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POLR2A

January 01, 1970

DNA-directed RNA polymerase II subunit RPB1, also known as RPB1, is an enzyme that is encoded by the POLR2A gene in humans.

POLR2A
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPOLR2A, POLR2, POLRA, RPB1, RPBh1, RPO2, RPOL2, RpIILS, hRPB220, hsRPB1, polymerase (RNA) II subunit A, RNA polymerase II subunit A, NEDHIB
External IDsOMIM: 180660 MGI: 98086 HomoloGene: 721 GeneCards: POLR2A
EC number2.7.7.48
Orthologs
SpeciesHumanMouse
Entrez

5430

20020

Ensembl

ENSG00000284832
ENSG00000181222

ENSMUSG00000005198

UniProt

P24928

P08775

RefSeq (mRNA)

NM_000937

NM_009089
NM_001291068

RefSeq (protein)

NP_000928

NP_001277997

Location (UCSC)Chr 17: 7.48 – 7.51 MbChr 11: 69.62 – 69.65 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function edit

This gene encodes the largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a carboxy terminal domain composed of heptapeptide repeats that are essential for polymerase activity. These repeats contain serine and threonine residues that are phosphorylated in actively transcribing RNA polymerase. In addition, this subunit, in combination with several other polymerase subunits, forms the DNA-binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA.[5]

Interactions edit

POLR2A has been shown to interact with:

References edit

  1. ^ a b c ENSG00000181222 GRCh38: Ensembl release 89: ENSG00000284832, ENSG00000181222 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005198 – 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: POLR2A polymerase (RNA) II (DNA directed) polypeptide A, 220kDa".
  6. ^ Krum SA, Miranda GA, Lin C, Lane TF (December 2003). "BRCA1 associates with processive RNA polymerase II". J. Biol. Chem. 278 (52): 52012–20. doi:10.1074/jbc.M308418200. PMID 14506230.
  7. ^ a b c d e f g h Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD (May 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5605–10. Bibcode:1997PNAS...94.5605S. doi:10.1073/pnas.94.11.5605. PMC 20825. PMID 9159119.
  8. ^ Chiba N, Parvin JD (October 2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage". J. Biol. Chem. 276 (42): 38549–54. doi:10.1074/jbc.M105227200. PMID 11504724.
  9. ^ Krum SA, Womack JE, Lane TF (September 2003). "Bovine BRCA1 shows classic responses to genotoxic stress but low in vitro transcriptional activation activity". Oncogene. 22 (38): 6032–44. doi:10.1038/sj.onc.1206515. PMID 12955082.
  10. ^ a b c d e f g Cho H, Orphanides G, Sun X, Yang XJ, Ogryzko V, Lees E, Nakatani Y, Reinberg D (September 1998). "A human RNA polymerase II complex containing factors that modify chromatin structure". Mol. Cell. Biol. 18 (9): 5355–63. doi:10.1128/MCB.18.9.5355. PMC 109120. PMID 9710619.
  11. ^ Suñé C, Hayashi T, Liu Y, Lane WS, Young RA, Garcia-Blanco MA (October 1997). "CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription". Mol. Cell. Biol. 17 (10): 6029–39. doi:10.1128/MCB.17.10.6029. PMC 232452. PMID 9315662.
  12. ^ Sato S, Tomomori-Sato C, Parmely TJ, Florens L, Zybailov B, Swanson SK, Banks CA, Jin J, Cai Y, Washburn MP, Conaway JW, Conaway RC (June 2004). "A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology". Mol. Cell. 14 (5): 685–91. doi:10.1016/j.molcel.2004.05.006. PMID 15175163.
