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{{Infobox_gene}}
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'''DNA-directed RNA polymerases I, II, and III subunit RPABC3''' is a [[protein]] that in humans is encoded by the ''POLR2H'' [[gene]].
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{{GNF_Protein_box
| image = PBB_Protein_POLR2H_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2f3i.
| PDB = {{PDB2|2f3i}}
| Name = Polymerase (RNA) II (DNA directed) polypeptide H
| HGNCid = 9195
| Symbol = POLR2H
| AltSymbols =; RPABC3; RPB17; RPB8; hsRPB8
| OMIM = 606023
| ECnumber = 
| Homologene = 4540
| MGIid = 2384309
| GeneAtlas_image1 = PBB_GE_POLR2H_209302_at_tn.png
| GeneAtlas_image2 = PBB_GE_POLR2H_gnf1h07731_at_tn.png
| Function = {{GNF_GO|id=GO:0003899 |text = DNA-directed RNA polymerase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5437
    | Hs_Ensembl = ENSG00000163882
    | Hs_RefseqProtein = NP_006223
    | Hs_RefseqmRNA = NM_006232
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 185562254
    | Hs_GenLoc_end = 185568989
    | Hs_Uniprot = P52434
    | Mm_EntrezGene = 245841
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_145632
    | Mm_RefseqProtein = NP_663607
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Polymerase (RNA) II (DNA directed) polypeptide H''', also known as '''POLR2H''', is a human [[gene]].


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: POLR2H polymerase (RNA) II (DNA directed) polypeptide H| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5437| accessdate = }}</ref>
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: POLR2H polymerase (RNA) II (DNA directed) polypeptide H| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5437| accessdate = }}</ref>
}}
}}
==Interactions==
POLR2H has been shown to [[Protein-protein interaction|interact]] with [[POLR2C]],<ref name=pmid9201987>{{cite journal |doi=10.1074/jbc.272.27.16815 |last=Acker |first=J |authorlink= |author2=de Graaff M |author3=Cheynel I |author4=Khazak V |author5=Kedinger C |author6=Vigneron M  |date=July 1997  |title=Interactions between the human RNA polymerase II subunits |journal=J. Biol. Chem. |volume=272 |issue=27 |pages=16815–21 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9201987 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[POLR2G]],<ref name=pmid9201987/> [[POLR2A]],<ref name=pmid9201987/> [[POLR2B]]<ref name=pmid9201987/> and [[POLR2E]].<ref name=pmid9201987/>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24-7 |year= 1998 |pmid= 9570510 |doi=  }}
*{{cite journal  | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24–7 |year= 1998 |pmid= 9570510 |doi=10.1007/BF02253352 }}
*{{cite journal  | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447-9 |year= 1998 |pmid= 9651670 |doi=  }}
*{{cite journal  |vauthors=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447–9 |year= 1998 |pmid= 9651670 |doi=10.1016/S0960-9822(98)70289-1 }}
*{{cite journal | author=Romano G, Kasten M, De Falco G, ''et al.'' |title=Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression. |journal=J. Cell. Biochem. |volume=75 |issue= 3 |pages= 357-68 |year= 2000 |pmid= 10536359 |doi= }}
*{{cite journal   |vauthors=Romano G, Kasten M, De Falco G, etal |title=Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression. |journal=J. Cell. Biochem. |volume=75 |issue= 3 |pages= 357–68 |year= 2000 |pmid= 10536359 |doi=10.1002/(SICI)1097-4644(19991201)75:3<357::AID-JCB1>3.0.CO;2-K  }}
*{{cite journal  | author=Marcello A, Zoppé M, Giacca M |title=Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator. |journal=IUBMB Life |volume=51 |issue= 3 |pages= 175-81 |year= 2002 |pmid= 11547919 |doi=  }}
*{{cite journal  |vauthors=Marcello A, Zoppé M, Giacca M |title=Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator. |journal=IUBMB Life |volume=51 |issue= 3 |pages= 175–81 |year= 2002 |pmid= 11547919 |doi=10.1080/152165401753544241 }}
