RBBP6

RBBP6
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2C7H, 2YSA, 2YUR, 3ZTG
Identifiers
Aliases	RBBP6, MY038, P2P-R, PACT, RBQ-1, SNAMA, retinoblastoma binding protein 6, RB binding protein 6, ubiquitin ligase
External IDs	OMIM: 600938; MGI: 894835; HomoloGene: 136812; GeneCards: RBBP6; OMA:RBBP6 - orthologs
Gene location (Human)
Chr.	Chromosome 16 (human)
End	24,572,863 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	122,601,780 bp
RNA expression pattern
	Top expressed in
	buccal mucosa cell; ; sperm; ; gastric mucosa; ; left ovary; ; mucosa of paranasal sinus; ; right ovary; ; right uterine tube; ; left testis; ; right testis; ; skin of abdomen;
	Top expressed in
	tail of embryo; ; genital tubercle; ; medullary collecting duct; ; neural layer of retina; ; ventricular zone; ; Ileal epithelium; ; thymus; ; spermatid; ; plantaris muscle; ; renal corpuscle;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	protein binding; zinc ion binding; nucleic acid binding; metal ion binding; ubiquitin-protein transferase activity; ubiquitin protein ligase activity; transferase activity; RNA binding; protein kinase binding;
Cellular component	nucleolus; microtubule organizing center; nucleus; chromosome; cytoplasm; cytoskeleton; cytosol; centrosome; nuclear speck; protein-containing complex;
Biological process	in utero embryonic development; embryonic organ development; regulation of DNA replication; DNA replication; cellular response to DNA damage stimulus; protein ubiquitination; multicellular organism growth; somite development; mRNA processing; protein polyubiquitination; ubiquitin-dependent protein catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	5930
	19647
	ENSG00000122257
	ENSMUSG00000030779
	Q7Z6E9
	P97868
	NM_006910; NM_018703; NM_032626
	NM_011247; NM_175023
	NP_008841; NP_061173; NP_116015
	NP_035377; NP_778188; NP_001390011; NP_001390012
	Wikidata
View/Edit Human	View/Edit Mouse

Retinoblastoma-binding protein 6 is a protein that in humans is encoded by the RBBP6 gene.⁵⁶⁷

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.⁷

Interactions

RBBP6 has been shown to interact with Y box binding protein 1.⁸

References

GRCh38: Ensembl release 89: ENSG00000122257 – Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000030779 – Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
"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. S2CID 25240477.
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. Bibcode:2004PNAS..10112130B. 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. S2CID 24888360.
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. S2CID 14294292.
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. S2CID 7827573.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000122257 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000030779 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8595913-5] 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.

[pmid16396680-6] 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.

[entrez-7] "Entrez Gene: RBBP6 retinoblastoma binding protein 6".

[pmid18851979-8] 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.

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