  13. ^ a b c d 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.
  14. ^ Humbert S, Saudou F (May 2002). "Toward cell specificity in SCA1". Neuron. 34 (5): 669–70. doi:10.1016/s0896-6273(02)00715-8. PMID 12062012. S2CID 15993809.
  15. ^ a b c Sif S, Saurin AJ, Imbalzano AN, Kingston RE (March 2001). "Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes". Genes Dev. 15 (5): 603–18. doi:10.1101/gad.872801. PMC 312641. PMID 11238380.
  16. ^ a b c Wang W, Côté J, Xue Y, Zhou S, Khavari PA, Biggar SR, Muchardt C, Kalpana GV, Goff SP, Yaniv M, Workman JL, Crabtree GR (October 1996). "Purification and biochemical heterogeneity of the mammalian SWI-SNF complex". EMBO J. 15 (19): 5370–82. doi:10.1002/j.1460-2075.1996.tb00921.x. PMC 452280. PMID 8895581.
  17. ^ Zhao K, Wang W, Rando OJ, Xue Y, Swiderek K, Kuo A, Crabtree GR (November 1998). "Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling". Cell. 95 (5): 625–36. doi:10.1016/s0092-8674(00)81633-5. PMID 9845365. S2CID 3184211.
  18. ^ Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, Li M, Yagyu R, Nakamura Y (August 2004). "SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells". Nat. Cell Biol. 6 (8): 731–40. doi:10.1038/ncb1151. PMID 15235609. S2CID 13456531.
  19. ^ Yang J, Aittomäki S, Pesu M, Carter K, Saarinen J, Kalkkinen N, Kieff E, Silvennoinen O (September 2002). "Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II". EMBO J. 21 (18): 4950–8. doi:10.1093/emboj/cdf463. PMC 126276. PMID 12234934.
  20. ^ Kim JB, Yamaguchi Y, Wada T, Handa H, Sharp PA (September 1999). "Tat-SF1 protein associates with RAP30 and human SPT5 proteins". Mol. Cell. Biol. 19 (9): 5960–8. doi:10.1128/mcb.19.9.5960. PMC 84462. PMID 10454543.
  21. ^ Wada T, Takagi T, Yamaguchi Y, Ferdous A, Imai T, Hirose S, Sugimoto S, Yano K, Hartzog GA, Winston F, Buratowski S, Handa H (February 1998). "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs". Genes Dev. 12 (3): 343–56. doi:10.1101/gad.12.3.343. PMC 316480. PMID 9450929.
  22. ^ Conaway RC, Kong SE, Conaway JW (August 2003). "TFIIS and GreB: two like-minded transcription elongation factors with sticky fingers". Cell. 114 (3): 272–4. doi:10.1016/S0092-8674(03)00607-X. PMID 12914690. S2CID 14209300.
  23. ^ Archambault J, Pan G, Dahmus GK, Cartier M, Marshall N, Zhang S, Dahmus ME, Greenblatt J (October 1998). "FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO". J. Biol. Chem. 273 (42): 27593–601. doi:10.1074/jbc.273.42.27593. PMID 9765293.
  24. ^ Pan G, Aso T, Greenblatt J (September 1997). "Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activators". J. Biol. Chem. 272 (39): 24563–71. doi:10.1074/jbc.272.39.24563. PMID 9305922.
  25. ^ Carty SM, Goldstrohm AC, Suñé C, Garcia-Blanco MA, Greenleaf AL (August 2000). "Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9015–20. Bibcode:2000PNAS...97.9015C. doi:10.1073/pnas.160266597. PMC 16813. PMID 10908677.
  26. ^ Grondin B, Côté F, Bazinet M, Vincent M, Aubry M (October 1997). "Direct interaction of the KRAB/Cys2-His2 zinc finger protein ZNF74 with a hyperphosphorylated form of the RNA polymerase II largest subunit". J. Biol. Chem. 272 (44): 27877–85. doi:10.1074/jbc.272.44.27877. PMID 9346935.

