Cyclin O: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Cyclin-O''' is a [[protein]] that in humans is encoded by the ''CCNO'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCNO cyclin O| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10309| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Cyclin O
| HGNCid = 18576
| Symbol = CCNO
| AltSymbols =; FLJ22422; UDG2; UNG2
| OMIM = 607752
| ECnumber = 
| Homologene = 50171
| MGIid = 2145534
| GeneAtlas_image1 = PBB_GE_CCNU_210021_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004844 |text = uracil DNA N-glycosylase activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10309
    | Hs_Ensembl = ENSG00000152669
    | Hs_RefseqProtein = NP_001019763
    | Hs_RefseqmRNA = NM_001024592
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 54562740
    | Hs_GenLoc_end = 54565265
    | Hs_Uniprot = P22674
    | Mm_EntrezGene = 218630
    | Mm_Ensembl = ENSMUSG00000042417
    | Mm_RefseqmRNA = XM_127523
    | Mm_RefseqProtein = XP_127523
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 114108776
    | Mm_GenLoc_end = 114111654
    | Mm_Uniprot = P0C242
  }}
}}
'''Cyclin O''', also known as '''CCNO''' or '''CCNU''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCNO cyclin O| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10309| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
Cyclin O has been shown to [[Protein-protein interaction|interact]] with [[RPA2]]<ref name=pmid10393198>{{cite journal | vauthors = Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O, Krokan HE | title = Post-replicative base excision repair in replication foci | journal = The EMBO Journal | volume = 18 | issue = 13 | pages = 3834–44 | date = July 1999 | pmid = 10393198 | pmc = 1171460 | doi = 10.1093/emboj/18.13.3834 }}</ref> and [[PCNA]].<ref name=pmid10393198/><ref name=pmid12171929>{{cite journal | vauthors = Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T | title = 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 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 43 | pages = 40362–7 | date = October 2002 | pmid = 12171929 | doi = 10.1074/jbc.M206194200 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Caradonna S, Muller-Weeks S | title = The nature of enzymes involved in uracil-DNA repair: isoform characteristics of proteins responsible for nuclear and mitochondrial genomic integrity | journal = Current Protein & Peptide Science | volume = 2 | issue = 4 | pages = 335–47 | date = December 2001 | pmid = 12369930 | doi = 10.2174/1389203013381044 }}
| citations =
* {{cite journal | vauthors = Muller SJ, Caradonna S | title = Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase | journal = Biochimica et Biophysica Acta | volume = 1088 | issue = 2 | pages = 197–207 | date = February 1991 | pmid = 2001396 | doi = 10.1016/0167-4781(91)90055-Q }}
*{{cite journal | author=Caradonna S, Muller-Weeks S |title=The nature of enzymes involved in uracil-DNA repair: isoform characteristics of proteins responsible for nuclear and mitochondrial genomic integrity. |journal=Curr. Protein Pept. Sci. |volume=2 |issue= 4 |pages= 335-47 |year= 2002 |pmid= 12369930 |doi= }}
* {{cite journal | vauthors = Muller SJ, Caradonna S | title = Cell cycle regulation of a human cyclin-like gene encoding uracil-DNA glycosylase | journal = The Journal of Biological Chemistry | volume = 268 | issue = 2 | pages = 1310–9 | date = January 1993 | pmid = 8419333 | doi =  }}
*{{cite journal | author=Muller SJ, Caradonna S |title=Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase. |journal=Biochim. Biophys. Acta |volume=1088 |issue= 2 |pages= 197-207 |year= 1991 |pmid= 2001396 |doi= }}
