Biology:RBPJ

From HandWiki
Revision as of 00:34, 12 February 2024 by Steve Marsio (talk | contribs) (update)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Recombination signal binding protein for immunoglobulin kappa J region is a protein that in humans is encoded by the RBPJ gene.[1][2][3]

RBPJ[4] also known as CBF1, is the human homolog for the Drosophila gene Suppressor of Hairless. Its promoter region is classically used to demonstrate Notch1 signaling.[5]

Interactions

RBPJ has been shown to interact with:

References

  1. "Human Jk recombination signal binding protein gene (IGKJRB): comparison with its mouse homologue". Genomics 17 (2): 306–315. August 1993. doi:10.1006/geno.1993.1326. PMID 8406481. 
  2. "Assignment of the human gene for KBF2/RBP-Jk to chromosome 9p12-13 and 9q13 by fluorescence in situ hybridization". The Japanese Journal of Human Genetics 42 (2): 337–341. June 1997. doi:10.1007/BF02766956. PMID 9290259. 
  3. "NCBI Gene: RBPJ recombination signal binding protein for immunoglobulin kappa J region". https://www.ncbi.nlm.nih.gov/gene/3516. 
  4. "HGNC: RBPJ Symbol Report". https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/5724. 
  5. "Truncated mammalian Notch1 activates CBF1/RBPJk-repressed genes by a mechanism resembling that of Epstein-Barr virus EBNA2". Molecular and Cellular Biology 16 (3): 952–959. March 1996. doi:10.1128/mcb.16.3.952. PMID 8622698. 
  6. "Structural requirements for assembly of the CSL.intracellular Notch1.Mastermind-like 1 transcriptional activation complex". The Journal of Biological Chemistry 278 (23): 21232–21239. June 2003. doi:10.1074/jbc.M301567200. PMID 12644465. 
  7. "Oncogenic forms of NOTCH1 lacking either the primary binding site for RBP-Jkappa or nuclear localization sequences retain the ability to associate with RBP-Jkappa and activate transcription". The Journal of Biological Chemistry 272 (17): 11336–11343. April 1997. doi:10.1074/jbc.272.17.11336. PMID 9111040. 
  8. "The origin of the ankyrin repeat region in Notch intracellular domains is critical for regulation of HES promoter activity". Mechanisms of Development 104 (1–2): 3–20. June 2001. doi:10.1016/s0925-4773(01)00373-2. PMID 11404076. 
  9. "Nuclear localization of CBF1 is regulated by interactions with the SMRT corepressor complex". Molecular and Cellular Biology 21 (18): 6222–6232. September 2001. doi:10.1128/mcb.21.18.6222-6232.2001. PMID 11509665. 
  10. "Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5". The Journal of Biological Chemistry 275 (22): 17211–17220. June 2000. doi:10.1074/jbc.M000909200. PMID 10747963. 
  11. 11.0 11.1 "A role for SKIP in EBNA2 activation of CBF1-repressed promoters". Journal of Virology 74 (4): 1939–1947. February 2000. doi:10.1128/jvi.74.4.1939-1947.2000. PMID 10644367. 
  12. "CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex". Proceedings of the National Academy of Sciences of the United States of America 96 (1): 23–28. January 1999. doi:10.1073/pnas.96.1.23. PMID 9874765. Bibcode1999PNAS...96...23H. 
  13. "SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function". Molecular and Cellular Biology 20 (7): 2400–2410. April 2000. doi:10.1128/mcb.20.7.2400-2410.2000. PMID 10713164. 
  14. "R-propranolol is a small molecule inhibitor of the SOX18 transcription factor in a rare vascular syndrome and hemangioma". eLife 8: e43026. July 2019. doi:10.7554/eLife.43026. PMID 31358114. 
  15. "Notch-independent RBPJ controls angiogenesis in the adult heart". Nature Communications 7 (1): 12088. June 2016. doi:10.1038/ncomms12088. PMID 27357444. Bibcode2016NatCo...712088D. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.