RBBP6: Difference between revisions
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{{ | '''Retinoblastoma-binding protein 6''' is a [[protein]] that in humans is encoded by the ''RBBP6'' [[gene]].<ref name="pmid8595913">{{cite journal | vauthors = Sakai Y, Saijo M, Coelho K, Kishino T, Niikawa N, Taya Y | title = cDNA sequence and chromosomal localization of a novel human protein, RBQ-1 (RBBP6), that binds to the retinoblastoma gene product | journal = Genomics | volume = 30 | issue = 1 | pages = 98–101 | date = Nov 1995 | pmid = 8595913 | pmc = | doi = 10.1006/geno.1995.0017 }}</ref><ref name="pmid16396680">{{cite journal | vauthors = Pugh DJ, Ab E, Faro A, Lutya PT, Hoffmann E, Rees DJ | title = DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways | journal = BMC Structural Biology | volume = 6 | pages = 1 | date = Feb 2006 | pmid = 16396680 | pmc = 1360078 | doi = 10.1186/1472-6807-6-1 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RBBP6 retinoblastoma binding protein 6| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5930| accessdate = }}</ref> | ||
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== Function == | |||
The retinoblastoma tumor suppressor (pRB) protein binds with many other proteins. In various human cancers, pRB suppresses cellular proliferation and is inactivated. Cell cycle-dependent phosphorylation regulates the activity of pRB. This gene encodes a protein which binds to underphosphorylated but not phosphorylated pRB. Multiple alternatively spliced transcript variants that encode different isoforms have been found for this gene.<ref name="entrez" /> | |||
==References== | == Interactions == | ||
{{reflist | |||
==Further reading== | RBBP6 has been shown to [[Protein-protein_interaction|interact]] with [[Y box binding protein 1]].<ref name=pmid18851979>{{cite journal | vauthors = Chibi M, Meyer M, Skepu A, G Rees DJ, Moolman-Smook JC, Pugh DJ | title = RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1 | journal = Journal of Molecular Biology | volume = 384 | issue = 4 | pages = 908–16 | date = Dec 2008 | pmid = 18851979 | doi = 10.1016/j.jmb.2008.09.060 }}</ref> | ||
== References == | |||
{{reflist}} | |||
== Further reading == | |||
{{refbegin | 2}} | {{refbegin | 2}} | ||
* {{cite journal | vauthors = Simons A, Melamed-Bessudo C, Wolkowicz R, Sperling J, Sperling R, Eisenbach L, Rotter V | title = PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb | journal = Oncogene | volume = 14 | issue = 2 | pages = 145–55 | date = Jan 1997 | pmid = 9010216 | doi = 10.1038/sj.onc.1200825 }} | |||
* {{cite journal | vauthors = Gao S, Witte MM, Scott RE | title = P2P-R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P-R immunoreactivity | journal = Journal of Cellular Physiology | volume = 191 | issue = 2 | pages = 145–54 | date = May 2002 | pmid = 12064457 | doi = 10.1002/jcp.10084 }} | |||
* {{cite journal | vauthors = Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM | title = Functional proteomics mapping of a human signaling pathway | journal = Genome Research | volume = 14 | issue = 7 | pages = 1324–32 | date = Jul 2004 | pmid = 15231748 | pmc = 442148 | doi = 10.1101/gr.2334104 }} | |||
*{{cite journal | * {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }} | ||
*{{cite journal | * {{cite journal | vauthors = Yoshitake Y, Nakatsura T, Monji M, Senju S, Matsuyoshi H, Tsukamoto H, Hosaka S, Komori H, Fukuma D, Ikuta Y, Katagiri T, Furukawa Y, Ito H, Shinohara M, Nakamura Y, Nishimura Y | title = Proliferation potential-related protein, an ideal esophageal cancer antigen for immunotherapy, identified using complementary DNA microarray analysis | journal = Clinical Cancer Research | volume = 10 | issue = 19 | pages = 6437–48 | date = Oct 2004 | pmid = 15475430 | doi = 10.1158/1078-0432.CCR-04-0841 }} | ||
