POLR2A

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Protein-coding gene in the species Homo sapiens

title: "POLR2A" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/POLR2A" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

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

Function

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.

Interactions

POLR2A has been shown to interact with:

References

References

  1. "Entrez Gene: POLR2A polymerase (RNA) II (DNA directed) polypeptide A, 220kDa".
  2. (December 2003). "BRCA1 associates with processive RNA polymerase II". J. Biol. Chem..
  3. (May 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A..
  4. (October 2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage". J. Biol. Chem..
  5. (September 2003). "Bovine BRCA1 shows classic responses to genotoxic stress but low in vitro transcriptional activation activity". Oncogene.
  6. (September 1998). "A human RNA polymerase II complex containing factors that modify chromatin structure". Mol. Cell. Biol..
  7. (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..
  8. (June 2004). "A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology". Mol. Cell.
  9. (July 1997). "Interactions between the human RNA polymerase II subunits". J. Biol. Chem..
  10. (May 2002). "Toward cell specificity in SCA1". Neuron.
  11. (March 2001). "Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes". Genes Dev..
  12. (October 1996). "Purification and biochemical heterogeneity of the mammalian SWI-SNF complex". EMBO J..
  13. (November 1998). "Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling". Cell.
  14. (August 2004). "SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells". Nat. Cell Biol..
  15. (September 2002). "Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II". EMBO J..
  16. (September 1999). "Tat-SF1 protein associates with RAP30 and human SPT5 proteins". Mol. Cell. Biol..
  17. (February 1998). "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs". Genes Dev..
  18. (August 2003). "TFIIS and GreB: two like-minded transcription elongation factors with sticky fingers". Cell.
  19. (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..
  20. (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..
  21. (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..
  22. (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..

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