Further reading edit

  • 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.
  • Szentirmay MN, Sawadogo M (2000). "Spatial organization of RNA polymerase II transcription in the nucleus". Nucleic Acids Res. 28 (10): 2019–25. doi:10.1093/nar/28.10.2019. PMC 105382. PMID 10773068.
  • 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.

January 01, 1970
polr2a, directed, polymerase, subunit, rpb1, also, known, rpb1, enzyme, that, encoded, gene, humans, available, structurespdbortholog, search, pdbe, rcsblist, codes2ghq, 2ght, 2lto, 3d9k, 3d9l, 3d9m, 3d9n, 3d9o, 3d9p, 4jxt, 5iy9, 5iya, 5iyc, 5iyb, 5iy7, 5iy8, . DNA directed RNA polymerase II subunit RPB1 also known as RPB1 is an enzyme that is encoded by the POLR2A gene in humans POLR2AAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes2GHQ 2GHT 2LTO 3D9K 3D9L 3D9M 3D9N 3D9O 3D9P 4JXT 5IY9 5IYA 5IYC 5IYB 5IY7 5IY8 5IYD 5IY6IdentifiersAliasesPOLR2A POLR2 POLRA RPB1 RPBh1 RPO2 RPOL2 RpIILS hRPB220 hsRPB1 polymerase RNA II subunit A RNA polymerase II subunit A NEDHIBExternal IDsOMIM 180660 MGI 98086 HomoloGene 721 GeneCards POLR2AEC number2 7 7 48Gene location Human Chr Chromosome 17 human 1 Band17p13 1Start7 484 366 bp 1 End7 514 616 bp 1 Gene location Mouse Chr Chromosome 11 mouse 2 Band11 B3 11 42 86 cMStart69 624 823 bp 2 End69 649 463 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed instromal cell of endometriumright uterine tubepituitary glandleft adrenal glandskin of abdomenanterior pituitaryvaginacanal of the cervixgastric mucosaminor salivary glandsTop expressed ininternal carotid arterytracheobronchial treeexternal carotid arterythymusmolarbloodmaxillary prominencetracheasomiteentorhinal cortexMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functiontransferase activity DNA binding nucleotidyltransferase activity RNA polymerase II activity metal ion binding RNA directed 5 3 RNA polymerase activity DNA directed 5 3 RNA polymerase activity protein binding ubiquitin protein ligase binding RNA binding protein C terminus binding promoter specific chromatin bindingCellular componentPrp19 complex nucleolus RNA polymerase II core complex nucleus nucleoplasm cytoplasmBiological processmRNA splicing via spliceosome regulation of transcription DNA templated somatic stem cell population maintenance DNA templated transcription termination transcription elongation from RNA polymerase II promoter 7 methylguanosine mRNA capping transcription by RNA polymerase II transcription RNA templated positive regulation of RNA splicing positive regulation of viral transcription transcription coupled nucleotide excision repair transcription initiation from RNA polymerase II promoter snRNA transcription by RNA polymerase II fibroblast growth factor receptor signaling pathway transcription DNA templated RNA metabolic process regulation of gene silencing by miRNASources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez543020020EnsemblENSG00000284832ENSG00000181222ENSMUSG00000005198UniProtP24928P08775RefSeq mRNA NM 000937NM 009089NM 001291068RefSeq protein NP 000928NP 001277997Location UCSC Chr 17 7 48 7 51 MbChr 11 69 62 69 65 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Interactions 3 References 4 Further readingFunction editThis gene encodes the largest subunit of RNA polymerase II the polymerase responsible for synthesizing messenger RNA in eukaryotes The product of this gene contains a carboxy terminal domain composed of heptapeptide repeats that are essential for polymerase activity These repeats contain serine and threonine residues that are phosphorylated in actively transcribing RNA polymerase In addition this subunit in combination with several other polymerase subunits forms the DNA binding domain of the polymerase a groove in which the DNA template is transcribed into RNA 5 Interactions editPOLR2A has been shown to interact with BRCA1 6 7 8 9 CREBBP 10 CTDP1 7 CDK8 10 GTF2B 7 GTF2F1 7 10 GTF2H4 7 MED21 7 10 11 MED26 12 PCAF 10 POLR2C 13 POLR2E 13 POLR2H 13 POLR2L 13 PQBP1 14 SMARCA2 10 15 16 SMARCA4 15 16 17 SMARCB1 10 15 16 SMYD3 18 SND1 19 SUPT5H 20 21 TAF11 7 TBP 7 TCEA1 22 23 24 TCERG1 25 and ZNF74 26 References edit a b c ENSG00000181222 GRCh38 Ensembl release 89 ENSG00000284832 ENSG00000181222 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000005198 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 POLR2A polymerase RNA II DNA directed polypeptide A 220kDa Krum SA Miranda GA Lin C Lane TF December 2003 BRCA1 associates with processive RNA polymerase II J Biol Chem 278 52 52012 20 doi 10 1074 jbc M308418200 PMID 14506230 a b c d e f g h Scully R Anderson SF Chao DM Wei W Ye L Young RA Livingston DM Parvin JD May 1997 BRCA1 is a component of the RNA polymerase II holoenzyme Proc Natl Acad Sci U S A 94 11 5605 10 Bibcode 1997PNAS 94 5605S doi 10 1073 pnas 94 11 5605 PMC 20825 PMID 9159119 Chiba N Parvin JD October 2001 Redistribution of BRCA1 among four different protein complexes following