*{{cite journal | * {{cite journal | vauthors = Scott RE, White-Grindley E, Ruley HE, Chesler EJ, Williams RW | title = P2P-R expression is genetically coregulated with components of the translation machinery and with PUM2, a translational repressor that associates with the P2P-R mRNA | journal = Journal of Cellular Physiology | volume = 204 | issue = 1 | pages = 99–105 | date = Jul 2005 | pmid = 15617101 | doi = 10.1002/jcp.20263 }} | ||
* {{cite journal | vauthors = Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP | title = A probability-based approach for high-throughput protein phosphorylation analysis and site localization | journal = Nature Biotechnology | volume = 24 | issue = 10 | pages = 1285–92 | date = Oct 2006 | pmid = 16964243 | doi = 10.1038/nbt1240 }} | |||
* {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = Nov 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 }} | |||
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{{refend}} | {{refend}} | ||
{{ | {{PDB Gallery|geneid=5930}} | ||
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{{gene-16-stub}} |
Latest revision as of 08:57, 10 September 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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Retinoblastoma-binding protein 6 is a protein that in humans is encoded by the RBBP6 gene.[1][2][3]
Function
The retinoblastoma tumor suppressor (pRB) protein binds with many other proteins. In various human cancers, pRB suppresses cellular proliferation and is inactivated. Cell cycle-dependent phosphorylation regulates the activity of pRB. This gene encodes a protein which binds to underphosphorylated but not phosphorylated pRB. Multiple alternatively spliced transcript variants that encode different isoforms have been found for this gene.[3]
Interactions
RBBP6 has been shown to interact with Y box binding protein 1.[4]
References
- ↑ Sakai Y, Saijo M, Coelho K, Kishino T, Niikawa N, Taya Y (Nov 1995). "cDNA sequence and chromosomal localization of a novel human protein, RBQ-1 (RBBP6), that binds to the retinoblastoma gene product". Genomics. 30 (1): 98–101. doi:10.1006/geno.1995.0017. PMID 8595913.
- ↑ Pugh DJ, Ab E, Faro A, Lutya PT, Hoffmann E, Rees DJ (Feb 2006). "DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways". BMC Structural Biology. 6: 1. doi:10.1186/1472-6807-6-1. PMC 1360078. PMID 16396680.
- ↑ 3.0 3.1 "Entrez Gene: RBBP6 retinoblastoma binding protein 6".
- ↑ Chibi M, Meyer M, Skepu A, G Rees DJ, Moolman-Smook JC, Pugh DJ (Dec 2008). "RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1". Journal of Molecular Biology. 384 (4): 908–16. doi:10.1016/j.jmb.2008.09.060. PMID 18851979.
Further reading
- Simons A, Melamed-Bessudo C, Wolkowicz R, Sperling J, Sperling R, Eisenbach L, Rotter V (Jan 1997). "PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb". Oncogene. 14 (2): 145–55. doi:10.1038/sj.onc.1200825. PMID 9010216.
- Gao S, Witte MM, Scott RE (May 2002). "P2P-R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P-R immunoreactivity". Journal of Cellular Physiology. 191 (2): 145–54. doi:10.1002/jcp.10084. PMID 12064457.
- Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- Yoshitake Y, Nakatsura T, Monji M, Senju S, Matsuyoshi H, Tsukamoto H, Hosaka S, Komori H, Fukuma D, Ikuta Y, Katagiri T, Furukawa Y, Ito H, Shinohara M, Nakamura Y, Nishimura Y (Oct 2004). "Proliferation potential-related protein, an ideal esophageal cancer antigen for immunotherapy, identified using complementary DNA microarray analysis". Clinical Cancer Research. 10 (19): 6437–48. doi:10.1158/1078-0432.CCR-04-0841. PMID 15475430.
- Scott RE, White-Grindley E, Ruley HE, Chesler EJ, Williams RW (Jul 2005). "P2P-R expression is genetically coregulated with components of the translation machinery and with PUM2, a translational repressor that associates with the P2P-R mRNA". Journal of Cellular Physiology. 204 (1): 99–105. doi:10.1002/jcp.20263. PMID 15617101.
- Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (Oct 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
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