CPSF3

From Wikipedia, the free encyclopedia


Cleavage and polyadenylation specific factor 3, 73kDa
PDB rendering based on 2i7t.
Available structures: 2i7t, 2i7v
Identifiers
Symbol(s) CPSF3; CPSF; CPSF-73; CPSF73
External IDs OMIM: 606029 MGI1859328 HomoloGene6499
Orthologs
Human Mouse
Entrez 51692 54451
Ensembl ENSG00000119203 ENSMUSG00000054309
Uniprot Q9UKF6 Q3TC91
Refseq NM_016207 (mRNA)
NP_057291 (protein)
NM_018813 (mRNA)
NP_061283 (protein)
Location Chr 2: 9.48 - 9.53 Mb Chr 12: 21.53 - 21.56 Mb
Pubmed search [1] [2]

Cleavage and polyadenylation specific factor 3, 73kDa, also known as CPSF3, is a human gene.[1]


[edit] References

[edit] Further reading

  • Murthy KG, Manley JL (1995). "The 160-kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3'-end formation.". Genes Dev. 9 (21): 2672–83. PMID 7590244. 
  • Jenny A, Hauri HP, Keller W (1994). "Characterization of cleavage and polyadenylation specificity factor and cloning of its 100-kilodalton subunit.". Mol. Cell. Biol. 14 (12): 8183–90. PMID 7969155. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298. 
  • Thuresson AC, Aström J, Aström A, et al. (1994). "Multiple forms of poly(A) polymerases in human cells.". Proc. Natl. Acad. Sci. U.S.A. 91 (3): 979–83. PMID 8302877. 
  • Jenny A, Minvielle-Sebastia L, Preker PJ, Keller W (1996). "Sequence similarity between the 73-kilodalton protein of mammalian CPSF and a subunit of yeast polyadenylation factor I.". Science 274 (5292): 1514–7. PMID 8929409. 
  • McCracken S, Fong N, Yankulov K, et al. (1997). "The C-terminal domain of RNA polymerase II couples mRNA processing to transcription.". Nature 385 (6614): 357–61. doi:10.1038/385357a0. PMID 9002523. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149. 
  • Takagaki Y, Manley JL (2000). "Complex protein interactions within the human polyadenylation machinery identify a novel component.". Mol. Cell. Biol. 20 (5): 1515–25. PMID 10669729. 
  • de Vries H, Rüegsegger U, Hübner W, et al. (2000). "Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors.". EMBO J. 19 (21): 5895–904. doi:10.1093/emboj/19.21.5895. PMID 11060040. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Kaufmann I, Martin G, Friedlein A, et al. (2005). "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase.". EMBO J. 23 (3): 616–26. doi:10.1038/sj.emboj.7600070. PMID 14749727. 
  • Calzado MA, Sancho R, Muñoz E (2004). "Human immunodeficiency virus type 1 Tat increases the expression of cleavage and polyadenylation specificity factor 73-kilodalton subunit modulating cellular and viral expression.". J. Virol. 78 (13): 6846–54. doi:10.1128/JVI.78.13.6846-6854.2004. PMID 15194760. 
  • Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Mandel CR, Kaneko S, Zhang H, et al. (2007). "Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease.". Nature 444 (7121): 953–6. doi:10.1038/nature05363. PMID 17128255. 
  • de la Vega L, Sánchez-Duffhues G, Fresno M, et al. (2007). "The 73 kDa subunit of the CPSF complex binds to the HIV-1 LTR promoter and functions as a negative regulatory factor that is inhibited by the HIV-1 Tat protein.". J. Mol. Biol. 372 (2): 317–30. doi:10.1016/j.jmb.2007.06.075. PMID 17669424.