POLR2F

Polymerase (RNA) II (DNA directed) polypeptide F

PDB rendering based on 1qkl.

Available structures
PDB	1qkl

Identifiers

Symbols

POLR2F; HRBP14.4; POLRF; RPABC2; RPB14.4; RPB6

External IDs

OMIM: 604414 MGI: 1349393 HomoloGene: 7178 GeneCards: POLR2F Gene

EC number

2.7.7.6

Gene Ontology
Molecular function	• DNA binding • DNA-directed RNA polymerase activity • protein kinase activity
Cellular component	• nucleus • nucleoplasm • nucleoplasm • DNA-directed RNA polymerase II, core complex • nucleolus • RNA polymerase complex
Biological process	• nuclear mRNA splicing, via spliceosome • DNA repair • transcription-coupled nucleotide-excision repair • nucleotide-excision repair • transcription from RNA polymerase II promoter • transcription from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • mRNA capping • transcription from RNA polymerase III promoter • transcription elongation from RNA polymerase III promoter • termination of RNA polymerase III transcription • protein phosphorylation • RNA splicing • gene expression • viral reproduction • positive regulation of viral transcription
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 22:
38.35 – 38.44 Mb

Chr 15:
78.97 – 78.98 Mb

PubMed search

[1]

[2]

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]

1 Interactions
2 See also
3 References
4 Further reading

Interactions

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

References

^ Pusch C, Wang Z, Roe B, Blin N (Sep 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.
^ "Entrez Gene: POLR2F polymerase (RNA) II (DNA directed) polypeptide F". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5435.
^ Acker, J; de Graaff M, Cheynel I, Khazak V, Kedinger C, Vigneron M (Jul. 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.

Jeang KT (1998). "Tat, Tat-associated kinase, and transcription.". J. Biomed. Sci. 5 (1): 24–7. doi:10.1007/BF02253352. PMID 9570510.
Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation.". Curr. Biol. 8 (13): R447–9. doi:10.1016/S0960-9822(98)70289-1. 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. doi:10.1002/(SICI)1097-4644(19991201)75:3<357::AID-JCB1>3.0.CO;2-K. 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. doi:10.1080/152165401753544241. 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. doi:10.2174/138945006779025338. 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. doi:10.1101/gad.6.4.655. PMID 1559613.
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.
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. doi:10.1073/pnas.92.16.7153. PMC 41297. PMID 7638159. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=41297.
Acker J, Wintzerith M, Vigneron M, Kedinger C (1995). "A 14.4 KDa acidic subunit of human RNA polymerase II with a putative leucine-zipper". DNA Seq. 4 (5): 329–31. doi:10.3109/10425179409020860. PMID 7803819.
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. PMC 188757. PMID 7853496. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=188757.
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. doi:10.1073/pnas.93.6.2505. PMC 39827. PMID 8637904. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=39827.
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. PMC 190394. PMID 8676484. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=190394.
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. doi:10.1126/science.274.5287.605. 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. doi:10.1073/pnas.93.21.11575. PMC 38099. PMID 8876177. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=38099.
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. doi:10.1074/jbc.271.44.27888. PMID 8910388.
Parada CA, Roeder RG (1996). "Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain". Nature 384 (6607): 375–8. doi:10.1038/384375a0. PMID 8934526.
García-Martínez LF, Ivanov D, Gaynor RB (1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes". J. Biol. Chem. 272 (11): 6951–8. doi:10.1074/jbc.272.11.6951. PMID 9054383.

PDB gallery

1qkl: HRPABC14.4, ESSENTIAL SUBUNIT OF HUMAN RNA POLYMERASES I, II AND III

POLR2F

Contents

Interactions

See also

References

Further reading