POLR2B: Difference between revisions

Jump to navigation Jump to search
m (Bot: HTTP→HTTPS (v470))
m (1 revision imported)
 
(One intermediate revision by one other user not shown)
Line 25: Line 25:
*{{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=Zheng XM, Black D, Chambon P, Egly JM |title=Sequencing and expression of complementary DNA for the general transcription factor BTF3 |journal=Nature |volume=344 |issue= 6266 |pages= 556–9 |year= 1990 |pmid= 2320128 |doi= 10.1038/344556a0 }}
*{{cite journal  |vauthors=Zheng XM, Black D, Chambon P, Egly JM |title=Sequencing and expression of complementary DNA for the general transcription factor BTF3 |journal=Nature |volume=344 |issue= 6266 |pages= 556–9 |year= 1990 |pmid= 2320128 |doi= 10.1038/344556a0 |bibcode=1990Natur.344..556Z }}
*{{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=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  | author=Andersson B |title=A "double adaptor" method for improved shotgun library construction |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138  |name-list-format=vanc| author2=Wentland MA  | author3=Ricafrente JY  | display-authors=3  | last4=Liu  | first4=W  | last5=Gibbs  | first5=RA }}
*{{cite journal  | author=Andersson B |title=A "double adaptor" method for improved shotgun library construction |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138  |name-list-format=vanc| author2=Wentland MA  | author3=Ricafrente JY  | display-authors=3  | last4=Liu  | first4=W  | last5=Gibbs  | first5=RA }}
*{{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  }}
}}
}}

Latest revision as of 12:01, 10 January 2019

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

n/a

n/a

RefSeq (protein)

n/a

n/a

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

DNA-directed RNA polymerase II subunit RPB2 is an enzyme that in humans is encoded by the POLR2B gene.[1][2]

This gene encodes the second largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. This subunit, in combination with at least two other polymerase subunits, forms a structure within the polymerase that maintains contact in the active site of the enzyme between the DNA template and the newly synthesized RNA.[3]

Interactions

POLR2B has been shown to interact with POLR2C,[4] POLR2E,[4] POLR2H[4] and POLR2L.[4]

References

  1. Acker J, Wintzerith M, Vigneron M, Kedinger C (October 1992). "Primary structure of the second largest subunit of human RNA polymerase II (or B)". J Mol Biol. 226 (4): 1295–9. doi:10.1016/0022-2836(92)91071-V. PMID 1518060.
  2. Acker J, Mattei MG, Wintzerith M, Roeckel N, Depetris D, Vigneron M, Kedinger C (August 1994). "Chromosomal localization of human RNA polymerase II subunit genes". Genomics. 20 (3): 496–9. doi:10.1006/geno.1994.1208. PMID 8034326.
  3. "Entrez Gene: POLR2B polymerase (RNA) II (DNA directed) polypeptide B, 140kDa".
  4. 4.0 4.1 4.2 4.3 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