes in the cell. It is also involved in the regulation of cell cycle, DNA replication, and apoptosis. RUVBL1 has been shown to interact with p53 and can modulate its activity. This interaction between RUVBL1 and p53 may have implications for the regulation of cell growth and division.

In addition to its potential as a drug target, RUVBL1 is also of interest as a biomarker. The ability of RUVBL1 to form a complex with TIP49A makes it a potential marker for the treatment of various diseases, including cancer. cancer. RUVBL1 has been shown to be expressed in a variety of cancer tissues and has been used as a biomarker for the diagnosis and progression of various cancers, including breast, lung, and ovarian cancers.

Overall, RUVBL1 is a protein that is of interest as a potential drug target and biomarker. Its unique N-terminal region and ability to form a complex with TIP49A make it a potential target for small molecules. Additionally, its interaction with p21 and p53 suggests that it may be involved in the regulation of cell signaling pathways and cell growth and division. Further research is needed to fully understand the role of RUVBL1 in cellular signaling and its potential as a drug target and biomarker.

Protein Name: RuvB Like AAA ATPase 1

Functions: Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity (PubMed:17157868, PubMed:33205750). Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (PubMed:14966270). This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription (PubMed:14966270). This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (PubMed:14966270). The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage (PubMed:14966270). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (PubMed:24463511). Proposed core component of the chromatin remodeling INO80 complex which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding (PubMed:16230350, PubMed:21303910). Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex (PubMed:10882073, PubMed:16014379). Essential for cell proliferation (PubMed:14506706). May be able to bind plasminogen at cell surface and enhance plasminogen activation (PubMed:11027681)

The "RUVBL1 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 RUVBL1 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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