* {{cite journal | vauthors = Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O, Krokan HE | title = Post-replicative base excision repair in replication foci | journal = The EMBO Journal | volume = 18 | issue = 13 | pages = 3834–44 | date = July 1999 | pmid = 10393198 | pmc = 1171460 | doi = 10.1093/emboj/18.13.3834 }}
*{{cite journal | author=Muller SJ, Caradonna S |title=Cell cycle regulation of a human cyclin-like gene encoding uracil-DNA glycosylase. |journal=J. Biol. Chem. |volume=268 |issue= 2 |pages= 1310-9 |year= 1993 |pmid= 8419333 |doi=  }}
* {{cite journal | vauthors = Mer G, Bochkarev A, Gupta R, Bochkareva E, Frappier L, Ingles CJ, Edwards AM, Chazin WJ | title = Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA | journal = Cell | volume = 103 | issue = 3 | pages = 449–56 | date = October 2000 | pmid = 11081631 | doi = 10.1016/S0092-8674(00)00136-7 }}
*{{cite journal | author=Otterlei M, Warbrick E, Nagelhus TA, ''et al.'' |title=Post-replicative base excision repair in replication foci. |journal=EMBO J. |volume=18 |issue= 13 |pages= 3834-44 |year= 1999 |pmid= 10393198 |doi= 10.1093/emboj/18.13.3834 }}
* {{cite journal | vauthors = Kavli B, Sundheim O, Akbari M, Otterlei M, Nilsen H, Skorpen F, Aas PA, Hagen L, Krokan HE, Slupphaug G | title = 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 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 42 | pages = 39926–36 | date = October 2002 | pmid = 12161446 | doi = 10.1074/jbc.M207107200 }}
*{{cite journal | author=Mer G, Bochkarev A, Gupta R, ''et al.'' |title=Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA. |journal=Cell |volume=103 |issue= 3 |pages= 449-56 |year= 2000 |pmid= 11081631 |doi= }}
* {{cite journal | vauthors = Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T | title = 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 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 43 | pages = 40362–7 | date = October 2002 | pmid = 12171929 | doi = 10.1074/jbc.M206194200 }}
*{{cite journal | author=Kavli B, Sundheim O, Akbari M, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39926-36 |year= 2002 |pmid= 12161446 |doi= 10.1074/jbc.M207107200 }}
* {{cite journal | vauthors = Priet S, Navarro JM, Gros N, Quérat G, Sire J | title = Differential incorporation of uracil DNA glycosylase UNG2 into HIV-1, HIV-2, and SIV(MAC) viral particles | journal = Virology | volume = 307 | issue = 2 | pages = 283–9 | date = March 2003 | pmid = 12667798 | doi = 10.1016/S0042-6822(02)00073-9 }}
*{{cite journal | author=Ohta S, Shiomi Y, Sugimoto K, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40362-7 |year= 2002 |pmid= 12171929 |doi= 10.1074/jbc.M206194200 }}
* {{cite journal | vauthors = Elder RT, Zhu X, Priet S, Chen M, Yu M, Navarro JM, Sire J, Zhao Y | title = A fission yeast homologue of the human uracil-DNA-glycosylase and their roles in causing DNA damage after overexpression | journal = Biochemical and Biophysical Research Communications | volume = 306 | issue = 3 | pages = 693–700 | date = July 2003 | pmid = 12810074 | doi = 10.1016/S0006-291X(03)01036-2 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Lu X, Bocangel D, Nannenga B, Yamaguchi H, Appella E, Donehower LA | title = The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair | journal = Molecular Cell | volume = 15 | issue = 4 | pages = 621–34 | date = August 2004 | pmid = 15327777 | doi = 10.1016/j.molcel.2004.08.007 }}
*{{cite journal  | author=Priet S, Navarro JM, Gros N, ''et al.'' |title=Differential incorporation of uracil DNA glycosylase UNG2 into HIV-1, HIV-2, and SIV(MAC) viral particles. |journal=Virology |volume=307 |issue= 2 |pages= 283-9 |year= 2003 |pmid= 12667798 |doi= }}
* {{cite journal | vauthors = Hirst R, Gosden R, Miller D | title = The cyclin-like uracil DNA glycosylase (UDG) of murine oocytes and its relationship to human and chimpanzee homologues | journal = Gene | volume = 375 | issue =  | pages = 95–102 | date = June 2006 | pmid = 16697536 | doi = 10.1016/j.gene.2006.02.030 }}
