Biology:RBBP5
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 Generic protein structure example |
Retinoblastoma-binding protein 5 is a protein that in humans is encoded by the RBBP5 gene.[1][2]
Function
The protein encoded by this gene is a ubiquitously expressed nuclear protein and belongs to a highly conserved subfamily of WD-repeat proteins. It is found among several proteins that bind directly to retinoblastoma protein, which regulates cell proliferation. The encoded protein interacts preferentially with the underphosphorylated retinoblastoma protein via the E1A-binding pocket B.[2]
Interactions
RBBP5 has been shown to interact with:
References
- ↑ "Molecular cloning of a human protein that binds to the retinoblastoma protein and chromosomal mapping". Genomics 27 (3): 511–9. Jun 1995. doi:10.1006/geno.1995.1084. PMID 7558034.
- ↑ 2.0 2.1 "Entrez Gene: RBBP5 retinoblastoma binding protein 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5929.
- ↑ 3.0 3.1 3.2 "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Molecular and Cellular Biology 23 (1): 140–9. Jan 2003. doi:10.1128/mcb.23.1.140-149.2003. PMID 12482968.
- ↑ "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Molecular and Cellular Biology 24 (13): 5639–49. Jul 2004. doi:10.1128/MCB.24.13.5639-5649.2004. PMID 15199122.
Further reading
- "Generation and analysis of 280,000 human expressed sequence tags". Genome Research 6 (9): 807–28. Sep 1996. doi:10.1101/gr.6.9.807. PMID 8889549.
- "Identification and characterization of the potential promoter regions of 1031 kinds of human genes". Genome Research 11 (5): 677–84. May 2001. doi:10.1101/gr.gr-1640r. PMID 11337467.
- "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Molecular and Cellular Biology 23 (1): 140–9. Jan 2003. doi:10.1128/MCB.23.1.140-149.2003. PMID 12482968.
- "Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus". Molecular Cell 13 (4): 587–97. Feb 2004. doi:10.1016/S1097-2765(04)00081-4. PMID 14992727.
- "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Molecular and Cellular Biology 24 (13): 5639–49. Jul 2004. doi:10.1128/MCB.24.13.5639-5649.2004. PMID 15199122.
- "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF". Cell 121 (6): 873–85. Jun 2005. doi:10.1016/j.cell.2005.04.031. PMID 15960975.
- "Genome-wide analysis of menin binding provides insights into MEN1 tumorigenesis". PLOS Genetics 2 (4): e51. Apr 2006. doi:10.1371/journal.pgen.0020051. PMID 16604156.
- "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation". Nature Cell Biology 8 (11): 1277–83. Nov 2006. doi:10.1038/ncb1490. PMID 17041588.
- "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. Nov 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
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