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Wikipedia

Cyclin O

Cyclin-O is a protein that in humans is encoded by the CCNO gene.[4]

CCNO
Identifiers
AliasesCCNO, CCNU, CILD29, UDG2, Cyclin O
External IDsOMIM: 607752 MGI: 2145534 HomoloGene: 50171 GeneCards: CCNO
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001024592
NM_021147

NM_001081062

RefSeq (protein)

NP_066970

NP_001074531

Location (UCSC)n/aChr 13: 113.12 – 113.13 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Interactions edit

Cyclin O has been shown to interact with RPA2[5] and PCNA.[5][6]

References edit

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000042417 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Entrez Gene: CCNO cyclin O".
  5. ^ a b 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.
  6. ^ 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 edit

  • 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 (BBA) - Gene Structure and Expression. 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. doi:10.1016/S0021-9258(18)54076-X. 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. S2CID 16640087.
  • 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. Bibcode:2007PNAS..104.4130S. 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 edit


cyclin, cyclin, protein, that, humans, encoded, ccno, gene, ccnoidentifiersaliasesccno, ccnu, cild29, udg2, external, idsomim, 607752, 2145534, homologene, 50171, genecards, ccnogene, location, mouse, chromosome, mouse, band13, 2start113, end113, expression, p. Cyclin O is a protein that in humans is encoded by the CCNO gene 4 CCNOIdentifiersAliasesCCNO CCNU CILD29 UDG2 Cyclin OExternal IDsOMIM 607752 MGI 2145534 HomoloGene 50171 GeneCards CCNOGene location Mouse Chr Chromosome 13 mouse 1 Band13 13 D2 2Start113 124 336 bp 1 End113 127 311 bp 1 RNA expression patternBgeeHumanMouse ortholog Top expressed inoocytesecondary oocytebronchial epithelial cellright uterine tubebody of pancreasright lobe of thyroid glandleft lobe of thyroid glandcorpus epididymisanterior pituitarynucleus accumbensTop expressed insecondary oocytemorulaovaryproximal tubuleleft lung lobesuperior frontal gyrusspermatocytecumulus cellvisual cortexrespiratory epitheliumMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionuracil DNA N glycosylase activity protein kinase activity cyclin dependent protein serine threonine kinase regulator activity protein kinase bindingCellular componentcytoplasm nucleus cyclin dependent protein kinase holoenzyme complexBiological processcell projection organization multi ciliated epithelial cell differentiation cilium assembly mitotic cell cycle cell cycle cell division regulation of cyclin dependent protein serine threonine kinase activity protein phosphorylation regulation of mitotic nuclear division positive regulation of cell population proliferation positive regulation of cell cycle mitotic cell cycle phase transitionSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez10309218630Ensembln aENSMUSG00000042417UniProtP22674P0C242RefSeq mRNA NM 001024592NM 021147NM 001081062RefSeq protein NP 066970NP 001074531Location UCSC n aChr 13 113 12 113 13 MbPubMed search 2 3 WikidataView Edit HumanView Edit Mouse Contents 1 Interactions 2 References 3 Further reading 4 External linksInteractions editCyclin O has been shown to interact with RPA2 5 and PCNA 5 6 References edit a b c GRCm38 Ensembl release 89 ENSMUSG00000042417 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Entrez Gene CCNO cyclin O a b 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 editCaradonna 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 amp 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 BBA Gene Structure and Expression 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 doi 10 1016 S0021 9258 18 54076 X 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 S2CID 16640087 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 Querat 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 Schrofelbauer 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 Bibcode 2007PNAS 104 4130S 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 editCCNO human gene location in the UCSC Genome Browser CCNO human gene details in the UCSC Genome Browser nbsp This article on a gene on human chromosome 5 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Cyclin O amp oldid 1116587605, wikipedia, wiki, book, books, library,

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