*{{cite journal | author=Elder RT, Zhu X, Priet S, ''et al.'' |title=A fission yeast homologue of the human uracil-DNA-glycosylase and their roles in causing DNA damage after overexpression. |journal=Biochem. Biophys. Res. Commun. |volume=306 |issue= 3 |pages= 693-700 |year= 2003 |pmid= 12810074 |doi= }}
* {{cite journal | vauthors = Verma SC, Bajaj BG, Cai Q, Si H, Seelhammer T, Robertson ES | title = 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 = Journal of Virology | volume = 80 | issue = 22 | pages = 11178–90 | date = November 2006 | pmid = 16928741 | pmc = 1642147 | doi = 10.1128/JVI.01334-06 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{cite journal | vauthors = Yang B, Chen K, Zhang C, Huang S, Zhang H | title = Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA | journal = The Journal of Biological Chemistry | volume = 282 | issue = 16 | pages = 11667–75 | date = April 2007 | pmid = 17272283 | doi = 10.1074/jbc.M606864200 }}
*{{cite journal | author=Lu X, Bocangel D, Nannenga B, ''et al.'' |title=The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair. |journal=Mol. Cell |volume=15 |issue= 4 |pages= 621-34 |year= 2004 |pmid= 15327777 |doi= 10.1016/j.molcel.2004.08.007 }}
* {{cite journal | vauthors = Schröfelbauer B, Hakata Y, Landau NR | title = HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 10 | pages = 4130–5 | date = March 2007 | pmid = 17360488 | pmc = 1820720 | doi = 10.1073/pnas.0610167104 }}
*{{cite journal | author=Schmutz J, Martin J, Terry A, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 5. |journal=Nature |volume=431 |issue= 7006 |pages= 268-74 |year= 2004 |pmid= 15372022 |doi= 10.1038/nature02919 }}
* {{cite journal | vauthors = Pettersen HS, Sundheim O, Gilljam KM, Slupphaug G, Krokan HE, Kavli B | title = Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms | journal = Nucleic Acids Research | volume = 35 | issue = 12 | pages = 3879–92 | year = 2007 | pmid = 17537817 | pmc = 1919486 | doi = 10.1093/nar/gkm372 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Hirst R, Gosden R, Miller D |title=The cyclin-like uracil DNA glycosylase (UDG) of murine oocytes and its relationship to human and chimpanzee homologues. |journal=Gene |volume=375 |issue=  |pages= 95-102 |year= 2006 |pmid= 16697536 |doi= 10.1016/j.gene.2006.02.030 }}
*{{cite journal | author=Verma SC, Bajaj BG, Cai Q, ''et al.'' |title=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=J. Virol. |volume=80 |issue= 22 |pages= 11178-90 |year= 2006 |pmid= 16928741 |doi= 10.1128/JVI.01334-06 }}
*{{cite journal | author=Yang B, Chen K, Zhang C, ''et al.'' |title=Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA. |journal=J. Biol. Chem. |volume=282 |issue= 16 |pages= 11667-75 |year= 2007 |pmid= 17272283 |doi= 10.1074/jbc.M606864200 }}
*{{cite journal | author=Schröfelbauer B, Hakata Y, Landau NR |title=HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=104 |issue= 10 |pages= 4130-5 |year= 2007 |pmid= 17360488 |doi= 10.1073/pnas.0610167104 }}
*{{cite journal | author=Pettersen HS, Sundheim O, Gilljam KM, ''et al.'' |title=Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms. |journal=Nucleic Acids Res. |volume=35 |issue= 12 |pages= 3879-92 |year= 2007 |pmid= 17537817 |doi= 10.1093/nar/gkm372 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
* {{UCSC genome browser|CCNO}}
* {{UCSC gene details|CCNO}}
 
 
 
{{gene-5-stub}}

Latest revision as of 17:58, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ "Entrez Gene: CCNO cyclin O".
  2. ↑ 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.
  3. ↑ 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

External links


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