*{{cite journal  | author=Stevens M, De Clercq E, Balzarini J |title=The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention. |journal=Med Res Rev |volume=26 |issue= 5 |pages= 595-625 |year= 2007 |pmid= 16838299 |doi= 10.1002/med.20081 }}
*{{cite journal  |vauthors=Stevens M, De Clercq E, Balzarini J |title=The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention. |journal=Med Res Rev |volume=26 |issue= 5 |pages= 595–625 |year= 2007 |pmid= 16838299 |doi= 10.1002/med.20081 }}
*{{cite journal | author=Harrich D, McMillan N, Munoz L, ''et al.'' |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595-606 |year= 2007 |pmid= 17168834 |doi=  }}
*{{cite journal   |vauthors=Harrich D, McMillan N, Munoz L, etal |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595–606 |year= 2007 |pmid= 17168834 |doi=10.2174/138945006779025338 }}
*{{cite journal  | author=Jang KL, Collins MK, Latchman DS |title=The human immunodeficiency virus tat protein increases the transcription of human Alu repeated sequences by increasing the activity of the cellular transcription factor TFIIIC. |journal=J. Acquir. Immune Defic. Syndr. |volume=5 |issue= 11 |pages= 1142-7 |year= 1992 |pmid= 1403646 |doi=  }}
*{{cite journal  |vauthors=Jang KL, Collins MK, Latchman DS |title=The human immunodeficiency virus tat protein increases the transcription of human Alu repeated sequences by increasing the activity of the cellular transcription factor TFIIIC. |journal=J. Acquir. Immune Defic. Syndr. |volume=5 |issue= 11 |pages= 1142–7 |year= 1992 |pmid= 1403646 |doi=  }}
*{{cite journal | author=Kato H, Sumimoto H, Pognonec P, ''et al.'' |title=HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors. |journal=Genes Dev. |volume=6 |issue= 4 |pages= 655-66 |year= 1992 |pmid= 1559613 |doi=  }}
*{{cite journal   |vauthors=Kato H, Sumimoto H, Pognonec P, etal |title=HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors. |journal=Genes Dev. |volume=6 |issue= 4 |pages= 655–66 |year= 1992 |pmid= 1559613 |doi=10.1101/gad.6.4.655 }}
*{{cite journal  | author=Southgate C, Zapp ML, Green MR |title=Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein. |journal=Nature |volume=345 |issue= 6276 |pages= 640-2 |year= 1990 |pmid= 2190099 |doi= 10.1038/345640a0 }}
*{{cite journal  |vauthors=Southgate C, Zapp ML, Green MR |title=Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein. |journal=Nature |volume=345 |issue= 6276 |pages= 640–2 |year= 1990 |pmid= 2190099 |doi= 10.1038/345640a0 |bibcode=1990Natur.345..640S }}
*{{cite journal  | author=Freund E, McGuire PM |title=Characterization of RNA polymerase type II from human term placenta. |journal=J. Cell. Physiol. |volume=127 |issue= 3 |pages= 432-8 |year= 1986 |pmid= 3754875 |doi= 10.1002/jcp.1041270312 }}
*{{cite journal  |vauthors=Freund E, McGuire PM |title=Characterization of RNA polymerase type II from human term placenta. |journal=J. Cell. Physiol. |volume=127 |issue= 3 |pages= 432–8 |year= 1986 |pmid= 3754875 |doi= 10.1002/jcp.1041270312 }}
*{{cite journal  | author=Wu-Baer F, Sigman D, Gaynor RB |title=Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 16 |pages= 7153-7 |year= 1995 |pmid= 7638159 |doi=  }}
*{{cite journal  |vauthors=Wu-Baer F, Sigman D, Gaynor RB |title=Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 16 |pages= 7153–7 |year= 1995 |pmid= 7638159 |doi=10.1073/pnas.92.16.7153  | pmc=41297 |bibcode=1995PNAS...92.7153W }}
*{{cite journal | author=Shpakovski GV, Acker J, Wintzerith M, ''et al.'' |title=Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae. |journal=Mol. Cell. Biol. |volume=15 |issue= 9 |pages= 4702-10 |year= 1995 |pmid= 7651387 |doi=  }}
*{{cite journal   |vauthors=Shpakovski GV, Acker J, Wintzerith M, etal |title=Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae. |journal=Mol. Cell. Biol. |volume=15 |issue= 9 |pages= 4702–10 |year= 1995 |pmid= 7651387 |doi= | pmc=230713 }}
