Rad1: A Key Component of The DNA Damage Response (G5810)

Target Name: RAD1

NCBI ID: G5810

RAD1

Rad1: A Key Component of The DNA Damage Response

Rad1-like DNA damage checkpoint protein (RAD1) is a protein that plays a critical role in the regulation of DNA replication and repair. It is a key component of the DNA damage response (DDR), which is a series of cellular pathways that respond to DNA damage and ensure the integrity of the genetic material. RAD1 is a protein that is highly conserved across various species and is found in all eukaryotic cells. It is named after its discoverer and research results, Radikolopoff A. Rad1 was first identified in the 1970s and has since been shown to play a crucial role in the regulation of DNA replication, repair, and cell division.

RAD1 is a protein that is composed of two main subunits, a 240-kDa protein and a 160-kDa protein. The 240-kDa protein is the catalytic subunit and is responsible for the chemical reaction that initiates DNA replication. is the structural subunit and plays a structural role in the protein.

RAD1 is highly conserved across various species, with sequence identities of up to 96% between human and mouse RAD1 proteins. It is found in all eukaryotic cells, including muscle, nerve, liver, and leukemia cells. RAD1 is also expressed in various organoids, such as cancer stem cells, and has been shown to play a role in the regulation of cancer cell division and survival.

RAD1 has been shown to play a critical role in the regulation of DNA replication and repair. It is a key component of the DDR and is involved in the checkpoint response to DNA damage. The DDR is a series of cellular pathways that respond to DNA damage and ensure the integrity of the genetic material. The DDR includes several checkpoints, each of which ensures that the damage to the DNA is repaired and the cell is able to continue with its normal function.

The checkpoint response to DNA damage is a critical component of the DDR and is a key factor in ensuring the integrity of the genetic material. It is during the checkpoint response that the cell checks the damage to its DNA and ensures that it is repaired before proceeding with the next step in the cell cycle.

RAD1 is involved in several checkpoints, including the G1 checkpoint, the S-phase checkpoint, and the G2 checkpoint. The G1 checkpoint is the first step in the DDR and is responsible for ensuring that the cell has enough replication material to begin the replication process . The S-phase checkpoint is the second step in the DDR and is responsible for ensuring that the replicated DNA is correctly replicated. The G2 checkpoint is the final step in the DDR and is responsible for ensuring that the cell has enough done DNA before entering the G1 phase again.

RAD1 is also involved in the regulation of DNA repair. DNA repair is a critical process that ensures that the genetic material is maintained in the cell and that any mutations or damage to the DNA is repaired. RAD1 is involved in the regulation of DNA repair by ensuring that the damaged DNA is properly repaired and that the cell is able to continue with its normal function.

In addition to its role in the DDR, RAD1 has also been shown to play a critical role in the regulation of cell division. RAD1 is involved in the regulation of cell cycle progression and is involved in the determination of the length of the cell cycle. It is also involved in the regulation of cell division and is shown to play a role in the regulation of mitosis.

RAD1 has also been shown to have potential as a drug target. The 240-kDa protein subunit of RAD1 has been shown to be a potential drug target in cancer therapy. Studies have shown that inhibiting the activity of the 240-kDa protein subunit of RAD1 can lead to a reduction in

Protein Name: RAD1 Checkpoint DNA Exonuclease

Functions: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:10846170, PubMed:10884395). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:12578958). Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:15871698). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates (PubMed:15314187, PubMed:15556996, PubMed:15871698). The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (PubMed:21659603). Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity (PubMed:9660799)

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