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*{{cite journal  | author=Harrich D |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595–606 |year= 2007 |pmid= 17168834 |doi=10.2174/138945006779025338  |name-list-format=vanc| author2=McMillan N  | author3=Munoz L  | display-authors=3  | last4=Apolloni  | first4=Ann  | last5=Meredith  | first5=Luke  }}
*{{cite journal  | author=Harrich D |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595–606 |year= 2007 |pmid= 17168834 |doi=10.2174/138945006779025338  |name-list-format=vanc| author2=McMillan N  | author3=Munoz L  | display-authors=3  | last4=Apolloni  | first4=Ann  | last5=Meredith  | first5=Luke  }}
*{{cite journal  | author=Kato H |title=HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors |journal=Genes Dev. |volume=6 |issue= 4 |pages= 655–66 |year= 1992 |pmid= 1559613 |doi=10.1101/gad.6.4.655  |name-list-format=vanc| author2=Sumimoto H  | author3=Pognonec P  | display-authors=3  | last4=Chen  | first4=C H  | last5=Rosen  | first5=C A  | last6=Roeder  | first6=R G  }}
*{{cite journal  | author=Kato H |title=HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors |journal=Genes Dev. |volume=6 |issue= 4 |pages= 655–66 |year= 1992 |pmid= 1559613 |doi=10.1101/gad.6.4.655  |name-list-format=vanc| author2=Sumimoto H  | author3=Pognonec P  | display-authors=3  | last4=Chen  | first4=C H  | last5=Rosen  | first5=C A  | last6=Roeder  | first6=R G  }}
*{{cite journal  |vauthors=Southgate C, Zapp ML, Green MR |title=Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein |journal=Nature |volume=345 |issue= 6276 |pages= 640–2 |year= 1990 |pmid= 2190099 |doi= 10.1038/345640a0 }}
*{{cite journal  |vauthors=Southgate C, Zapp ML, Green MR |title=Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein |journal=Nature |volume=345 |issue= 6276 |pages= 640–2 |year= 1990 |pmid= 2190099 |doi= 10.1038/345640a0 |bibcode=1990Natur.345..640S }}
*{{cite journal  |vauthors=Wu-Baer F, Sigman D, Gaynor RB |title=Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 16 |pages= 7153–7 |year= 1995 |pmid= 7638159 |doi=10.1073/pnas.92.16.7153  | pmc=41297  }}
*{{cite journal  |vauthors=Wu-Baer F, Sigman D, Gaynor RB |title=Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 16 |pages= 7153–7 |year= 1995 |pmid= 7638159 |doi=10.1073/pnas.92.16.7153  | pmc=41297  |bibcode=1995PNAS...92.7153W }}
*{{cite journal  |vauthors=Acker J, Wintzerith M, Vigneron M, Kedinger C |title=A 14.4 KDa acidic subunit of human RNA polymerase II with a putative leucine-zipper |journal=DNA Seq. |volume=4 |issue= 5 |pages= 329–31 |year= 1995 |pmid= 7803819 |doi=10.3109/10425179409020860  }}
*{{cite journal  |vauthors=Acker J, Wintzerith M, Vigneron M, Kedinger C |title=A 14.4 KDa acidic subunit of human RNA polymerase II with a putative leucine-zipper |journal=DNA Seq. |volume=4 |issue= 5 |pages= 329–31 |year= 1995 |pmid= 7803819 |doi=10.3109/10425179409020860  }}
*{{cite journal  |vauthors=Herrmann CH, Rice AP |title=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 |journal=J. Virol. |volume=69 |issue= 3 |pages= 1612–20 |year= 1995 |pmid= 7853496 |doi=  | pmc=188757  }}
*{{cite journal  |vauthors=Herrmann CH, Rice AP |title=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 |journal=J. Virol. |volume=69 |issue= 3 |pages= 1612–20 |year= 1995 |pmid= 7853496 |doi=  | pmc=188757  }}
*{{cite journal  |vauthors=Keen NJ, Gait MJ, Karn J |title=Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 6 |pages= 2505–10 |year= 1996 |pmid= 8637904 |doi=10.1073/pnas.93.6.2505  | pmc=39827  }}
*{{cite journal  |vauthors=Keen NJ, Gait MJ, Karn J |title=Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 6 |pages= 2505–10 |year= 1996 |pmid= 8637904 |doi=10.1073/pnas.93.6.2505  | pmc=39827  |bibcode=1996PNAS...93.2505K }}
*{{cite journal  |vauthors=Yang X, Herrmann CH, Rice AP |title=The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function |journal=J. Virol. |volume=70 |issue= 7 |pages= 4576–84 |year= 1996 |pmid= 8676484 |doi=  | pmc=190394  }}
*{{cite journal  |vauthors=Yang X, Herrmann CH, Rice AP |title=The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function |journal=J. Virol. |volume=70 |issue= 7 |pages= 4576–84 |year= 1996 |pmid= 8676484 |doi=  | pmc=190394  }}
*{{cite journal  | author=Agostini I |title=The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB |journal=J. Mol. Biol. |volume=261 |issue= 5 |pages= 599–606 |year= 1996 |pmid= 8800208 |doi= 10.1006/jmbi.1996.0485  |name-list-format=vanc| author2=Navarro JM  | author3=Rey F  | display-authors=3  | last4=Bouhamdan  | first4=M  | last5=Spire  | first5=B  | last6=Vigne  | first6=R  | last7=Sire  | first7=J }}
*{{cite journal  | author=Agostini I |title=The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB |journal=J. Mol. Biol. |volume=261 |issue= 5 |pages= 599–606 |year= 1996 |pmid= 8800208 |doi= 10.1006/jmbi.1996.0485  |name-list-format=vanc| author2=Navarro JM  | author3=Rey F  | display-authors=3  | last4=Bouhamdan  | first4=M  | last5=Spire  | first5=B  | last6=Vigne  | first6=R  | last7=Sire  | first7=J }}
*{{cite journal  |vauthors=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat |journal=Science |volume=274 |issue= 5287 |pages= 605–10 |year= 1996 |pmid= 8849451 |doi=10.1126/science.274.5287.605  }}
*{{cite journal  |vauthors=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat |journal=Science |volume=274 |issue= 5287 |pages= 605–10 |year= 1996 |pmid= 8849451 |doi=10.1126/science.274.5287.605  |bibcode=1996Sci...274..605Z }}
*{{cite journal  | author=Okamoto H |title=Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 21 |pages= 11575–9 |year= 1996 |pmid= 8876177 |doi=10.1073/pnas.93.21.11575  | pmc=38099  |name-list-format=vanc| author2=Sheline CT  | author3=Corden JL  | display-authors=3  | last4=Jones  | first4=KA  | last5=Peterlin  | first5=BM  }}
*{{cite journal  | author=Okamoto H |title=Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 21 |pages= 11575–9 |year= 1996 |pmid= 8876177 |doi=10.1073/pnas.93.21.11575  | pmc=38099  |name-list-format=vanc| author2=Sheline CT  | author3=Corden JL  | display-authors=3  | last4=Jones  | first4=KA  | last5=Peterlin  | first5=BM  |bibcode=1996PNAS...9311575O}}
*{{cite journal  |vauthors=Chun RF, Jeang KT |title=Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1 |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27888–94 |year= 1996 |pmid= 8910388 |doi=10.1074/jbc.271.44.27888  }}
*{{cite journal  |vauthors=Chun RF, Jeang KT |title=Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1 |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27888–94 |year= 1996 |pmid= 8910388 |doi=10.1074/jbc.271.44.27888  }}
*{{cite journal  |vauthors=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain |journal=Nature |volume=384 |issue= 6607 |pages= 375–8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal  |vauthors=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain |journal=Nature |volume=384 |issue= 6607 |pages= 375–8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 |bibcode=1996Natur.384..375P }}
*{{cite journal  |vauthors=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951–8 |year= 1997 |pmid= 9054383 |doi=10.1074/jbc.272.11.6951  }}
*{{cite journal  |vauthors=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951–8 |year= 1997 |pmid= 9054383 |doi=10.1074/jbc.272.11.6951  }}
}}
}}

