POLR2H

Polymerase (RNA) II (DNA directed) polypeptide H

PDB rendering based on 2f3i.

Available structures
PDB	2f3i

Identifiers

Symbols

POLR2H; RPABC3; RPB17; RPB8; hsRPB8

External IDs

OMIM: 606023 MGI: 2384309 HomoloGene: 4540 GeneCards: POLR2H Gene

EC number

2.7.7.6

Gene Ontology
Molecular function	• DNA-directed RNA polymerase activity • protein kinase activity • protein binding • zinc ion binding
Cellular component	• nucleus • nucleoplasm • nucleoplasm • DNA-directed RNA polymerase II, core complex • nucleolus
Biological process	• nuclear mRNA splicing, via spliceosome • DNA repair • transcription-coupled nucleotide-excision repair • nucleotide-excision repair • transcription, DNA-dependent • transcription from RNA polymerase I promoter • transcription initiation from RNA polymerase I promoter • transcription elongation from RNA polymerase I promoter • termination of RNA polymerase I transcription • 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

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
184.08 – 184.09 Mb

Chr 16:
20.72 – 20.72 Mb

PubMed search

[1]

[2]

DNA-directed RNA polymerases I, II, and III subunit RPABC3 is a protein that in humans is encoded by the POLR2H gene.

This gene encodes one of the essential subunits of RNA polymerase II that is shared by the other two eukaryotic DNA-directed RNA polymerases, I and III.^[1]

Interactions

POLR2H has been shown to interact with POLR2C,^[2] POLR2G,^[2] POLR2A,^[2] POLR2B^[2] and POLR2E.^[2]

References

^ "Entrez Gene: POLR2H polymerase (RNA) II (DNA directed) polypeptide H". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5437.
^ ^a ^b ^c ^d ^e 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.
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. 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.
Freund E, McGuire PM (1986). "Characterization of RNA polymerase type II from human term placenta.". J. Cell. Physiol. 127 (3): 432–8. doi:10.1002/jcp.1041270312. PMID 3754875.
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.
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. PMC 230713. PMID 7651387. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230713.
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.
McKune K, Moore PA, Hull MW, Woychik NA (1996). "Six human RNA polymerase subunits functionally substitute for their yeast counterparts.". Mol. Cell. Biol. 15 (12): 6895–900. PMC 230944. PMID 8524256. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230944.
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.

PDB gallery

2f3i: Solution Structure of a Subunit of RNA Polymerase II

POLR2H

Interactions

References

Further reading