POLR2J: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''DNA-directed RNA polymerase II subunit RPB11-a''' is an [[enzyme]] that in humans is encoded by the ''POLR2J'' [[gene]].
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Polymerase (RNA) II (DNA directed) polypeptide J, 13.3kDa
| HGNCid = 9197
| Symbol = POLR2J
| AltSymbols =; MGC71910; POLR2J1; RPB11; RPB11A; RPB11m; hRPB14
| OMIM = 604150
| ECnumber = 
| Homologene = 4542
| MGIid = 109582
| GeneAtlas_image1 = PBB_GE_POLR2J_212782_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003899 |text = DNA-directed RNA polymerase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005665 |text = DNA-directed RNA polymerase II, core complex}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5439
    | Hs_Ensembl = ENSG00000005075
    | Hs_RefseqProtein = XP_001126227
    | Hs_RefseqmRNA = XM_001126227
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 101900555
    | Hs_GenLoc_end = 101906386
    | Hs_Uniprot = P52435
    | Mm_EntrezGene = 20022
    | Mm_Ensembl = ENSMUSG00000039771
    | Mm_RefseqmRNA = NM_011293
    | Mm_RefseqProtein = NP_035423
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 136401361
    | Mm_GenLoc_end = 136407566
    | Mm_Uniprot = Q3TYI2
  }}
}}
'''Polymerase (RNA) II (DNA directed) polypeptide J, 13.3kDa''', also known as '''POLR2J''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene exists as a heterodimer with another polymerase subunit; together they form a core subassembly unit of the polymerase. Two similar genes are located nearby on chromosome 7q22.1 and a pseudogene is found on chromosome 7p13.<ref>{{cite web | title = Entrez Gene: POLR2J polymerase (RNA) II (DNA directed) polypeptide J, 13.3kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5439| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene exists as a heterodimer with another polymerase subunit; together they form a core subassembly unit of the polymerase. Two similar genes are located nearby on chromosome 7q22.1 and a pseudogene is found on chromosome 7p13.<ref>{{cite web | title = Entrez Gene: POLR2J polymerase (RNA) II (DNA directed) polypeptide J, 13.3kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5439| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
POLR2J has been shown to [[Protein-protein interaction|interact]] with:
{{refbegin | 2}}
* [[Apoptosis antagonizing transcription factor]],<ref name = pmid10783144>{{cite journal | vauthors = Fanciulli M, Bruno T, Di Padova M, De Angelis R, Iezzi S, Iacobini C, Floridi A, Passananti C | title = Identification of a novel partner of RNA polymerase II subunit 11, Che-1, which interacts with and affects the growth suppression function of Rb | journal = FASEB J. | volume = 14 | issue = 7 | pages = 904–12 | date = May 2000 | pmid = 10783144 | doi =  }}</ref>
{{PBB_Further_reading
* [[POLR2C]],<ref name = pmid9201987>{{cite journal | vauthors = Acker J, de Graaff M, Cheynel I, Khazak V, Kedinger C, Vigneron M | title = Interactions between the human RNA polymerase II subunits | journal = J. Biol. Chem. | volume = 272 | issue = 27 | pages = 16815–21 | date = July 1997 | pmid = 9201987 | doi =  10.1074/jbc.272.27.16815}}</ref><ref name = pmid12207009>{{cite journal | vauthors = Corbi N, Di Padova M, De Angelis R, Bruno T, Libri V, Iezzi S, Floridi A, Fanciulli M, Passananti C | title = 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 | journal = FASEB J. | volume = 16 | issue = 12 | pages = 1639–41 | date = October 2002 | pmid = 12207009 | doi = 10.1096/fj.02-0123fje }}</ref>  and
| citations =  
* [[SATB1]].<ref name = pmid12036295>{{cite journal | vauthors = Durrin LK, Krontiris TG | title = The thymocyte-specific MAR binding protein, SATB1, interacts in vitro with a novel variant of DNA-directed RNA polymerase II, subunit 11 | journal = Genomics | volume = 79 | issue = 6 | pages = 809–17 | date = June 2002 | pmid = 12036295 | doi = 10.1006/geno.2002.6772 }}</ref>
*{{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=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=  }}
== References ==
*{{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= }}
{{reflist}}
*{{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= }}
{{Clear}}
*{{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 | 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= }}
== Further reading ==
*{{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= }}
{{refbegin|35em}}
*{{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 = 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=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 = 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=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 = Romano G, Kasten M, De Falco G, Micheli P, Khalili K, Giordano A | 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=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 = 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=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 = 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=Fanciulli M, Bruno T, Cerboni C, ''et al.'' |title=Cloning of a novel human RNA polymerase II subunit downregulated by doxorubicin: new potential mechanisms of drug related toxicity. |journal=FEBS Lett. |volume=384 |issue= 1 |pages= 48-52 |year= 1996 |pmid= 8797801 |doi= }}
* {{cite journal | vauthors = Harrich D, McMillan N, Munoz L, Apolloni A, Meredith L | 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=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 = Kato H, Sumimoto H, Pognonec P, Chen CH, Rosen CA, Roeder RG | 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=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 = 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 | 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 = 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 | pmc = 41297 | doi = 10.1073/pnas.92.16.7153 }}
*{{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 = 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 | pmc = 188757 | doi = }}
*{{cite journal | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
* {{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 | pmc = 39827 | doi = 10.1073/pnas.93.6.2505 }}
*{{cite journal | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |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 | pmc = 190394 | doi =  }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi=  }}
* {{cite journal | vauthors = Fanciulli M, Bruno T, Cerboni C, Bonetto F, Iacobini C, Frati L, Piccoli M, Floridi A, Santoni A, Punturieri A | title = Cloning of a novel human RNA polymerase II subunit downregulated by doxorubicin: new potential mechanisms of drug related toxicity | journal = FEBS Lett. | volume = 384 | issue = 1 | pages = 48–52 | year = 1996 | pmid = 8797801 | doi = 10.1016/0014-5793(96)00277-3 }}
}}
* {{cite journal | vauthors = Agostini I, Navarro JM, Rey F, Bouhamdan M, Spire B, Vigne R, Sire J | 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 = 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 }}
* {{cite journal | vauthors = Okamoto H, Sheline CT, Corden JL, Jones KA, Peterlin BM | 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 | pmc = 38099 | doi = 10.1073/pnas.93.21.11575 }}
* {{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 }}
* {{cite journal | vauthors = Parada CA, Roeder RG | title = Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain | journal = Nature | volume = 384 | issue = 6607 | pages = 375–8 | year = 1996 | pmid = 8934526 | doi = 10.1038/384375a0 }}
* {{cite journal | vauthors = García-Martínez LF, Ivanov D, Gaynor RB | title = Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes | journal = J. Biol. Chem. | volume = 272 | issue = 11 | pages = 6951–8 | year = 1997 | pmid = 9054383 | doi = 10.1074/jbc.272.11.6951 }}
* {{cite journal | vauthors = Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM | title = The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme | journal = Mol. Cell. Biol. | volume = 17 | issue = 4 | pages = 1817–23 | year = 1997 | pmid = 9121429 | pmc = 232028 | doi =  }}
{{refend}}
{{refend}}


