POLR2C

Polymerase (RNA) II (DNA directed) polypeptide C, 33kDa
Identifiers
Symbols	POLR2C ; RPB3; RPB31; hRPB33; hsRPB3
External IDs	OMIM: 180663 MGI: 109299 HomoloGene: 2017 GeneCards: POLR2C Gene
EC number	2.7.7.6
Gene ontology Molecular function • RNA polymerase II activity • DNA binding • protein dimerization activity Cellular component • nucleus • nucleoplasm • DNA-directed RNA polymerase II, core complex • cytoplasm • microtubule cytoskeleton Biological process • mRNA splicing, via spliceosome • DNA repair • transcription-coupled nucleotide-excision repair • nucleotide-excision repair • transcription from RNA polymerase II promoter • transcription initiation from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • 7-methylguanosine mRNA capping • RNA splicing • gene expression • viral process • piRNA metabolic process • somatic stem cell maintenance • positive regulation of viral transcription Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5432	20021
Ensembl	ENSG00000102978	ENSMUSG00000031783
UniProt	P19387	E9Q898
RefSeq (mRNA)	NM_002694	NM_009090
RefSeq (protein)	NP_116558	NP_033116
Location (UCSC)	Chr 16: 57.46 – 57.47 Mb	Chr 8: 94.86 – 94.86 Mb
PubMed search

DNA-directed RNA polymerase II subunit RPB3 is an enzyme that in humans is encoded by the POLR2C gene.^[1]

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.^[2]

Interactions

POLR2C has been shown to interact with:

• ATF4,^[3]
• CCHCR1,^[4]
• Myogenin,^[5]
• POLR2A,^[6]
• POLR2B,^[6]
• POLR2E^[6] and
• POLR2F,^[6]
• POLR2G,^[6]
• POLR2H,^[6]
• POLR2J,^[5][6]
• POLR2K,^[6]
• POLR2L,^[6] and
• TAF15.^[7]

References

1. 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.
2. "Entrez Gene: POLR2C polymerase (RNA) II (DNA directed) polypeptide C, 33kDa".
3. 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.
4. 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.
5. 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.
6. 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.
7. 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. 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.