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- Table of Contents
Facts about Cell cycle checkpoint control protein RAD9A.
Acts then as a sliding clamp platform on DNA for many proteins involved in long-patch base excision repair (LP-BER). 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 different sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates.
Human | |
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Gene Name: | RAD9A |
Uniprot: | Q99638 |
Entrez: | 5883 |
Belongs to: |
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rad9 family |
cell cycle checkpoint control protein RAD9A; DNA repair exonuclease rad9 homolog A; EC 3.1.11.2; hRAD9; RAD9 (S. pombe) homolog; RAD9 homolog A (S. pombe); RAD9
Mass (kDA):
42.547 kDA
Human | |
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Location: | 11q13.2 |
Sequence: | 11; NC_000011.10 (67391976..67398412) |
Nucleus.
This article will discuss the best uses for the RAD9A marker in the construction of phylogenetic tree, Evolutionary relationships analysis and Cell cycle checkpoints. This information is universally applicable to scientists all over the world. We will also show you how to use specific species' results. You will be able to use the results of this marker to better understand functions of various proteins that are involved in a cell’s life cycle.
Molecular phylogenetics offers many advantages. The RAD9A marker is a great choice for such studies. It can be used to estimate the age of species and their origins, as well as to reconstruct their relationships in multiple taxonomies. The RAD9A mark is widely used in tree construction. The results show that RAD9A has been found to be a common marker among mammals.
RAD9A has shared homology with a number of protein families, including the Hus1 family and Rad9 families. A generalized sequence profil of the entire S.cerevisiae genome was used to establish homology among these families. One such family is Rad1/Rad1, which is closely related with the Hus1 family. However, there are numerous divergences in the sequences of these proteins, and the study's findings suggest that they may be distantly related.
The Maximum Likelihood method was used in the construction of a phylogenetic Tree based on RPA1 protein sequences. Amino acid sequences were aligned with ClustalW, using the Jones-Taylor-Thornton amino acid substitution model. The analysis included many RPA1 paralogs as well as amino acid sequences. This included two species of plants with a DBD–F deletion. Branches were characterized by their bootstrap values, and their scale reflects the number of amino acid substitutions at each site.
RAD9, RAD24 play a crucial role in DNA damage response. They are required for cell cycle arrest at G1/S or G2/M and for the induction DNA damage-dependent (DDR) response. Both proteins function in close proximity of DNA damage and converge at that point. This mechanism has been extensively studied for identifying cellular processes that regulate DNA damage.
RAD9A (subunit of the nine -one-one checkpoint-clamp) is phosphorylated on Thr292. This phosphorylation activates PoloLike-Kinase1 to trigger a checkpoint like response. RAD9A plays a role in checkpoint activation. However, it also has other roles. For example, it prevents non-homologous ending joining.
Transient arrest caused by DNA damage in the G2/M Phase is the most prominent checkpoint in S. Cerevisiae's cell cycle. UV-induced DNA damage repair is mediated by the RAD9 genes. We found that rad9A knockout and wild-type cells were synchronized in G2/M phases. Interestingly, UV-induced DNA damages repair can also be done by the RAD9A genes.
RAD9 has been shown to play an important role during DNA repair and as a clinical indicator for prostate cancer. Originally identified by radioresistance genes, RAD9 was shown to play a crucial role in prostate carcinoma. It also regulates cell cycle checkpoints and at least five DNA repair pathways. It regulates the levels of the key protein NEIL1.
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