{{protein-stub}}
 
{{WikiDoc Sources}}
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Latest revision as of 00:23, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

DNA-directed RNA polymerase II subunit RPB11-a is an enzyme that in humans is encoded by the POLR2J gene.

Function

This gene encodes a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene exists as a heterodimer with another polymerase subunit; together they form a core subassembly unit of the polymerase. Two similar genes are located nearby on chromosome 7q22.1 and a pseudogene is found on chromosome 7p13.[1]

Interactions

POLR2J has been shown to interact with:

References

  1. "Entrez Gene: POLR2J polymerase (RNA) II (DNA directed) polypeptide J, 13.3kDa".
  2. Fanciulli M, Bruno T, Di Padova M, De Angelis R, Iezzi S, Iacobini C, Floridi A, Passananti C (May 2000). "Identification of a novel partner of RNA polymerase II subunit 11, Che-1, which interacts with and affects the growth suppression function of Rb". FASEB J. 14 (7): 904–12. PMID 10783144.
  3. 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. 272 (27): 16815–21. doi:10.1074/jbc.272.27.16815. PMID 9201987.
  4. Corbi N, Di Padova M, De Angelis R, Bruno T, Libri V, Iezzi S, Floridi A, Fanciulli M, Passananti C (October 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.
  5. Durrin LK, Krontiris TG (June 2002). "The thymocyte-specific MAR binding protein, SATB1, interacts in vitro with a novel variant of DNA-directed RNA polymerase II, subunit 11". Genomics. 79 (6): 809–17. doi:10.1006/geno.2002.6772. PMID 12036295.

Further reading