replication blockage J Biol Chem 276 42 38549 54 doi 10 1074 jbc M105227200 PMID 11504724 Krum SA Womack JE Lane TF September 2003 Bovine BRCA1 shows classic responses to genotoxic stress but low in vitro transcriptional activation activity Oncogene 22 38 6032 44 doi 10 1038 sj onc 1206515 PMID 12955082 a b c d e f g Cho H Orphanides G Sun X Yang XJ Ogryzko V Lees E Nakatani Y Reinberg D September 1998 A human RNA polymerase II complex containing factors that modify chromatin structure Mol Cell Biol 18 9 5355 63 doi 10 1128 MCB 18 9 5355 PMC 109120 PMID 9710619 Sune C Hayashi T Liu Y Lane WS Young RA Garcia Blanco MA October 1997 CA150 a nuclear protein associated with the RNA polymerase II holoenzyme is involved in Tat activated human immunodeficiency virus type 1 transcription Mol Cell Biol 17 10 6029 39 doi 10 1128 MCB 17 10 6029 PMC 232452 PMID 9315662 Sato S Tomomori Sato C Parmely TJ Florens L Zybailov B Swanson SK Banks CA Jin J Cai Y Washburn MP Conaway JW Conaway RC June 2004 A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology Mol Cell 14 5 685 91 doi 10 1016 j molcel 2004 05 006 PMID 15175163 a b c d 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 Humbert S Saudou F May 2002 Toward cell specificity in SCA1 Neuron 34 5 669 70 doi 10 1016 s0896 6273 02 00715 8 PMID 12062012 S2CID 15993809 a b c Sif S Saurin AJ Imbalzano AN Kingston RE March 2001 Purification and characterization of mSin3A containing Brg1 and hBrm chromatin remodeling complexes Genes Dev 15 5 603 18 doi 10 1101 gad 872801 PMC 312641 PMID 11238380 a b c Wang W Cote J Xue Y Zhou S Khavari PA Biggar SR Muchardt C Kalpana GV Goff SP Yaniv M Workman JL Crabtree GR October 1996 Purification and biochemical heterogeneity of the mammalian SWI SNF complex EMBO J 15 19 5370 82 doi 10 1002 j 1460 2075 1996 tb00921 x PMC 452280 PMID 8895581 Zhao K Wang W Rando OJ Xue Y Swiderek K Kuo A Crabtree GR November 1998 Rapid and phosphoinositol dependent binding of the SWI SNF like BAF complex to chromatin after T lymphocyte receptor signaling Cell 95 5 625 36 doi 10 1016 s0092 8674 00 81633 5 PMID 9845365 S2CID 3184211 Hamamoto R Furukawa Y Morita M Iimura Y Silva FP Li M Yagyu R Nakamura Y August 2004 SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells Nat Cell Biol 6 8 731 40 doi 10 1038 ncb1151 PMID 15235609 S2CID 13456531 Yang J Aittomaki S Pesu M Carter K Saarinen J Kalkkinen N Kieff E Silvennoinen O September 2002 Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II EMBO J 21 18 4950 8 doi 10 1093 emboj cdf463 PMC 126276 PMID 12234934 Kim JB Yamaguchi Y Wada T Handa H Sharp PA September 1999 Tat SF1 protein associates with RAP30 and human SPT5 proteins Mol Cell Biol 19 9 5960 8 doi 10 1128 mcb 19 9 5960 PMC 84462 PMID 10454543 Wada T Takagi T Yamaguchi Y Ferdous A Imai T Hirose S Sugimoto S Yano K Hartzog GA Winston F Buratowski S Handa H February 1998 DSIF a novel transcription elongation factor that regulates RNA polymerase II processivity is composed of human Spt4 and Spt5 homologs Genes Dev 12 3 343 56 doi 10 1101 gad 12 3 343 PMC 316480 PMID 9450929 Conaway RC Kong SE Conaway JW August 2003 TFIIS and GreB two like minded transcription elongation factors with sticky fingers Cell 114 3 272 4 doi 10 1016 S0092 8674 03 00607 X PMID 12914690 S2CID 14209300 Archambault J Pan G Dahmus GK Cartier M Marshall N Zhang S Dahmus ME Greenblatt J October 1998 FCP1 the RAP74 interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl terminal domain of RNA polymerase IIO J Biol Chem 273 42 27593 601 doi 10 1074 jbc 273 42 27593 PMID 9765293 Pan G Aso T Greenblatt J September 1997 Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter specific initiation and responsive to transcriptional activators J Biol Chem 272 39 24563 71 doi 10 1074 jbc 272 39 24563 PMID 9305922 Carty SM Goldstrohm AC Sune C Garcia Blanco MA Greenleaf AL August 2000 Protein interaction modules that organize nuclear function FF domains of CA150 bind the phosphoCTD of RNA polymerase II Proc Natl Acad Sci U S A 97 16 9015 20 Bibcode 2000PNAS 97 9015C doi 10 1073 pnas 160266597 PMC 16813 PMID 10908677 Grondin B Cote F Bazinet M Vincent M Aubry M October 1997 Direct interaction of the KRAB Cys2 His2 zinc finger protein ZNF74 with a hyperphosphorylated form of the RNA polymerase II largest subunit J Biol Chem 272 44 27877 85 doi 10 1074 jbc 272 44 27877 PMID 9346935 Further reading editJeang 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 lt 357 AID JCB1 gt 3 0 CO 2 K PMID 10536359 S2CID 43685090 Szentirmay MN Sawadogo M 2000 Spatial organization of RNA polymerase II transcription in the nucleus Nucleic Acids Res 28 10 2019 25 doi 10 1093 nar 28 10 2019 PMC 105382 PMID 10773068 Marcello A Zoppe 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 Retrieved from https en wikipedia org w index php title POLR2A amp oldid 1218107828, wikipedia, wiki, book, books, library,

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