POLR2K

From Wikipedia, the free encyclopedia

Polymerase (RNA) II (DNA directed) polypeptide K, 7.0kDa

Identifiers

POLR2K; ABC10-alpha; RPABC4; RPB10alpha; RPB12; RPB7.0; hRPB7.0; hsRPB10a

External IDs

OMIM: 606033 MGI: 102725 HomoloGene: 86049

Gene ontology
Molecular Function:	• DNA binding • DNA-directed RNA polymerase activity • zinc ion binding • transferase activity • metal ion binding
Cellular Component:	• nucleus • DNA-directed RNA polymerase II, core complex • DNA-directed RNA polymerase III complex
Biological Process:	• transcription • regulation of transcription from RNA polymerase I promoter • transcription from RNA polymerase II promoter • transcription from RNA polymerase III promoter

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005034 (mRNA)
NP_005025 (protein)

NM_001039368 (mRNA)
NP_001034457 (protein)

Location

Chr 8: 101.23 - 101.24 Mb

Chr 15: 36.12 - 36.12 Mb

Pubmed search

[1]

[2]

Polymerase (RNA) II (DNA directed) polypeptide K, 7.0kDa, also known as POLR2K, is a human gene.

This gene encodes one of the smallest subunits 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.^[1]

[edit] References

^ Entrez Gene: POLR2K polymerase (RNA) II (DNA directed) polypeptide K, 7.0kDa.

[edit] 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.
Howe KJ (2002). "RNA polymerase II conducts a symphony of pre-mRNA processing activities.". Biochim. Biophys. Acta 1577 (2): 308–24. PMID 12213660.
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.
Jang KL, Collins MK, Latchman DS (1992). "The human immunodeficiency virus tat protein increases the transcription of human Alu repeated sequences by increasing the activity of the cellular transcription factor TFIIIC.". J. Acquir. Immune Defic. Syndr. 5 (11): 1142–7. PMID 1403646.
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.
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. PMID 7638159.
Shpakovski GV, Acker J, Wintzerith M, et al. (1995). "Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae.". Mol. Cell. Biol. 15 (9): 4702–10. PMID 7651387.
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.
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.
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.