*{{cite journal  | author=Herrmann CH, Rice AP |title=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. |journal=J. Virol. |volume=69 |issue= 3 |pages= 1612-20 |year= 1995 |pmid= 7853496 |doi=  }}
*{{cite journal  |vauthors=Herrmann CH, Rice AP |title=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. |journal=J. Virol. |volume=69 |issue= 3 |pages= 1612–20 |year= 1995 |pmid= 7853496 |doi= | pmc=188757 }}
*{{cite journal  | author=McKune K, Moore PA, Hull MW, Woychik NA |title=Six human RNA polymerase subunits functionally substitute for their yeast counterparts. |journal=Mol. Cell. Biol. |volume=15 |issue= 12 |pages= 6895-900 |year= 1996 |pmid= 8524256 |doi=  }}
*{{cite journal  |vauthors=McKune K, Moore PA, Hull MW, Woychik NA |title=Six human RNA polymerase subunits functionally substitute for their yeast counterparts. |journal=Mol. Cell. Biol. |volume=15 |issue= 12 |pages= 6895–900 |year= 1996 |pmid= 8524256 |doi= | pmc=230944 }}
*{{cite journal  | author=Keen NJ, Gait MJ, Karn J |title=Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 6 |pages= 2505-10 |year= 1996 |pmid= 8637904 |doi=  }}
*{{cite journal  |vauthors=Keen NJ, Gait MJ, Karn J |title=Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 6 |pages= 2505–10 |year= 1996 |pmid= 8637904 |doi=10.1073/pnas.93.6.2505 | pmc=39827  |bibcode=1996PNAS...93.2505K }}
*{{cite journal  | author=Yang X, Herrmann CH, Rice AP |title=The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function. |journal=J. Virol. |volume=70 |issue= 7 |pages= 4576-84 |year= 1996 |pmid= 8676484 |doi=  }}
*{{cite journal  |vauthors=Yang X, Herrmann CH, Rice AP |title=The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function. |journal=J. Virol. |volume=70 |issue= 7 |pages= 4576–84 |year= 1996 |pmid= 8676484 |doi= | pmc=190394 }}
*{{cite journal | author=Agostini I, Navarro JM, Rey F, ''et al.'' |title=The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB. |journal=J. Mol. Biol. |volume=261 |issue= 5 |pages= 599-606 |year= 1996 |pmid= 8800208 |doi= 10.1006/jmbi.1996.0485 }}
*{{cite journal   |vauthors=Agostini I, Navarro JM, Rey F, etal |title=The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB. |journal=J. Mol. Biol. |volume=261 |issue= 5 |pages= 599–606 |year= 1996 |pmid= 8800208 |doi= 10.1006/jmbi.1996.0485 }}
*{{cite journal  | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
*{{cite journal  |vauthors=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605–10 |year= 1996 |pmid= 8849451 |doi=10.1126/science.274.5287.605  |bibcode=1996Sci...274..605Z }}
*{{cite journal | author=Okamoto H, Sheline CT, Corden JL, ''et al.'' |title=Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 21 |pages= 11575-9 |year= 1996 |pmid= 8876177 |doi=  }}
*{{cite journal   |vauthors=Okamoto H, Sheline CT, Corden JL, etal |title=Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 21 |pages= 11575–9 |year= 1996 |pmid= 8876177 |doi=10.1073/pnas.93.21.11575  | pmc=38099 |bibcode=1996PNAS...9311575O }}
*{{cite journal  | author=Chun RF, Jeang KT |title=Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27888-94 |year= 1996 |pmid= 8910388 |doi=  }}
*{{cite journal  |vauthors=Chun RF, Jeang KT |title=Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27888–94 |year= 1996 |pmid= 8910388 |doi=10.1074/jbc.271.44.27888 }}
}}
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{{refend}}
{{PDB Gallery|geneid=5437}}
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Latest revision as of 19:46, 25 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ "Entrez Gene: POLR2H polymerase (RNA) II (DNA directed) polypeptide H".
  2. ↑ 2.0 2.1 2.2 2.3 2.4 Acker, J; de Graaff M; Cheynel I; Khazak V; Kedinger C; Vigneron M (July 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.

Further reading



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