POLR2E

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Polymerase (RNA) II (DNA directed) polypeptide E, 25kDa
Identifiers
Symbols POLR2E ; RPABC1; RPB5; XAP4; hRPB25; hsRPB5
External IDs Template:OMIM5 Template:MGI HomoloGene2018
RNA expression pattern
File:PBB GE POLR2E 217854 s at tn.png
File:PBB GE POLR2E 213887 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Polymerase (RNA) II (DNA directed) polypeptide E, 25kDa, also known as POLR2E, is a human gene.

This gene encodes the fifth largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. This subunit is shared by the other two DNA-directed RNA polymerases and is present in two-fold molar excess over the other polymerase subunits. An interaction between this subunit and a hepatitis virus transactivating protein has been demonstrated, suggesting that interaction between transcriptional activators and the polymerase can occur through this subunit. A pseudogene is located on chromosome 11.[1]

References

  1. "Entrez Gene: POLR2E polymerase (RNA) II (DNA directed) polypeptide E, 25kDa".

Further reading

  • Jeang KT (1998). "Tat, Tat-associated kinase, and transcription". J. Biomed. Sci. 5 (1): 24–7. PMID 9570510.
  • Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation". Curr. Biol. 8 (13): R447–9. PMID 9651670.
  • Romano G, Kasten M, De Falco G; et al. (2000). "Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression". J. Cell. Biochem. 75 (3): 357–68. PMID 10536359.
  • Marcello A, Zoppé M, Giacca M (2002). "Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator". IUBMB Life. 51 (3): 175–81. PMID 11547919.
  • Stevens M, De Clercq E, Balzarini J (2007). "The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention". Med Res Rev. 26 (5): 595–625. doi:10.1002/med.20081. PMID 16838299.
  • Harrich D, McMillan N, Munoz L; et al. (2007). "Will diverse Tat interactions lead to novel antiretroviral drug targets?". Current drug targets. 7 (12): 1595–606. PMID 17168834.
  • Kato H, Sumimoto H, Pognonec P; et al. (1992). "HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors". Genes Dev. 6 (4): 655–66. PMID 1559613.
  • Pati UK, Weissman SM (1991). "Isolation and molecular characterization of a cDNA encoding the 23-kDa subunit of human RNA polymerase II". J. Biol. Chem. 266 (20): 13468. PMID 2071613.
  • Southgate C, Zapp ML, Green MR (1990). "Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein". Nature. 345 (6276): 640–2. doi:10.1038/345640a0. PMID 2190099.
  • Pati UK, Weissman SM (1989). "Isolation and molecular characterization of a cDNA encoding the 23-kDa subunit of human RNA polymerase II". J. Biol. Chem. 264 (22): 13114–21. PMID 2753903.
  • Wu-Baer F, Sigman D, Gaynor RB (1995). "Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat". Proc. Natl. Acad. Sci. U.S.A. 92 (16): 7153–7. PMID 7638159.
  • Cheong JH, Yi M, Lin Y, Murakami S (1995). "Human RPB5, a subunit shared by eukaryotic nuclear RNA polymerases, binds human hepatitis B virus X protein and may play a role in X transactivation". EMBO J. 14 (1): 143–50. PMID 7828586.
  • Herrmann CH, Rice AP (1995). "Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor". J. Virol. 69 (3): 1612–20. PMID 7853496.
  • Acker J, Mattei MG, Wintzerith M; et al. (1994). "Chromosomal localization of human RNA polymerase II subunit genes". Genomics. 20 (3): 496–9. doi:10.1006/geno.1994.1208. PMID 8034326.
  • Keen NJ, Gait MJ, Karn J (1996). "Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex". Proc. Natl. Acad. Sci. U.S.A. 93 (6): 2505–10. PMID 8637904.
  • Yang X, Herrmann CH, Rice AP (1996). "The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function". J. Virol. 70 (7): 4576–84. PMID 8676484.
  • Agostini I, Navarro JM, Rey F; et al. (1996). "The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB". J. Mol. Biol. 261 (5): 599–606. doi:10.1006/jmbi.1996.0485. PMID 8800208.
  • Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science. 274 (5287): 605–10. PMID 8849451.
  • Okamoto H, Sheline CT, Corden JL; et al. (1996). "Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II". Proc. Natl. Acad. Sci. U.S.A. 93 (21): 11575–9. PMID 8876177.
  • Chun RF, Jeang KT (1996). "Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1". J. Biol. Chem. 271 (44): 27888–94. PMID 8910388.

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