RAD9A

From Wikipedia, the free encyclopedia

RAD9 homolog A (S. pombe)

Identifiers

External IDs

OMIM: 603761 MGI: 1328356 HomoloGene: 32118

Gene ontology
Molecular Function:	• protein binding • 3'-5' exonuclease activity • exodeoxyribonuclease III activity • hydrolase activity • SH3 domain binding • protein kinase binding • histone deacetylase binding
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• cell cycle checkpoint • DNA replication checkpoint • DNA damage checkpoint • DNA repair • positive regulation of apoptosis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004584 (mRNA)
NP_004575 (protein)

NM_011237 (mRNA)
NP_035367 (protein)

Location

Chr 11: 66.92 - 66.92 Mb

Chr 19: 4.2 - 4.2 Mb

Pubmed search

[1]

[2]

RAD9 homolog A (S. pombe), also known as RAD9A, is a human gene.

This gene product is highly similar to Schizosaccharomyces pombe rad9, a cell cycle checkpoint protein required for cell cycle arrest and DNA damage repair in response to DNA damage. This protein is found to possess 3' to 5' exonuclease activity, which may contribute to its role in sensing and repairing DNA damage. It forms a checkpoint protein complex with RAD1 and HUS1. This complex is recruited by checkpoint protein RAD17 to the sites of DNA damage, which is thought to be important for triggering the checkpoint-signaling cascade. Use of alternative polyA sites has been noted for this gene.^[1]

[edit] References

^ Entrez Gene: RAD9A RAD9 homolog A (S. pombe).

[edit] Further reading

Lieberman HB (2006). "Rad9, an evolutionarily conserved gene with multiple functions for preserving genomic integrity.". J. Cell. Biochem. 97 (4): 690–7. doi:10.1002/jcb.20759. PMID 16365875.
Lieberman HB, Hopkins KM, Nass M, et al. (1997). "A human homolog of the Schizosaccharomyces pombe rad9+ checkpoint control gene.". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13890–5. PMID 8943031.
Volkmer E, Karnitz LM (1999). "Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex.". J. Biol. Chem. 274 (2): 567–70. PMID 9872989.
St Onge RP, Udell CM, Casselman R, Davey S (1999). "The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1.". Mol. Biol. Cell 10 (6): 1985–95. PMID 10359610.
Komatsu K, Miyashita T, Hang H, et al. (2000). "Human homologue of S. pombe Rad9 interacts with BCL-2/BCL-xL and promotes apoptosis.". Nat. Cell Biol. 2 (1): 1–6. doi:10.1038/71316. PMID 10620799.
Bessho T, Sancar A (2000). "Human DNA damage checkpoint protein hRAD9 is a 3' to 5' exonuclease.". J. Biol. Chem. 275 (11): 7451–4. PMID 10713044.
Hang H, Lieberman HB (2000). "Physical interactions among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression.". Genomics 65 (1): 24–33. doi:10.1006/geno.2000.6142. PMID 10777662.
Cai RL, Yan-Neale Y, Cueto MA, et al. (2000). "HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins.". J. Biol. Chem. 275 (36): 27909–16. doi:10.1074/jbc.M000168200. PMID 10846170.
Burtelow MA, Kaufmann SH, Karnitz LM (2000). "Retention of the human Rad9 checkpoint complex in extraction-resistant nuclear complexes after DNA damage.". J. Biol. Chem. 275 (34): 26343–8. doi:10.1074/jbc.M001244200. PMID 10852904.
Rauen M, Burtelow MA, Dufault VM, Karnitz LM (2000). "The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9.". J. Biol. Chem. 275 (38): 29767–71. doi:10.1074/jbc.M005782200. PMID 10884395.
Komatsu K, Wharton W, Hang H, et al. (2000). "PCNA interacts with hHus1/hRad9 in response to DNA damage and replication inhibition.". Oncogene 19 (46): 5291–7. doi:10.1038/sj.onc.1203901. PMID 11077446.
Chen MJ, Lin YT, Lieberman HB, et al. (2001). "ATM-dependent phosphorylation of human Rad9 is required for ionizing radiation-induced checkpoint activation.". J. Biol. Chem. 276 (19): 16580–6. doi:10.1074/jbc.M008871200. PMID 11278446.
Burtelow MA, Roos-Mattjus PM, Rauen M, et al. (2001). "Reconstitution and molecular analysis of the hRad9-hHus1-hRad1 (9-1-1) DNA damage responsive checkpoint complex.". J. Biol. Chem. 276 (28): 25903–9. doi:10.1074/jbc.M102946200. PMID 11340080.
Mäkiniemi M, Hillukkala T, Tuusa J, et al. (2001). "BRCT domain-containing protein TopBP1 functions in DNA replication and damage response.". J. Biol. Chem. 276 (32): 30399–406. doi:10.1074/jbc.M102245200. PMID 11395493.
St Onge RP, Besley BD, Park M, et al. (2001). "DNA damage-dependent and -independent phosphorylation of the hRad9 checkpoint protein.". J. Biol. Chem. 276 (45): 41898–905. doi:10.1074/jbc.M105152200. PMID 11551919.
Xiang SL, Kumano T, Iwasaki SI, et al. (2001). "The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9.". Biochem. Biophys. Res. Commun. 287 (4): 932–40. doi:10.1006/bbrc.2001.5685. PMID 11573955.
Zou L, Cortez D, Elledge SJ (2002). "Regulation of ATR substrate selection by Rad17-dependent loading of Rad9 complexes onto chromatin.". Genes Dev. 16 (2): 198–208. doi:10.1101/gad.950302. PMID 11799063.
Griffith JD, Lindsey-Boltz LA, Sancar A (2002). "Structures of the human Rad17-replication factor C and checkpoint Rad 9-1-1 complexes visualized by glycerol spray/low voltage microscopy.". J. Biol. Chem. 277 (18): 15233–6. doi:10.1074/jbc.C200129200. PMID 11907025.
Hang H, Zhang Y, Dunbrack RL, et al. (2002). "Identification and characterization of a paralog of human cell cycle checkpoint gene HUS1.". Genomics 79 (4): 487–92. doi:10.1006/geno.2002.6737. PMID 11944979.
Yoshida K, Komatsu K, Wang HG, Kufe D (2002). "c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage.". Mol. Cell. Biol. 22 (10): 3292–300. PMID 11971963.