POLR2J

POLR2J
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	5FLM, 5IY9, 5IYA, 5IYC, 5IYB, 5IY7, 5IY8, 5IYD, 5IY6
Identifiers
Aliases	POLR2J, POLR2J1, RPB11, RPB11A, RPB11m, hRPB14, polymerase (RNA) II subunit J, RNA polymerase II subunit J
External IDs	OMIM: 604150; MGI: 109582; HomoloGene: 4542; GeneCards: POLR2J; OMA:POLR2J - orthologs
Gene location (Human)
Chr.	Chromosome 7 (human)
End	102,478,922 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	136,151,801 bp
RNA expression pattern
	Top expressed in
	gastrocnemius muscle; ; muscle of thigh; ; apex of heart; ; left ventricle; ; right auricle; ; left adrenal cortex; ; mucosa of transverse colon; ; substantia nigra; ; putamen; ; amygdala;
	Top expressed in
	yolk sac; ; zygote; ; embryo; ; morula; ; embryo; ; otic placode; ; internal carotid artery; ; ventricular zone; ; primary oocyte; ; epiblast;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	DNA binding; LRR domain binding; protein dimerization activity; DNA-directed 5'-3' RNA polymerase activity; protein binding; RNA polymerase II activity;
Cellular component	nucleoplasm; nucleus; RNA polymerase II, core complex;
Biological process	mRNA splicing, via spliceosome; transcription elongation from RNA polymerase II promoter; 7-methylguanosine mRNA capping; transcription-coupled nucleotide-excision repair; transcription initiation from RNA polymerase II promoter; snRNA transcription by RNA polymerase II; fibroblast growth factor receptor signaling pathway; RNA metabolic process; regulation of gene silencing by miRNA; transcription by RNA polymerase II; transcription, DNA-templated; somatic stem cell population maintenance; positive regulation of viral transcription;
	Sources:Amigo / QuickGO
Orthologs
	5439
	20022
	ENSG00000005075
	ENSMUSG00000039771
	P52435
	O08740
	NM_006234; NM_001371100; NM_001393919
	NM_011293
	NP_006225; NP_001358029
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

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.^[5]

Interactions

POLR2J has been shown to interact with:

Apoptosis antagonizing transcription factor,^[6]
POLR2C,^[7]^[8] and
SATB1.^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000005075 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000039771 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: POLR2J polymerase (RNA) II (DNA directed) polypeptide J, 13.3kDa".
^ 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. doi:10.1096/fasebj.14.7.904. PMID 10783144. S2CID 43175069.
^ 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.
^ 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. S2CID 30243193.
^ 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.

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. Bibcode:1998CBio....8.R447Y. doi:10.1016/S0960-9822(98)70289-1. PMID 9651670. S2CID 15480646.
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. S2CID 43685090.
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. S2CID 10931640.
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. PMC 7168390. 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.
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. Bibcode:1990Natur.345..640S. doi:10.1038/345640a0. PMID 2190099. S2CID 4233742.
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. Bibcode:1995PNAS...92.7153W. 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. doi:10.1128/JVI.69.3.1612-1620.1995. 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. Bibcode:1996PNAS...93.2505K. 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. doi:10.1128/JVI.70.7.4576-4584.1996. PMC 190394. PMID 8676484.
Fanciulli M, Bruno T, Cerboni C, Bonetto F, Iacobini C, Frati L, Piccoli M, Floridi A, Santoni A, Punturieri A (1996). "Cloning of a novel human RNA polymerase II subunit downregulated by doxorubicin: new potential mechanisms of drug related toxicity". FEBS Lett. 384 (1): 48–52. doi:10.1016/0014-5793(96)00277-3. PMID 8797801. S2CID 7809458.
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. Bibcode:1996Sci...274..605Z. doi:10.1126/science.274.5287.605. PMID 8849451. S2CID 13266489.
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. Bibcode:1996PNAS...9311575O. 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. Bibcode:1996Natur.384..375P. doi:10.1038/384375a0. PMID 8934526. S2CID 4278432.
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.
Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme". Mol. Cell. Biol. 17 (4): 1817–23. doi:10.1128/mcb.17.4.1817. PMC 232028. PMID 9121429.

This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000005075 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000039771 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] "Entrez Gene: POLR2J polymerase (RNA) II (DNA directed) polypeptide J, 13.3kDa".

[pmid10783144-6] 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. doi:10.1096/fasebj.14.7.904. PMID 10783144. S2CID 43175069.

[pmid9201987-7] 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.

[pmid12207009-8] 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. S2CID 30243193.

[pmid12036295-9] 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.

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[9]

Function

Interactions

References

Further reading