POLR2A

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POLR2A
Protein POLR2A PDB 2GHQ.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases POLR2A, POLR2, POLRA, RPB1, RPBh1, RPO2, RPOL2, RpIILS, hRPB220, hsRPB1, polymerase (RNA) II subunit A
External IDs OMIM: 180660 MGI: 98086 HomoloGene: 721 GeneCards: POLR2A
EC number 2.7.7.48
RNA expression pattern
PBB GE POLR2A 202725 at fs.png

PBB GE POLR2A 217420 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000937

NM_009089
NM_001291068

RefSeq (protein)

NP_000928

NP_001277997.1
NP_001277997

Location (UCSC) Chr 17: 7.48 – 7.51 Mb Chr 11: 69.73 – 69.76 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

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

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.[3]

Interactions[edit]

POLR2A has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ "Entrez Gene: POLR2A polymerase (RNA) II (DNA directed) polypeptide A, 220kDa". 
  4. ^ 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. 
  5. ^ 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. doi:10.1073/pnas.94.11.5605. PMC 20825Freely accessible. PMID 9159119. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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. PMC 109120Freely accessible. PMID 9710619. 
  9. ^ 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. PMC 232452Freely accessible. PMID 9315662. 
  10. ^ 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. 
  11. ^ 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. 
  12. ^ 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. 
  13. ^ 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 312641Freely accessible. PMID 11238380. 
  14. ^ 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. PMC 452280Freely accessible. PMID 8895581. 
  15. ^ 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. 
  16. ^ 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. 
  17. ^ 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 126276Freely accessible. PMID 12234934. 
  18. ^ 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 84462Freely accessible. PMID 10454543. 
  19. ^ 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 316480Freely accessible. PMID 9450929. 
  20. ^ 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. 
  21. ^ 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. 
  22. ^ 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. 
  23. ^ 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. doi:10.1073/pnas.160266597. PMC 16813Freely accessible. PMID 10908677. 
  24. ^ 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]