POLR2C

POLR2C
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPOLR2C, RPB3, RPB31, hRPB33, hsRPB3, polymerase (RNA) II subunit C, RNA polymerase II subunit C
External IDsMGI: 109299 HomoloGene: 2017 GeneCards: POLR2C
Gene location (Human)
Chr.Chromosome 16 (human)[1]
Band16q21Start57,462,387 bp[1]
End57,472,010 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

5432

20021

Ensembl

ENSG00000102978

ENSMUSG00000031783

UniProt

P19387
Q6FGR6

P97760

RefSeq (mRNA)

NM_002694
NM_032940

NM_009090

RefSeq (protein)

NP_116558
NP_116558.1

NP_033116

Location (UCSC)Chr 16: 57.46 – 57.47 MbChr 8: 94.86 – 94.87 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DNA-directed RNA polymerase II subunit RPB3 is an enzyme that in humans is encoded by the POLR2C gene.[5]

Function

This gene encodes the third largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a cysteine rich region and exists as a heterodimer with another polymerase subunit, POLR2J. These two subunits form a core subassembly unit of the polymerase. A pseudogene has been identified on chromosome 21.[6]

Interactions

POLR2C has been shown to interact with:

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000102978 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031783 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Acker J, Mattei MG, Wintzerith M, Roeckel N, Depetris D, Vigneron M, Kedinger C (Aug 1994). "Chromosomal localization of human RNA polymerase II subunit genes". Genomics. 20 (3): 496–9. doi:10.1006/geno.1994.1208. PMID 8034326.
  6. ↑ "Entrez Gene: POLR2C polymerase (RNA) II (DNA directed) polypeptide C, 33kDa".
  7. ↑ De Angelis R, Iezzi S, Bruno T, Corbi N, Di Padova M, Floridi A, Fanciulli M, Passananti C (Jul 2003). "Functional interaction of the subunit 3 of RNA polymerase II (RPB3) with transcription factor-4 (ATF4)". FEBS Lett. 547 (1–3): 15–9. doi:10.1016/s0014-5793(03)00659-8. PMID 12860379.
  8. ↑ Corbi N, Bruno T, De Angelis R, Di Padova M, Libri V, Di Certo MG, Spinardi L, Floridi A, Fanciulli M, Passananti C (Sep 2005). "RNA polymerase II subunit 3 is retained in the cytoplasm by its interaction with HCR, the psoriasis vulgaris candidate gene product". J. Cell Sci. 118 (Pt 18): 4253–60. doi:10.1242/jcs.02545. PMID 16141233.
  9. 1 2 Corbi N, Di Padova M, De Angelis R, Bruno T, Libri V, Iezzi S, Floridi A, Fanciulli M, Passananti C (Oct 2002). "The alpha-like RNA polymerase II core subunit 3 (RPB3) is involved in tissue-specific transcription and muscle differentiation via interaction with the myogenic factor myogenin". FASEB J. 16 (12): 1639–41. doi:10.1096/fj.02-0123fje. PMID 12207009.
  10. 1 2 3 4 5 6 7 8 9 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. 272 (27): 16815–21. doi:10.1074/jbc.272.27.16815. PMID 9201987.
  11. ↑ Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (Mar 1998). "EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes". Mol. Cell. Biol. 18 (3): 1489–97. doi:10.1128/mcb.18.3.1489. PMC 108863. PMID 9488465.

Further reading

  • 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, Micheli P, Khalili K, Giordano A (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, Apolloni A, Meredith L (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, Chen CH, Rosen CA, Roeder RG (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.
  • Pati UK, Weissman SM (1990). "The amino acid sequence of the human RNA polymerase II 33-kDa subunit hRPB 33 is highly conserved among eukaryotes". J. Biol. Chem. 265 (15): 8400–3. PMID 2187864.
  • 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.
  • 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.
  • 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.
  • 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.
  • Agostini I, Navarro JM, Rey F, Bouhamdan M, Spire B, Vigne R, Sire J (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, Jones KA, Peterlin BM (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.
  • 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.


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