Cyclin O
Cyclin-O is a protein that in humans is encoded by the CCNO gene.[1]
Interactions
Cyclin O has been shown to interact with RPA2[2] and PCNA.[2][3]
References
- ↑ “Entrez Gene: CCNO cyclin O”.
- ↑ 2.0 2.1 Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O, Krokan HE (July 1999). “Post-replicative base excision repair in replication foci”. The EMBO Journal. 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. PMC 1171460. PMID 10393198.
- ↑ Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (October 2002). “A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein”. The Journal of Biological Chemistry. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.
Further reading
- Caradonna S, Muller-Weeks S (December 2001). “The nature of enzymes involved in uracil-DNA repair: isoform characteristics of proteins responsible for nuclear and mitochondrial genomic integrity”. Current Protein & Peptide Science. 2 (4): 335–47. doi:10.2174/1389203013381044. PMID 12369930.
- Muller SJ, Caradonna S (February 1991). “Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase”. Biochimica et Biophysica Acta. 1088 (2): 197–207. doi:10.1016/0167-4781(91)90055-Q. PMID 2001396.
- Muller SJ, Caradonna S (January 1993). “Cell cycle regulation of a human cyclin-like gene encoding uracil-DNA glycosylase”. The Journal of Biological Chemistry. 268 (2): 1310–9. PMID 8419333.
- Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O, Krokan HE (July 1999). “Post-replicative base excision repair in replication foci”. The EMBO Journal. 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. PMC 1171460. PMID 10393198.
- Mer G, Bochkarev A, Gupta R, Bochkareva E, Frappier L, Ingles CJ, Edwards AM, Chazin WJ (October 2000). “Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA”. Cell. 103 (3): 449–56. doi:10.1016/S0092-8674(00)00136-7. PMID 11081631.
- Kavli B, Sundheim O, Akbari M, Otterlei M, Nilsen H, Skorpen F, Aas PA, Hagen L, Krokan HE, Slupphaug G (October 2002). “hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup”. The Journal of Biological Chemistry. 277 (42): 39926–36. doi:10.1074/jbc.M207107200. PMID 12161446.
- Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (October 2002). “A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein”. The Journal of Biological Chemistry. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.
- Priet S, Navarro JM, Gros N, Quérat G, Sire J (March 2003). “Differential incorporation of uracil DNA glycosylase UNG2 into HIV-1, HIV-2, and SIV(MAC) viral particles”. Virology. 307 (2): 283–9. doi:10.1016/S0042-6822(02)00073-9. PMID 12667798.
- Elder RT, Zhu X, Priet S, Chen M, Yu M, Navarro JM, Sire J, Zhao Y (July 2003). “A fission yeast homologue of the human uracil-DNA-glycosylase and their roles in causing DNA damage after overexpression”. Biochemical and Biophysical Research Communications. 306 (3): 693–700. doi:10.1016/S0006-291X(03)01036-2. PMID 12810074.
- Lu X, Bocangel D, Nannenga B, Yamaguchi H, Appella E, Donehower LA (August 2004). “The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair”. Molecular Cell. 15 (4): 621–34. doi:10.1016/j.molcel.2004.08.007. PMID 15327777.
- Hirst R, Gosden R, Miller D (June 2006). “The cyclin-like uracil DNA glycosylase (UDG) of murine oocytes and its relationship to human and chimpanzee homologues”. Gene. 375: 95–102. doi:10.1016/j.gene.2006.02.030. PMID 16697536.
- Verma SC, Bajaj BG, Cai Q, Si H, Seelhammer T, Robertson ES (November 2006). “Latency-associated nuclear antigen of Kaposi’s sarcoma-associated herpesvirus recruits uracil DNA glycosylase 2 at the terminal repeats and is important for latent persistence of the virus”. Journal of Virology. 80 (22): 11178–90. doi:10.1128/JVI.01334-06. PMC 1642147. PMID 16928741.
- Yang B, Chen K, Zhang C, Huang S, Zhang H (April 2007). “Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA”. The Journal of Biological Chemistry. 282 (16): 11667–75. doi:10.1074/jbc.M606864200. PMID 17272283.
- Schröfelbauer B, Hakata Y, Landau NR (March 2007). “HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1”. Proceedings of the National Academy of Sciences of the United States of America. 104 (10): 4130–5. doi:10.1073/pnas.0610167104. PMC 1820720. PMID 17360488.
- Pettersen HS, Sundheim O, Gilljam KM, Slupphaug G, Krokan HE, Kavli B (2007). “Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms”. Nucleic Acids Research. 35 (12): 3879–92. doi:10.1093/nar/gkm372. PMC 1919486. PMID 17537817.
External links
- CCNO human gene location in the UCSC Genome Browser.
- CCNO human gene details in the UCSC Genome Browser.
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