Revision as of 19:46, 25 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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n/a

RefSeq (protein)

n/a

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

DNA-directed RNA polymerases I, II, and III subunit RPABC2 is a protein that in humans is encoded by the POLR2F gene.[1]

This gene encodes the sixth largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes, that is also shared by the other two DNA-directed RNA polymerases. In yeast, this polymerase subunit, in combination with at least two other subunits, forms a structure that stabilizes the transcribing polymerase on the DNA template.[2]

Interactions

POLR2F has been shown to interact with POLR2C.[3]

See also

References

  1. Pusch C, Wang Z, Roe B, Blin N (September 1996). "Genomic structure of the RNA polymerase II small subunit (hRPB14.4) locus (POLRF) and mapping to 22q13.1 by sequence identity". Genomics. 34 (3): 440–2. doi:10.1006/geno.1996.0312. PMID 8786150.
  2. "Entrez Gene: POLR2F polymerase (RNA) II (DNA directed) polypeptide F".
  3. Acker, J; de Graaff M; Cheynel I; Khazak V; Kedinger C; Vigneron M (July 1997). "Interactions between the human RNA polymerase II subunits". J. Biol. Chem. UNITED STATES. 272 (27): 16815–21. doi:10.1074/jbc.272.27.16815. ISSN 0021-9258. PMID 9201987.

Further reading